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TMPRSS2 encodes a protein that belongs to the serine protease family. Additionally we are shipping TMPRSS2 Antibodies (73) and TMPRSS2 Kits (26) and many more products for this protein.
Showing 7 out of 12 products:
Our findings indicate that TGF-beta (show TGFB1 Proteins) signaling is a major determinant of EMT (show ITK Proteins) in T/E overexpressing LNCaP cells.
A potential novel function of TMPRSS2-ERG (show ERG Proteins) as a major regulator of IGF1R (show IGF1R Proteins) gene expression.
Study shows that T2E fusion transcripts are associated with higher levels of AMACR (show AMACR Proteins) mRNA in patients with atypical small acinar proliferation (ASAP (show MAP9 Proteins)) which represents an indicator of risk for prostate cancer in patients with ASAP (show MAP9 Proteins).
TMPRSS2-ERG (show ERG Proteins) may have a role in progression of prostate neoplasms and in alteration of the metabolic profile
Meta-analysis showed the prevalence of TMPRSS2:ERG (show ERG Proteins) fusions in prostate cancer to be highest in men of European descent (49%), followed by Asians (27%) and then African (25%) descent.
Data show that tumors displaying TMPRSS2-ERG (show ERG Proteins) fusions that retained interstitial genes were less likely to be associated with biochemical recurrence
We demonstrate a role for inflammation-induced oxidative stress in the formation of DNA breaks leading to recurrent TMPRSS2-ERG (show ERG Proteins) gene fusions. The transcriptional status and epigenetic features of the target genes influence this effect.
NOTCH (show NOTCH1 Proteins) pathway inhibition antagonizes the growth and invasion of transmembrane protease serine 2 (TMPRSS2)-transforming protein ERG (ERG) (T2E) -positive prostate cancer cells.
The TMPRSS2-ERG (show ERG Proteins) gene fusion is the most frequently observed genetic aberration in prostate cancer.
Study provide evidence that PTEN deletion and TMPRSS2-ERG (show ERG Proteins) gene fusion were mutually exclusive in patients with prostate neoplasm. TMPRSS2-ERG (show ERG Proteins) gene fusion was rare compared to peripheral zone tumors and to PTEN inactivation in T1a (show PDPN Proteins) transition zone tumors.
Study shows that Influenza A (IAV) possessing a monobasic cleavage site in the haemagglutinin (HA) replicates poorly in TMPRSS2 knockout mice due to insufficient HA cleavage. On the contrary, IBV successfully underwent HA cleavage in TMPRSS2 knockout mice, and that the mouse-adapted strain was fully pathogenic. These data demonstrate a clear difference between IAV and IBV in their molecular mechanisms for spreading.
DPP4 (show DPP4 Proteins):CD9 (show CD9 Proteins):TTSP (show TMPRSS11E Proteins) as the protein complexes are necessary for early efficient MERS-coronavirus entry.
Genetic inhibition of TMPRSS2-ERG (show ERG Proteins) junction oncogene (show RAB1A Proteins) in prostate cancer by means of siRNA has strong antineoplastic effect in a mouse model and in vitro.
The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis
TMPRSS2 as a host cell factor essential for viral spread and pathogenesis of mono-basic H1N1 and H3N2 influenza A viruses.
These results demonstrate that TMPRSS2 expression is essential for influenza A virus replication in vivo.
These data demonstrate that TMPRSS2 is a host factor that is essential for pneumotropism and pathogenicity of H7N9 and H1N1 influenza virus in mice.
Loss of TMPRSS2 serine protease (show F2 Proteins) activity does not influence fertility, reduce survival, result in prostate hyperplasia or carcinoma, or alter prostatic luminal epithelial cell regrowth following castration and androgen replacement.
This gene encodes a protein that belongs to the serine protease family. The encoded 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. This 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. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, serine protease 10
, transmembrane protease serine 2
, plasmic transmembrane protein X