The identification of specific protein kinases as oncogenic drivers in a variety of cancer sorts, coupled with the clinical success of particular kinase-directed targeted therapies, has cemented the human kinome as an attractive source of 'actionable' targets for cancer remedy. However, 'mining' of the human kinome for precision oncology applications has yet to yield its full potential. This reflects a variety of points, including oncogenic kinase dysregulation at levels not detectable by genomic sequencing and the uncharacterized nature of a considerable fraction of the kinome. In addition, selective therapeutic targeting of specific kinases requires efficient mapping of total kinome space impacted by candidate small molecule medication. Fortunately, recent developments in proteomics strategies, particularly in mass spectrometry-based phosphoproteomics and kinomics, provide the necessary technology platforms to address these impediments. Moreover, initiatives such as the Clinical Proteomic Tumour Analysis Consortium have enabled the era, deposition and integration of genomic, transcriptomic and (phospho)proteomic data for many cancer sorts, providing unprecedented insights into oncogenic kinases and cancer cell signalling typically. These multi-omic data are identifying novel therapeutic targets, highlighting opportunities for drug re-purposing, and helping assign optimal therapies to specific tumour subtypes, heralding a new era of 'enhanced' precision oncology. This article is protected by copyright. All rights reserved.
by: Hugh DixonPosted on:

Human pores and skin is composed of the cell-rich dermis, the extracellular matrix (ECM) wealthy dermis, and the hypodermis.

Within the dermis, a dense community of ECM proteins offers structural assist to the pores and skin and regulates a large variety of signaling pathways which govern cell proliferation and different crucial processes. Both intrinsic ageing, which happens steadily over time, and extrinsic ageing (photoaging), which happens as a consequence of exterior insults such as photo voltaic radiation, trigger alterations to the dermal ECM. In this examine, we utilized each quantitative and world proteomics, alongside single harmonic era (SHG) and two-photon autofluorescence (TPAF) imaging, to assess modifications in dermal composition throughout intrinsic and extrinsic ageing.

We discover that each intrinsic and extrinsic ageing consequence in important decreases in ECM-supporting proteoglycans and structural ECM integrity, evidenced by reducing collagen abundance and rising fibril fragmentation. Intrinsic ageing additionally produces modifications distinct from these produced by photoaging, including reductions in elastic fiber and crosslinking enzyme abundance. In distinction, photoaging is primarily outlined by will increase in elastic fiber-associated protein and pro-inflammatory proteases. Network evaluation steered that AM and Bk have been accountable for PHN preliminary assault, whereas Inq, B, T and Bc-h would degrade PHN metabolites.

Changes related with photoaging are evident even in younger (mid 20s) sun-exposed forearm pores and skin, indicating that proteomic proof of photoaging is current many years prior to clinical indicators of photoaging. GO time period enrichment revealed that each intrinsic ageing and photoaging share widespread options of persistent irritation. The proteomic data has been deposited to the ProteomeXchange Consortium by way of the PRIDE associate repository with the data set identifier PXD015982.

Quantitative proteomic profiling of extracellular matrix and site-specific collagen post-translational modifications in an in vitro mannequin of lung fibrosis

Lung fibrosis is characterised by extreme deposition of extracellular matrix (ECM), in particular collagens, by fibroblasts in the interstitium. Transforming development factor-β1 (TGF-β1) alters the expression of many extracellular matrix (ECM) elements produced by fibroblasts, however such modifications in ECM composition as effectively as modulation of collagen post-translational modification (PTM) levels have not been comprehensively investigated. Here, we carried out mass spectrometry (MS)-based proteomics analyses to assess modifications in the ECM deposited by cultured lung fibroblasts from idiopathic pulmonary fibrosis (IPF) sufferers upon stimulation with remodeling development issue β1 (TGF-β1).

In addition to the ECM modifications generally related with lung fibrosis, MS-based label-free quantification revealed profound results on enzymes concerned in ECM crosslinking and turnover as effectively as a number of constructive and unfavorable suggestions mechanisms of TGF-β1 signaling. Notably, the ECM modifications noticed in this in vitro mannequin correlated considerably with ECM modifications noticed in affected person samples. Because collagens are topic to a number of PTMs with main implications in illness, we carried out a new bioinformatic platform to analyze MS data that enables for the complete mapping and site-specific quantitation of collagen PTMs in crude ECM preparations.

These analyses yielded a complete map of prolyl and lysyl hydroxylations as effectively as lysyl glycosylations for 15 collagen chains. In addition, site-specific PTM evaluation revealed novel websites of prolyl-3-hydroxylation and lysyl glycosylation in sort I collagen. Interestingly, the outcomes present, for the first time, that TGF-β1 can modulate prolyl-3-hydroxylation and glycosylation in a site-specific method. Taken collectively, this proof of idea examine not solely reveals unanticipated TGF-β1 mediated regulation of collagen PTMs and different ECM elements but additionally lays the basis for dissecting their key roles in well being and illness.

The identification of specific protein kinases as oncogenic drivers in a variety of cancer sorts, coupled with the clinical success of particular kinase-directed targeted therapies, has cemented the human kinome as an attractive source of 'actionable' targets for cancer remedy. However, 'mining' of the human kinome for precision oncology applications has yet to yield its full potential. This reflects a variety of points, including oncogenic kinase dysregulation at levels not detectable by genomic sequencing and the uncharacterized nature of a considerable fraction of the kinome. In addition, selective therapeutic targeting of specific kinases requires efficient mapping of total kinome space impacted by candidate small molecule medication. Fortunately, recent developments in proteomics strategies, particularly in mass spectrometry-based phosphoproteomics and kinomics, provide the necessary technology platforms to address these impediments. Moreover, initiatives such as the Clinical Proteomic Tumour Analysis Consortium have enabled the era, deposition and integration of genomic, transcriptomic and (phospho)proteomic data for many cancer sorts, providing unprecedented insights into oncogenic kinases and cancer cell signalling typically. These multi-omic data are identifying novel therapeutic targets, highlighting opportunities for drug re-purposing, and helping assign optimal therapies to specific tumour subtypes, heralding a new era of 'enhanced' precision oncology. This article is protected by copyright. All rights reserved.

Time-resolved Analysis of the Matrix Metalloproteinase 10 Substrate Degradome

Proteolysis is an irreversible post-translational modification that impacts intra- and intercellular communication by modulating the exercise of bioactive mediators. Key to understanding protease operate is the system-wide identification of cleavage occasions and their dynamics in physiological contexts. Despite recent advances in mass spectrometry-based proteomics for high-throughput substrate screening, present approaches endure from excessive false constructive charges and solely seize single states of protease exercise. Here, we current a workflow primarily based on multiplexed terminal amine isotopic labeling of substrates for time-resolved substrate degradomics in complicated proteomes.

This method considerably enhances confidence in substrate identification and categorizes cleavage occasions by specificity and structural accessibility of the cleavage web site. We reveal concomitant quantification of cleavage web site spanning peptides and neo-N and/or neo-C termini to estimate relative ratios of noncleaved and cleaved varieties of substrate proteins. By making use of this technique to dissect the matrix metalloproteinase 10 (MMP10) substrate degradome in fibroblast secretomes, we recognized the extracellular matrix protein ADAMTS-like protein 1 (ADAMTSL1) as a direct MMP10 substrate and revealed MMP10-dependent ectodomain shedding of platelet-derived development issue receptor alpha (PDGFRα) as effectively as sequential processing of sort I collagen.

Mouse anti Podoplanin-Biotin (human)
101-MBi40 50ug
EUR 297.6

Hamster anti Podoplanin-Biotin (mouse)
103-MBi40 50ug
EUR 297.6

Anti-Mouse Podoplanin Antibody
103-M552 100 µg
EUR 399
Description: Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. The ECD contains abundant Ser/Thr residues as potential sites for Oglycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation. Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and on numerous tumors including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Mouse Podoplanin Antibody
103-PA40 200 µg
EUR 204.75
Description: Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. The ECD contains abundant Ser/Thr residues as potential sites for Oglycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation. Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and on numerous tumors including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Mouse Podoplanin Antibody
103-PA40S 100 µg
EUR 126
Description: Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. The ECD contains abundant Ser/Thr residues as potential sites for Oglycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation. Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and on numerous tumors including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Mouse Podoplanin ELISA kit
E01A24381 96T
EUR 700
Description: ELISA

Mouse Podoplanin ELISA kit
E03P0082-192T 192 tests
EUR 1524
Description: A sandwich ELISA for quantitative measurement of Mouse Podoplanin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Mouse Podoplanin ELISA kit
E03P0082-48 1 plate of 48 wells
EUR 624
Description: A sandwich ELISA for quantitative measurement of Mouse Podoplanin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Mouse Podoplanin ELISA kit
E03P0082-96 1 plate of 96 wells
EUR 822
Description: A sandwich ELISA for quantitative measurement of Mouse Podoplanin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Mouse Podoplanin ELISA Kit
IMSPDPNKT each
EUR 752
Description: Mouse Podoplanin ELISA Kit

anti- Podoplanin antibody
FNab06598 100µg
EUR 702
Description: Antibody raised against Podoplanin

anti- Podoplanin antibody
FNab06599 100µg
EUR 702
Description: Antibody raised against Podoplanin

Mouse Monoclonal anti-Rat Podoplanin Antibody
xAP-0897 100ug
EUR 280

Mouse Podoplanin (PDPN) Protein
20-abx650139
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  • Ask for price
  • Ask for price
  • 100 ug
  • 10 ug
  • 1 mg
  • 200 ug
  • 50 ug

Mouse Podoplanin (PDPN) Protein
abx694266-10nmol 10 nmol
EUR 700

Mouse Podoplanin (PDPN) Protein
abx694266-5nmol 5 nmol
EUR 462.5

Mouse Podoplanin (PDPN) Protein
abx650139-100g 100 µg
EUR 537.5

Mouse Podoplanin (PDPN) Protein
abx650139-10g 10 µg
EUR 212.5

Mouse Podoplanin (PDPN) Protein
abx650139-50g 50 µg
EUR 375

Mouse Monoclonal Podoplanin Antibody
TA327727 1 ml Ask for price

Mouse Podoplanin (PDPN) CLIA Kit
20-abx493858
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  • 10 × 96 tests
  • 5 × 96 tests
  • 96 tests

Mouse Podoplanin (PDPN) ELISA Kit
DLR-PDPN-Mu 96T
EUR 475
Description: tissue homogenates, cell lysates or other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
DLR-PDPN-Mu-48T 48T
EUR 632.4
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Podoplanin (PDPN) in samples from tissue homogenates, cell lysates or other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
DLR-PDPN-Mu-96T 96T
EUR 825.6
Description: A sandwich quantitative ELISA assay kit for detection of Mouse Podoplanin (PDPN) in samples from tissue homogenates, cell lysates or other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
EK8596 96Т
EUR 799

Mouse Podoplanin, Pdpn ELISA KIT
ELI-06723m 96 Tests
EUR 1038

Mouse Podoplanin (PDPN) ELISA Kit
EKN47838-48T 48T
EUR 389.62

Mouse Podoplanin (PDPN) ELISA Kit
EKN47838-5x96T 5x96T
EUR 2643.85

Mouse Podoplanin (PDPN) ELISA Kit
EKN47838-96T 96T
EUR 556.6

Mouse Podoplanin (PDPN) ELISA Kit
EKU06727-48T 48T
EUR 571.55

Mouse Podoplanin (PDPN) ELISA Kit
EKU06727-5x96T 5x96T
EUR 3878.38

Mouse Podoplanin (PDPN) ELISA Kit
EKU06727-96T 96T
EUR 816.5

Mouse Podoplanin (PDPN) ELISA Kit
DL-PDPN-Mu 96T
EUR 453
Description: tissue homogenates, cell lysates or other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
abx571749-96tests 96 tests
EUR 943.2

Mouse Podoplanin (PDPN) ELISA Kit
AE28131MO-48Tests 48 Tests
EUR 325
Description: Mouse (Mus musculus)

Mouse Podoplanin (PDPN) ELISA Kit
AE28131MO-96Tests 96 Tests
EUR 610
Description: Mouse (Mus musculus)

Mouse Podoplanin (PDPN) ELISA Kit
20-abx154564
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  • 10 × 96 tests
  • 5 × 96 tests
  • 96 tests

Mouse Podoplanin (PDPN) ELISA Kit
RD-PDPN-Mu-48T 48T
EUR 464.3
Description: tissue homogenates, cell lysates and other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
RD-PDPN-Mu-48Tests 48 Tests
EUR 639.6

Mouse Podoplanin (PDPN) ELISA Kit
RD-PDPN-Mu-96T 96T
EUR 663.3
Description: tissue homogenates, cell lysates and other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
RD-PDPN-Mu-96Tests 96 Tests
EUR 888

Mouse Podoplanin (PDPN) ELISA Kit
RK13459 96T
EUR 280

Mouse Podoplanin(PDPN)ELISA kit
QY-E21215 96T
EUR 433.2

Mouse Podoplanin (PDPN) ELISA Kit
SEC719Mu-10x96wellstestplate 10x96-wells test plate
EUR 5834.88
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Podoplanin (PDPN) in tissue homogenates, cell lysates and other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
SEC719Mu-1x48wellstestplate 1x48-wells test plate
EUR 585.7
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Podoplanin (PDPN) in tissue homogenates, cell lysates and other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
SEC719Mu-1x96wellstestplate 1x96-wells test plate
EUR 785.28
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Podoplanin (PDPN) in tissue homogenates, cell lysates and other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
SEC719Mu-5x96wellstestplate 5x96-wells test plate
EUR 3173.76
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Podoplanin (PDPN) in tissue homogenates, cell lysates and other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
4-SEC719Mu
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  • Ask for price
  • 10 plates of 96 wells
  • 5 plates of 96 wells
  • 1 plate of 96 wells
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Podoplanin (PDPN) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.

Mouse Podoplanin (PDPN) ELISA Kit
RDR-PDPN-Mu-48T 48T
EUR 487.52
Description: tissue homogenates, cell lysates and other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
RDR-PDPN-Mu-48Tests 48 Tests
EUR 668.4

Mouse Podoplanin (PDPN) ELISA Kit
RDR-PDPN-Mu-96T 96T
EUR 696.47
Description: tissue homogenates, cell lysates and other biological fluids.

Mouse Podoplanin (PDPN) ELISA Kit
RDR-PDPN-Mu-96Tests 96 Tests
EUR 928.8

Mouse Podoplanin (PDPN)ELISA kit
YLA0596MO-48T 48T Ask for price

Mouse Podoplanin (PDPN)ELISA kit
YLA0596MO-96T 96T Ask for price

Mouse PDPN(Podoplanin) ELISA Kit
ELK7080-48T 48T Ask for price
Description: The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse PDPN. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse PDPN. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse PDPN, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse PDPN in the samples is then determined by comparing the OD of the samples to the standard curve.

Mouse PDPN(Podoplanin) ELISA Kit
ELK7080-96T 96T Ask for price
Description: The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse PDPN. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse PDPN. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse PDPN, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse PDPN in the samples is then determined by comparing the OD of the samples to the standard curve.

Mouse PDPN (Podoplanin) ELISA Kit
EKE61859-5x96T 5x96T
EUR 3124.08

Mouse PDPN (Podoplanin) ELISA Kit
EKE61859-96T 96T
EUR 657.7

Mouse PDPN(Podoplanin) ELISA Kit
RE2052M-48wells 48 wells
EUR 116.55

Mouse PDPN(Podoplanin) ELISA Kit
RE2052M-96wells 96 wells
EUR 161.55

Mouse Pdpn / Podoplanin ELISA Kit
E2095m 96T
EUR 776

Anti-Rat Podoplanin Antibody
104-M40 100 µg
EUR 189
Description: Podoplanin is a well-recognized lymphatic endothelium marker, which can be used to reliably distinguish lymphatic vessels from blood vessels. It was originally discovered in kidney podocytes. This mouse monoclonal antibody (IgG) against rat podoplanin works well for immunohistochemistry with formalin-fixed paraffin embedded sections. This antibody also can be used in FACS sorting.

Anti- Podoplanin Human Antibody
GWB-F131C7 0.2 mg Ask for price

Podoplanin
E8ER1915-23 100ul
EUR 275
Description: Available in various conjugation types.

Podoplanin
E8ET1703-61 100ul
EUR 275
Description: Available in various conjugation types.

Podoplanin
AP79286 1mg
EUR 2640

Podoplanin
AP86601 1mg
EUR 2640

Podoplanin
AP87092 1mg
EUR 2640

Podoplanin
AP87543 1mg
EUR 2640

Podoplanin
MO47016 100 ul
EUR 418.8

Rabbit Anti-Human Podoplanin
102-PA40 100ug
EUR 240

Recombinant Mouse Podoplanin (C-Fc)
CU73-10ug 10ug
EUR 157.2
Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Recombinant Mouse Podoplanin (C-Fc)
CU73-1mg 1mg
EUR 2008.8
Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Recombinant Mouse Podoplanin (C-Fc)
CU73-500ug 500ug
EUR 1399.2
Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Recombinant Mouse Podoplanin (C-Fc)
CU73-50ug 50ug
EUR 327.6
Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Mouse Podoplanin, PDPN GENLISA ELISA
KLM1437 1 x 96 wells
EUR 341

Anti-Human Podoplanin Antibody
102-PA40AG 50 µg
EUR 147
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver (1). Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody
102-PA40S 100 µg
EUR 126
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential O-linked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on O-glycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody
101-M40-FITC 50 µg Ask for price
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody
101-M40-PE 50 µg Ask for price
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody
101-M40S-FITC 25 µg Ask for price
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody
101-M40S-PE 25 µg Ask for price
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody
101-M41 100 µg
EUR 199.5
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential O-linked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on O-glycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Hamster Monoclonal anti-mouse Podoplanin
mAP-0062 100ug
EUR 250

Podoplanin (PDPN) Polyclonal Antibody (Mouse)
4-PAC719Mu01
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  • 100ul
  • 10ml
  • 1ml
  • 200ul
  • 20ul
Description: A Rabbit polyclonal antibody against Mouse Podoplanin (PDPN)

ELISA kit for Mouse Podoplanin (PDPN)
KTE70775-48T 48T
EUR 398.4
Description: Quantitative sandwich ELISA for measuring Mouse Podoplanin (PDPN) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

ELISA kit for Mouse Podoplanin (PDPN)
KTE70775-5platesof96wells 5 plates of 96 wells
EUR 2538
Description: Quantitative sandwich ELISA for measuring Mouse Podoplanin (PDPN) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

ELISA kit for Mouse Podoplanin (PDPN)
KTE70775-96T 96T
EUR 646.8
Description: Quantitative sandwich ELISA for measuring Mouse Podoplanin (PDPN) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

ELISA kit for Mouse PDPN (Podoplanin)
E-EL-M2409 1 plate of 96 wells
EUR 640.8
Description: A sandwich ELISA kit for quantitative measurement of Mouse PDPN (Podoplanin) in samples from Serum, Plasma, Cell supernatant

ELISA kit for Mouse PDPN (Podoplanin)
ELK7080 1 plate of 96 wells
EUR 518.4
Description: A sandwich ELISA kit for detection of Podoplanin from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids.

Podoplanin antibody
10R-7662 100 ug
EUR 754.8
Description: Mouse monoclonal Podoplanin antibody

Podoplanin antibody
10R-7663 100 ug
EUR 754.8
Description: Hamster monoclonal Podoplanin antibody

Podoplanin antibody
10R-7664 100 ug
EUR 754.8
Description: Mouse monoclonal Podoplanin antibody

Podoplanin antibody
10R-P133a 100 ug
EUR 438
Description: Mouse monoclonal Podoplanin antibody

Podoplanin antibody
10R-P155a 100 ug
EUR 468
Description: Hamster monoclonal Podoplanin antibody

Podoplanin Antibody
E38PA2500 100ul
EUR 225
Description: Available in various conjugation types.

Podoplanin Antibody
DF12456 200ul
EUR 420

Podoplanin Antibody
DF12456-100ul 100ul
EUR 280

Podoplanin Antibody
DF12456-200ul 200ul
EUR 350

Podoplanin Antibody
49474 100ul
EUR 499

Podoplanin Antibody
49474-100ul 100ul
EUR 399.6

Podoplanin Antibody
49474-50ul 50ul
EUR 286.8

Podoplanin antibody
70R-PR007 100 ug
EUR 524
Description: Affinity purified Rabbit polyclonal Podoplanin antibody

Podoplanin antibody
70R-13952 100 ug
EUR 484
Description: Affinity purified Rabbit polyclonal Podoplanin antibody

Podoplanin antibody
70R-11540 100 ug
EUR 632.4
Description: Rabbit polyclonal Podoplanin antibody

Podoplanin antibody
70R-6816 50 ug
EUR 467
Description: Rabbit polyclonal Podoplanin antibody raised against the N terminal of PDPN

Podoplanin antibody
70R-6817 50 ug
EUR 467
Description: Rabbit polyclonal Podoplanin antibody raised against the middle region of PDPN

Podoplanin antibody
70R-50819 100 ul
EUR 242
Description: Purified Polyclonal Podoplanin antibody

Podoplanin Antibody
GWB-9E8999 1 ml Ask for price

Podoplanin Antibody
GWB-61B370 0.1 mg Ask for price

Podoplanin Antibody
R20464-0.1ML 100ul
EUR 409

Podoplanin Antibody
R33852-100UG 100 ug
EUR 339.15
Description: Additional name(s) for this target protein: PDPN; AGGRUS; GP36; GP40; Gp38; HT1A-1; OTS8; PA2.26

Podoplanin Antibody
P1051-01m 0.1m
EUR 250.8

Podoplanin Antibody
P1051-1ml 1ml
EUR 1129.2

Anti-D2-40 Podoplanin antibody
STJ16100360 1 mL
EUR 1482

Anti-D2-40/Podoplanin antibody
STJ190048 200 µl
EUR 236.4
Description: Unconjugated Mouse monoclonal to D2-40/Podoplanin (7D1)

Podoplanin (PDPN) Polyclonal Antibody (Mouse), PE
4-PAC719Mu01-PE
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  • 100ul
  • 10ml
  • 1ml
  • 200ul
  • 20ul
Description: A Rabbit polyclonal antibody against Mouse Podoplanin (PDPN). This antibody is labeled with PE.

Pdpn (untagged) - Mouse podoplanin (Pdpn), (10ug)
MC201786 10 µg Ask for price

Podoplanin (PDPN) Polyclonal Antibody (Mouse), APC
4-PAC719Mu01-APC
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  • 100ul
  • 10ml
  • 1ml
  • 200ul
  • 20ul
Description: A Rabbit polyclonal antibody against Mouse Podoplanin (PDPN). This antibody is labeled with APC.

Podoplanin (PDPN) Polyclonal Antibody (Mouse), Cy3
4-PAC719Mu01-Cy3
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  • 100ul
  • 10ml
  • 1ml
  • 200ul
  • 20ul
Description: A Rabbit polyclonal antibody against Mouse Podoplanin (PDPN). This antibody is labeled with Cy3.

Podoplanin (PDPN) Polyclonal Antibody (Mouse), HRP
4-PAC719Mu01-HRP
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  • 100ul
  • 10ml
  • 1ml
  • 200ul
  • 20ul
Description: A Rabbit polyclonal antibody against Mouse Podoplanin (PDPN). This antibody is labeled with HRP.

Podoplanin Mouse Monoclonal Antibody (IHC Gold)
E44H20290 250ul
EUR 655
Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

Rat Monoclonal anti-Mouse Podoplanin Antibody
xAP-0812 100ug
EUR 280

Podoplanin (PDPN) Polyclonal Antibody (Mouse), FITC
4-PAC719Mu01-FITC
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  • 100ul
  • 10ml
  • 1ml
  • 200ul
  • 20ul
Description: A Rabbit polyclonal antibody against Mouse Podoplanin (PDPN). This antibody is labeled with FITC.

Mouse Anti-Human Podoplanin monoclonal antibody, clone JID761
CABT-L2919-100uL500uL 100 uL, 500 uL
EUR 602.4

Mouse Anti-Human Podoplanin monoclonal antibody, clone JID761
CABT-L2919 100 µl, 500 µl Ask for price
Description: Mouse

Mouse Podoplanin, soluble Recombinant Protein
S01-M46 5 µg
EUR 63
Description: Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. The ECD contains abundant Ser/Thr residues as potential sites for Oglycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation. Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and on numerous tumors including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Podoplanin (PDPN) Antibody
abx433110-200ul 200 ul
EUR 460.8

Podoplanin (PDPN) Antibody
20-abx339428
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  • 100 ul
  • 50 ul

Podoplanin (PDPN) Antibody
20-abx129101
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  • 100 ug
  • 10 ug
  • 1 mg
  • 200 ug
  • 50 ug

Podoplanin (PDPN) Antibody
20-abx131102
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  • 100 ug
  • 10 ug
  • 1 mg
  • 200 ug
  • 50 ug

Podoplanin (PDPN) Antibody
20-abx211099
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  • 100 ul
  • 50 ul

Podoplanin (PDPN) Antibody
20-abx174125
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  • 1 mg
  • 200 ug

Podoplanin (PDPN) Antibody
20-abx174126
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  • 1 mg
  • 200 ug

Podoplanin (PDPN) Antibody
20-abx178065
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  • 1 mg
  • 200 ug

Two artificial bacterial consortia (SC) composed of bacterial strains Sphingobium sp. (AM), Klebsiella aerogenes (B), Pseudomonas sp. (Bc-h and T), Burkholderia sp. (Bk) and Inquilinus limosus (Inq) remoted from a pure phenanthrene (PHN)-degrading consortium (CON) have been developed and evaluated as an various method to PHN biodegradation in bioremediation processes. A metabolic community displaying the potential function of strains was reconstructed by in silico examine of the six genomes and classification of dioxygenase enzymes utilizing RHObase and AromaDeg databases. The predicted roles have been additional confirmed by physiological, RT-qPCR and metaproteomic assays. SC-1 with AM as the sole PHN degrader was the most efficient. The ecological roles inferred in this examine might be utilized to optimize the design of bacterial consortia and sort out the biodegradation of complicated environmental pollution.