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Overview
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Recombinant HSPH1 produced in E. Coli is a single, non-glycosylated polypeptide chain containing 894 amino acids and having a molecular mass of 100.9kDa. HSP105 Alpha is fused with a 36 a.a. His tag and purified by conventional chromatography techniques. HSPH1 analysis is used as an indicator and as a diagnostic aid in problematic lesions. HSPH1 chaperones the responses to endoplasmic reticulum (ER) stress during its interactions with GRP78 and GSK3, and without HSP105 cell death following ER stress proceeds by a non-caspase-3-dependent process. HSPH1 is highly expressed in a variety of human tumors. HSPH1 is a mammalian member of the HSP105/110 family, a diverged subgroup of the HSP70 family. HSP105 has 2 isoforms, alpha and beta. Hsp105a associates with Hsp70/Hsc70 as complexes in vivo and regulates the chaperone activity of Hsp70/Hsc70 negatively in vitro and in vivo.
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- Properties
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Overview