protein

Recombinant Human Stress-Induced-Phosphoprotein 1

MBS143490

0.002 mg

140 USD

Recombinant Protein

Recombinant Human Stress-Induced-Phosphoprotein 1

Stress-Induced-Phosphoprotein 1

STIP1 Human; Stress-Induced-Phosphoprotein 1 Human Recombinant; HOP; P60; STI1; STI1L; IEF-SSP-3521; STIP1; Stress-induced-phosphoprotein 1; Hsc70/Hsp90-organizing protein; Transformation-sensitive protein IEF SSP 3521; Renal carcinoma antigen NY-REN-11

stress-induced-phosphoprotein 1 isoform a; Stress-induced-phosphoprotein 1; stress-induced-phosphoprotein 1; Hsp70/Hsp90-organizing protein; NY-REN-11 antigen; epididymis secretory sperm binding protein Li 94n; hsc70/Hsp90-organizing protein; renal carcinoma antigen NY-REN-11; transformation-sensitive protein IEF SSP 3521; stress-induced phosphoprotein 1; Hsc70/Hsp90-organizing protein; Hop; Renal carcinoma antigen NY-REN-11; Transformation-sensitive protein IEF SSP 3521

STIP1

STIP1; STIP1; HOP; P60; STI1; STI1L; HEL-S-94n; IEF-SSP-3521; STI1; Hop

STIP1_HUMAN

E Coli

590

Greater than 90.0% as determined by SDS-PAGE.

The STIP1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA, 0.2mM PMSF and 20% Glycerol. Sterile filtered colorless solution.

1mg/ml

Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

RECOMBINANT & NATURAL PROTEINS; Recombinant Proteins

Description: Recombinant Human STIP1 produced in E Coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543 a.a) and having a molecular mass of 64.8kDa. STIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques. Introduction: STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

544063423

NP_001269581.1

NM_001282652.1

P31948

59,778 Da

Prion Diseases Pathway (101144); Prion Diseases Pathway (100065)

STIP1 is an adaptor protein that coordinates the functions of HSP70 (see HSPA1A; MIM 140550) and HSP90 (see HSP90AA1; MIM 140571) in protein folding. It is thought to assist in the transfer of proteins from HSP70 to HSP90 by binding both HSP90 and substrate-bound HSP70. STIP1 also stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones (Song and Masison, 2005 [PubMed 16100115]).[supplied by OMIM, Jul 2009]

STI1: a protein that is apparently involved in the response to stress. Specifically interacts with the C-terminal tails of Hsp70 and Hsp90 via TPR1 and TPR2A domains. Deletion of STI1 reduces the activity of the glucocorticoid receptor, a Hsp90 target protein. Phosphorylated in vitro by p90RSK and casein kinase II. Protein type: Chaperone. Chromosomal Location of Human Ortholog: 11q13. Cellular Component: Golgi apparatus; nucleus. Molecular Function: protein binding. Biological Process: response to stress

0.002 mg

140 USD

0.01 mg

205

1 mg

5015