Catl Tmprss2 Spike Protein

Description: TMPRSS2 Antibody: TMPRSS2 is a plasma membrane-anchored serine protease that 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. It 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. It 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). TMPRSS2 is essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9), and it is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Description: TMPRSS2 Antibody: TMPRSS2 is a plasma membrane-anchored serine protease that 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. It 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. It 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). TMPRSS2 is essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9), and it is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Description: TMPRSS2 Antibody: TMPRSS2 is a plasma membrane-anchored serine protease that 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. It 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. It 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). TMPRSS2 is essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9), and it is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Description: Antibody raised against TMPRSS2

Description: A polyclonal antibody against TMPRSS2. Recognizes TMPRSS2 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB;ELISA:1:1000-1:2000, WB:1:200-1:1000

Description: Additional name(s) for this target protein: Transmembrane protease, serine 2

Description: Human transmembrane serine protease 2 (TMPRSS2) is an enzyme primarily expressed by endothelial cells across the respiratory and digestive tracts. It is involved in viral entry and spread of coronaviruses including SARS-CoV-2, the virus that causes COVID19. TMPRSS2 primes the spike protein by cleaving at the S1/S2 site, leading to the virus fusing to the respiratory epithelia on the cell surface through binding to ACE2. Blocking TMPRSS2 activity could potentially be an effective clinical therapy for COVID-19._x000D_
The TMPRSS2 Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to be transduced into almost all types of mammalian cells, including primary and non-dividing cells. The particles contain an TMPRSS2 gene (NM_005656.4) driven by an EF1a promoter._x000D_

Description: Human transmembrane serine protease 2 (TMPRSS2) is an enzyme primarily expressed by endothelial cells across the respiratory and digestive tracts. It is involved in viral entry and spread of coronaviruses including SARS-CoV-2, the virus that causes COVID19. TMPRSS2 primes the spike protein by cleaving at the S1/S2 site, leading to the virus fusing to the respiratory epithelia on the cell surface through binding to ACE2. Blocking TMPRSS2 activity could potentially be an effective clinical therapy for COVID-19._x000D_
The TMPRSS2 Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to be transduced into almost all types of mammalian cells, including primary and non-dividing cells. The particles contain an TMPRSS2 gene (NM_005656.4) driven by an EF1a promoter._x000D_

Description: Human transmembrane serine protease 2 (TMPRSS2) is an enzyme primarily expressed by endothelial cells across the respiratory and digestive tracts. It is involved in viral entry and spread of coronaviruses including SARS-CoV-2, the virus that causes COVID19. TMPRSS2 primes the spike protein by cleaving at the S1/S2 site, leading to the virus fusing to the respiratory epithelia on the cell surface through binding to ACE2. Blocking TMPRSS2 activity could potentially be an effective clinical therapy for COVID-19._x000D_
The TMPRSS2 Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to be transduced into almost all types of mammalian cells, including primary and non-dividing cells. The particles contain an TMPRSS2 gene (NM_005656.4) driven by an EF1a promoter._x000D_

Description: TMPRSS2 (CT)

Description: TMPRSS2 (IN)

Description: TMPRSS2 Antibody: TMPRSS2 is a plasma membrane-anchored serine protease that 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. It 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. It 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). TMPRSS2 is essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9), and it is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Description: TMPRSS2 Antibody: TMPRSS2 is a plasma membrane-anchored serine protease that 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. It 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. It 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). TMPRSS2 is essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9), and it is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.

Description: TMPRSS2 Antibody: TMPRSS2 is a plasma membrane-anchored serine protease that 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. It 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. It 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). TMPRSS2 is essential for spread and pathogenesis of influenza A virus (strains H1N1, H3N2 and H7N9), and it is involved in proteolytic cleavage and activation of hemagglutinin (HA) protein which is essential for viral infectivity.