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Related ArticlesGPR176 is a Members of the G protein-coupled receptor family, such as GPR176, are cell surface receptors involved in responses to hormones, growth factors, and neurotransmitters (Hata et al., 1995 [PubMed 7893747]).[supplied by OMIM, Jul 2008].
This gene encodes one of the many small GTP-binding proteins in the Rho family shown to be associated with focal adhesions in endothelial cells (PMID: 21148427, 22103495). The encoded protein is activated by vascular endothelial growth factor and may regulate angiogenesis. [provided by RefSeq, Dec 2011]
The CW domain is a structural module found in many vertebrate, parasitic and plant proteins. It consists of a mononuclear four-cysteine zinc-finger domain that plays a role in DNA binding, chromatin methylation and early embryonic development. ZCWCC1 (zinc finger CW-type coiled-coil domain protein 1), also known as MORC2 (MORC family CW-type zinc finger protein 2) or ZCW3, is a 1,032 amino acid protein that contains one CW-type zinc finger domain. ZCWCC1 is located on chromosome 22 and is ub
The CW domain is a structural module found in many vertebrate, parasitic and plant proteins. It consists of a mononuclear four-cysteine zinc-finger domain that plays a role in DNA binding, chromatin methylation and early embryonic development. ZCWCC1 (zinc finger CW-type coiled-coil domain protein 1), also known as MORC2 (MORC family CW-type zinc finger protein 2) or ZCW3, is a 1,032 amino acid protein that contains one CW-type zinc finger domain. ZCWCC1 is located on chromosome 22 and is ub
Orphan receptor.
Pin1 is a Peptidyl-prolyl isomerases (PPIase). Peptidyl-prolyl isomerases (PPIase) facilitate the cis-trans interconversion of the peptidyl-prolyl bond thereby affecting protein folding. Pin1 is a PPIase which specifically recognizes phosphorylated S/T-P bonds. Pin1 has been implicated in tau pathologies that underlie Alzheimer's Disease. Pin1 binds to tau phosphorylated specifically on the Thr231-Pro site and induces conformational changes in tau. Such conformational changes can directly res
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