SRI Human
Description
SRI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 221 amino acids (1-198 a.a.) and having a molecular mass of 24.1kDa. The SRI is purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MGSMAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS V.
Product Science Overview
Sorcin is a member of the penta-EF-hand (PEF) protein family, characterized by its calcium-binding domains. It consists of two main domains:
- N-terminal domain: A flexible, glycine-rich region.
- Calcium-binding domain: Contains five EF-hand motifs, which are helix-loop-helix structures that bind calcium ions with high affinity .
The SRI gene can produce at least four alternative transcripts, resulting in different isoforms of Sorcin. The primary isoform, known as isoform A, is a 198-amino-acid-long protein .
Sorcin plays a crucial role in calcium homeostasis and excitation-contraction coupling in the heart. It modulates the activity of RYR2 calcium channels in the sarcoplasmic reticulum, contributing to the regulation of calcium levels within cardiac cells . Upon binding calcium, Sorcin undergoes a conformational change that allows it to interact with its molecular targets .
Sorcin has been implicated in multidrug resistance in cancer cells. It has been identified as a binding partner of TRAP1, a mitochondrial chaperone, in human colorectal carcinoma cells. This interaction suggests that Sorcin may play a role in the TRAP1-associated signaling pathway, contributing to the cytoprotective functions in cancer cells .
