Recombinant human Hip/ST13 protein

MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG DENAEITEEM MDQANDKKVA AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER KREEREIKER IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK LSAKFGGQA

Hip (Hsc70-interacting protein), also known as ST13, is a co-chaperone to the major heat shock proteins, Hsp70 and Hsp90, and appears in early receptor complexes. Through mutual binding to both Hsp70 and Hsp90, Hip functions as an adaptor that can integrate Hsp70 and Hsp90 interactions. Also, Hip has been shown to be involved in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. Recombinant human Hip was expressed in E. coli and purified by using conventional chromatography

< 1 EU per 1ug of protein (determined by LAL method)

Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 0.1M NaCl, 10% glycerol

Nelson GM., et al. (2004). Mol Endocrinol. 18(7):1620-30; ; Johnson BD., et al. (1998). J Biol chem. 273(6):3679-86; ;