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TMPRSS2 Antibody (Center)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - TMPRSS2 Antibody (Center) AP7377c
    Western blot analysis of TMPRSS2 antibody (Center) (Cat. #AP7377c) in HepG2 cell line lysates (35ug/lane). TMPRSS2 (arrow) was detected using the purified Pab.
  • 4 - TMPRSS2 Antibody (Center) AP7377c
    TMPRSS2 Antibody (Center) (Cat. #AP7377c) flow cytometric analysis of HepG2 cells (right histogram) compared to a negative control cell (left histogram).FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, FC, E
Primary Accession O15393
Other Accession Q9JIQ8
Reactivity Human, Rat, Mouse
Predicted Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 53859 Da
Antigen Region 314-343 aa
Additional Information
Gene ID 7113
Other Names Transmembrane protease serine 2, 3421-, Serine protease 10, Transmembrane protease serine 2 non-catalytic chain, Transmembrane protease serine 2 catalytic chain, TMPRSS2, PRSS10
Target/Specificity This TMPRSS2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 314-343 amino acids from the Central region of human TMPRSS2.
Dilution WB~~1:1000
FC~~1:10~50
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsTMPRSS2 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name TMPRSS2 (HGNC:11876)
Synonyms PRSS10
Function Plasma membrane-anchored serine protease that cleaves at arginine residues (PubMed:32703818, PubMed:35676539, PubMed:37990007, PubMed:38964328). Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate (PubMed:25122198). Androgen-induced TMPRSS2 activates several substrates that include pro- hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells (PubMed:15537383, PubMed:25122198, PubMed:26018085). In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia (By similarity).
Cellular Location Cell membrane; Single-pass type II membrane protein
Tissue Location Expressed in several tissues that comprise large populations of epithelial cells with the highest level of transcripts measured in the prostate gland. Expressed in type II pneumocytes in the lung (at protein level). Expressed strongly in small intestine. Also expressed in colon, stomach and salivary gland. Coexpressed with ACE2 within lung type II pneumocytes, ileal absorptive enterocytes, intestinal epithelial cells, cornea, gallbladder and nasal goblet secretory cells (Ref.21). {ECO:0000269|PubMed:11169526, ECO:0000269|PubMed:20382709, ECO:0000269|PubMed:21325420, ECO:0000269|PubMed:32404436, ECO:0000269|Ref.21}
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

TMPRSS2 is a protein that belongs to the serine protease family. The protein contains a type II transmembrane domain, a receptor class A domain, a scavenger receptor cysteine-rich domain and a protease domain. Serine proteases are known to be involved in many physiological and pathological processes. Its gene was demonstrated to be up-regulated by androgenic hormones in prostate cancer cells and down-regulated in androgen-independent prostate cancer tissue. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage.

REFERENCES

Gopalan,A., Cancer Res. 69 (4), 1400-1406 (2009)
Hofer,M.D., Cancer Res. 69 (2), 640-646 (2009)

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