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 HUMAN PODOPLANIN
MBS212743-01mg 0.1mg
EUR 450

MOUSE ANTI HUMAN PODOPLANIN
MBS212743-5x01mg 5x0.1mg
EUR 1840

Mouse Anti Human Podoplanin
MBS140296-0005mg 0.005mg
EUR 240

Mouse Anti Human Podoplanin
MBS140296-002mg 0.02mg
EUR 310

Mouse Anti Human Podoplanin
MBS140296-01mg 0.1mg
EUR 610

Mouse Anti Human Podoplanin
MBS140296-5x01mg 5x0.1mg
EUR 2405

Mouse Anti-Rat Podoplanin
MBS690143-01mg 0.1mg
EUR 450

Mouse Anti-Rat Podoplanin
MBS690143-5x01mg 5x0.1mg
EUR 1725

Mouse anti-rat podoplanin
11-035 0.2 mL Ask for price

Hamster anti Podoplanin (mouse)
103-M40 100ug
EUR 297.6

Mouse Anti-Human Podoplanin
MBS690117-0025mg 0.025mg
EUR 310

Mouse Anti-Human Podoplanin
MBS690117-5x0025mg 5x0.025mg
EUR 1110

Mouse Anti-Human Podoplanin
MBS690586-01mg 0.1mg
EUR 450

Mouse Anti-Human Podoplanin
MBS690586-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human Podoplanin
MBS690680-0025mg 0.025mg
EUR 310

Mouse Anti-Human Podoplanin
MBS690680-5x0025mg 5x0.025mg
EUR 1110

Mouse Anti-Human Podoplanin
MBS690759-01mg 0.1mg
EUR 450

Mouse Anti-Human Podoplanin
MBS690759-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human Podoplanin
MBS690992-005mg 0.05mg
EUR 430

Mouse Anti-Human Podoplanin
MBS690992-5x005mg 5x0.05mg
EUR 1645

Mouse Anti-Human Podoplanin
MBS692357-005mg 0.05mg
EUR 450

Mouse Anti-Human Podoplanin
MBS692357-5x005mg 5x0.05mg
EUR 1725

Mouse Anti-Human Podoplanin
MBS692358-005mg 0.05mg
EUR 450

Mouse Anti-Human Podoplanin
MBS692358-5x005mg 5x0.05mg
EUR 1725

Mouse anti-human podoplanin
11-003 0.2 mL Ask for price

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

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

Podoplanin Mouse mAb
A18776 100μL
EUR 719.13

Podoplanin Mouse mAb
E47M34236 100ul
EUR 295

Mouse Podoplanin, soluble
MBS691731-0005mg 0.005mg
EUR 250

Mouse Podoplanin, soluble
MBS691731-5x0005mg 5x0.005mg
EUR 835

Mouse Anti Human Podoplanin clone P56F7AT
MBS146676-0005mg 0.005mg
EUR 240

Mouse Anti Human Podoplanin clone P56F7AT
MBS146676-002mg 0.02mg
EUR 310

Mouse Anti Human Podoplanin clone P56F7AT
MBS146676-01mg 0.1mg
EUR 610

Mouse Anti Human Podoplanin clone P56F7AT
MBS146676-5x01mg 5x0.1mg
EUR 2405

Anti-Human/Mouse PDPN/Podoplanin Antibody
MBS1569238-01mg 0.1mg
EUR 405

Anti-Human/Mouse PDPN/Podoplanin Antibody
MBS1569238-5x01mg 5x0.1mg
EUR 1520

PE anti-mouse Podoplanin
GT03332 50 µg Ask for price

PE anti-mouse Podoplanin
GT03333 200 µg Ask for price

APC anti-mouse Podoplanin
GT03334 25 µg Ask for price

APC anti-mouse Podoplanin
GT03335 100 µg Ask for price

FITC anti-mouse Podoplanin
GT03339 100 µg Ask for price

FITC anti-mouse Podoplanin
GT03338 25 µg Ask for price

Recombinant Mouse Podoplanin
MBS7610672-005mg 0.05mg
EUR 345

Recombinant Mouse Podoplanin
MBS7610672-02mg 0.2mg
EUR 635

Recombinant Mouse Podoplanin
MBS7610672-1mg 1mg
EUR 1800

Recombinant Mouse Podoplanin
MBS7610672-5x1mg 5x1mg
EUR 6955

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

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
E03P0082-48wellsplate 48 wells plate
EUR 280

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
E03P0082-96wellsplate 96 wells plate
EUR 405

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

Mouse Podoplanin ELISA Kit
MBS2884556-10x96StripWells 10x96-Strip-Wells
EUR 4080

Mouse Podoplanin ELISA Kit
MBS2884556-48StripWells 48-Strip-Wells
EUR 390

Mouse Podoplanin ELISA Kit
MBS2884556-5x96StripWells 5x96-Strip-Wells
EUR 2220

Mouse Podoplanin ELISA Kit
MBS2884556-96StripWells 96-Strip-Wells
EUR 520

Mouse Podoplanin ELISA Kit
MBS725552-10x96StripWells 10x96-Strip-Wells
EUR 5685

Mouse Podoplanin ELISA Kit
MBS725552-48StripWells 48-Strip-Wells
EUR 485

Mouse Podoplanin ELISA Kit
MBS725552-5x96StripWells 5x96-Strip-Wells
EUR 3020

Mouse Podoplanin ELISA Kit
MBS725552-96StripWells 96-Strip-Wells
EUR 690

Biotin anti-mouse Podoplanin
GT03328 50 µg Ask for price

Biotin anti-mouse Podoplanin
GT03329 500 µg Ask for price

Hamster Anti-Mouse Podoplanin
MBS690646-01mg 0.1mg
EUR 450

Hamster Anti-Mouse Podoplanin
MBS690646-5x01mg 5x0.1mg
EUR 1725

Hamster Anti-Mouse Podoplanin
MBS690790-005mg 0.05mg
EUR 430

Hamster Anti-Mouse Podoplanin
MBS690790-5x005mg 5x0.05mg
EUR 1645

Hamster anti-mouse podoplanin
11-033 100 µg Ask for price

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 (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
20-abx650139
  • Ask for price
  • Ask for price
  • Ask for price
  • Ask for price
  • Ask for price
  • 10 ug
  • 50 ug
  • 100 ug
  • 200 ug
  • 1 mg

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

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

Podoplanin (ABT360) Mouse mAb
UB-GEN-15155 100 ul
EUR 200

Podoplanin (ABT513) Mouse mAb
UB-GEN-14883 100 ul
EUR 200

Mouse Monoclonal Podoplanin Antibody
TA327727 1 ml Ask for price

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

ELISA Kit for Mouse Podoplanin
E2095m 96T
EUR 387.4

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 Podoplanin (PDPN) ELISA Kit
abx571749-96tests 96 tests
EUR 587.5

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
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
20-abx154564
  • Ask for price
  • Ask for price
  • Ask for price
  • 96 tests
  • 5 × 96 tests
  • 10 × 96 tests

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

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

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

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

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
E1437Mo-1096T 10*96T
EUR 4122

Mouse Podoplanin,PDPN ELISA KIT
E1437Mo-48wells 48 wells
EUR 300

Mouse Podoplanin,PDPN ELISA KIT
E1437Mo-596T 5*96T
EUR 2061

Mouse Podoplanin,PDPN ELISA KIT
E1437Mo-96wells 96 wells
EUR 458

Mouse Podoplanin,PDPN ELISA KIT
JOT-EK1437Mo 96 wells Ask for price
Description: Mouse

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
EK8596 96Т
EUR 799

Mouse Podoplanin (PDPN) ELISA Kit
MBS1601033-10x96StripWells 10x96-Strip-Wells
EUR 3955

Mouse Podoplanin (PDPN) ELISA Kit
MBS1601033-48StripWells 48-Strip-Wells
EUR 305

Mouse Podoplanin (PDPN) ELISA Kit
MBS1601033-5x96StripWells 5x96-Strip-Wells
EUR 2005

Mouse Podoplanin (PDPN) ELISA Kit
MBS1601033-96StripWells 96-Strip-Wells
EUR 475

Mouse Podoplanin (PDPN) ELISA Kit
MBS4501762-10x96Tests 10x96Tests
EUR 5375

Mouse Podoplanin (PDPN) ELISA Kit
MBS4501762-48Tests 48Tests
EUR 470

Mouse Podoplanin (PDPN) ELISA Kit
MBS4501762-5x96Tests 5x96Tests
EUR 2755

Mouse Podoplanin (PDPN) ELISA Kit
MBS4501762-96Test 96Test
EUR 620

Mouse Podoplanin (PDPN) ELISA Kit
MBS2020020-10x96StripWells 10x96-Strip-Wells
EUR 5455

Mouse Podoplanin (PDPN) ELISA Kit
MBS2020020-24StripWells 24-Strip-Wells
EUR 365

Mouse Podoplanin (PDPN) ELISA Kit
MBS2020020-48StripWells 48-Strip-Wells
EUR 550

Mouse Podoplanin (PDPN) ELISA Kit
MBS2020020-5x96StripWells 5x96-Strip-Wells
EUR 2985

Mouse Podoplanin (PDPN) ELISA Kit
MBS2020020-96StripWells 96-Strip-Wells
EUR 740

Mouse Podoplanin (PDPN) ELISA Kit
MBS455766-10x96StripWells 10x96-Strip-Wells
EUR 5160

Mouse Podoplanin (PDPN) ELISA Kit
MBS455766-48StripWells 48-Strip-Wells
EUR 450

Mouse Podoplanin (PDPN) ELISA Kit
MBS455766-5x96StripWells 5x96-Strip-Wells
EUR 2645

Mouse Podoplanin (PDPN) ELISA Kit
MBS455766-96StripWells 96-Strip-Wells
EUR 595

Mouse Podoplanin (PDPN) ELISA Kit
MBS2803565-10x96StripWells 10x96-Strip-Wells
EUR 6255

Mouse Podoplanin (PDPN) ELISA Kit
MBS2803565-48StripWells 48-Strip-Wells
EUR 445

Mouse Podoplanin (PDPN) ELISA Kit
MBS2803565-5x96StripWells 5x96-Strip-Wells
EUR 3290

Mouse Podoplanin (PDPN) ELISA Kit
MBS2803565-96StripWells 96-Strip-Wells
EUR 730

Mouse Podoplanin (PDPN) ELISA Kit
MBS2704635-10x96StripWells 10x96-Strip-Wells
EUR 3215

Mouse Podoplanin (PDPN) ELISA Kit
MBS2704635-24StripWells 24-Strip-Wells
EUR 255

Mouse Podoplanin (PDPN) ELISA Kit
MBS2704635-48StripWells 48-Strip-Wells
EUR 340

Mouse Podoplanin (PDPN) ELISA Kit
MBS2704635-5x96StripWells 5x96-Strip-Wells
EUR 1675

Mouse Podoplanin (PDPN) ELISA Kit
MBS2704635-96StripWells 96-Strip-Wells
EUR 430

Mouse Podoplanin (PDPN) ELISA Kit
MBS9309796-10x96StripWells 10x96-Strip-Wells
EUR 6725

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.