Anti-TMPRSS2 antibody (2-50 aa) (STJ13102583)

SPECIFICATIONS
ClonalityPolyclonal
HostGuinea Pig
ConjugationUnconjugated
ImmunogenA synthetic peptide from aa region 2-50 of human TMPRSS2 conjugated to blue carrier protein was used as the antigen.
STJ13102583-100
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General Information

Short DescriptionGuinea Pig polyclonal anti-TMPRSS2 (2-50 aa) for use in IHC and WB in Human and Rat samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsIHC/WB
HostGuinea Pig
ReactivityHuman/Rat
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityPolyclonal
ConjugationUnconjugated
PurificationAffinity purification
Dilution RangeIHC, WB. A dilution of 1: 2000 is recommended fro WB and IHC-P. The optimal dilution should be determined by the end user. Not yet tested in other applications.
FormulationLyophilised
Storage InstructionMaintain the lyophilised/reconstituted antibodies frozen at-20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, Glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Target Information

Gene SymbolTMPRSS2
Gene ID7113
Uniprot IDTMPS2_HUMAN
ImmunogenA synthetic peptide from aa region 2-50 of human TMPRSS2 conjugated to blue carrier protein was used as the antigen.
Immunogen Region2-50 aa
SpecificitySpecific for TMPRSS2.

Additional Info

Post Translational Modifications Proteolytically processed.by an autocatalytic mechanism. Autocleavage induces active conformation.
Function Plasma membrane-anchored serine protease that cleaves at arginine residues. Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate. 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. In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia. (Microbial infection) Facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via two independent mechanisms, proteolytic cleavage of ACE2 receptor which promotes viral uptake, and cleavage of coronavirus spike glycoproteins which activates the glycoprotein for host cell entry. The cleavage of SARS-COV2 spike glycoprotein occurs between the S2 and S2' site. Upon SARS-CoV-2 infection, increases syncytia formation by accelerating the fusion process. Proteolytically cleaves and activates the spike glycoproteins of human coronavirus 229E (HCoV-229E) and human coronavirus EMC (HCoV-EMC) and the fusion glycoproteins F0 of Sendai virus (SeV), human metapneumovirus (HMPV), human parainfluenza 1, 2, 3, 4a and 4b viruses (HPIV). Essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9).involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity. (Microbial infection) Receptor for human coronavirus HKU1-CoV, acts synergistically with disialoside glycans to facilitate the entry of the virus. After binding to cell-surface disialoside glycans, the viral S protein interacts with the inactive form of TMPRSS2 and inhibits its protease activity.
Protein Name Transmembrane Protease Serine 2
Serine Protease 10 Cleaved Into - Transmembrane Protease Serine 2 Non-Catalytic Chain - Transmembrane Protease Serine 2 Catalytic Chain
Database Links Reactome: R-HSA-9678110
Reactome: R-HSA-9694614
Reactome: R-HSA-9733458
Cellular Localisation Cell Membrane
Single-Pass Type Ii Membrane Protein
Transmembrane Protease Serine 2 Catalytic Chain: Secreted
Activated By Cleavage And Secreted
Alternative Antibody Names Anti-Transmembrane Protease Serine 2 antibody
Anti-Serine Protease 10 Cleaved Into - Transmembrane Protease Serine 2 Non-Catalytic Chain - Transmembrane Protease Serine 2 Catalytic Chain antibody
Anti-TMPRSS2 antibody
Anti-PRSS10 antibody

Information sourced from Uniprot.org

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