Transmembrane Protease Serine 2 Antibody (YA2356)
(Synonyms: Epitheliasin; PRSS10; TMPRSS2)
Based on 1 Customer Validation
Transmembrane Protease Serine 2 Antibody (YA2356) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Transmembrane Protease Serine 2.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF, FC
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in rabbit IgG in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40%Glycerol, 0.01% sodium azide and 0.05% BSA.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
FC
FC: Flow Cytometry
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|---|---|---|---|---|
| Dilution Ratio | 1:1000-1:2000 | 1:100-1:200 | 1:50-1:200 | 1:50-1:100 |
Product Details
Transmembrane Protease Serine 2 Antibody (YA2356) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Transmembrane Protease Serine 2.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 54 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 54 kDa
A synthesized peptide derived from human TMPRSS2 aa1-45.
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in rabbit IgG in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40%Glycerol, 0.01% sodium azide and 0.05% BSA.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Transmembrane Protease Serine 2 is a 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[1][2][3][4][5][6][7][8][9][10][11][12].
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Subcellular Localization
Cell membrane; Single-pass type II membrane protein; Secreted
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Expression
Tissue_specificity: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)
Induction:By androgenic hormones in vivo -
Isoforms & Post-Translational Modification
O15393 has 2 isomers: O15393-1: 53859 Da (predicted); O15393-2: 57690 Da (predicted).
Proteolytically processed; by an autocatalytic mechanism. Autocleavage induces active conformation -
Subunit
The catalytically active form interacts with ACE2
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SwissProt ID
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Synonyms
Epitheliasin; PRSS10; TMPRSS2
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Research Field
Neuroscience
Documentation
References
[1]. Bestle D, et al. TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells. Life Sci Alliance. 2020 Sep;3(9):. [Content Brief]
[2]. Fraser BJ, et al. Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation. Nat Chem Biol. 2022 Sep;18(9):963-971. [Content Brief]
[3]. Wang H, et al. Structure-based discovery of dual pathway inhibitors for SARS-CoV-2 entry. Nat Commun. 2023 Nov 21;14(1):7574. [Content Brief]
[4]. McCallum M, et al. Human coronavirus HKU1 recognition of the TMPRSS2 host receptor. Cell. 2024 Aug 8;187(16):4231-4245.e13. [Content Brief]
[5]. Lucas JM, et al. The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis. Cancer Discov. 2014 Nov;4(11):1310-25. [Content Brief]
[6]. Wilson S, et al. The membrane-anchored serine protease, TMPRSS2, activates PAR-2 in prostate cancer cells. Biochem J. 2005 Jun 15;388(Pt 3):967-72. [Content Brief]
[7]. Ko CJ, et al. Androgen-Induced TMPRSS2 Activates Matriptase and Promotes Extracellular Matrix Degradation, Prostate Cancer Cell Invasion, Tumor Growth, and Metastasis. Cancer Res. 2015 Jul 15;75(14):2949-60. [Content Brief]
[8]. Heurich A, et al. TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein. J Virol. 2014 Jan;88(2):1293-307. [Content Brief]
[9]. Hoffmann M, et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell. 2020 Apr 16;181(2):271-280.e8. [Content Brief]
[10]. Zang R, et al. TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal enterocytes. Sci Immunol. 2020 May 13;5(47):. [Content Brief]
[11]. Buchrieser J, et al. Syncytia formation by SARS-CoV-2-infected cells. EMBO J. 2020 Dec 1;39(23):e106267. [Content Brief]
[12]. Koch J, et al. TMPRSS2 expression dictates the entry route used by SARS-CoV-2 to infect host cells. EMBO J. 2021 Aug 16;40(16):e107821. [Content Brief]
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