SGTA Protein(N-6His) (recombinant human)

Protein Construction: Recombinant Human Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein alpha is produced by our E.coli expression system and the target gene encoding Met1-Glu313 is expressed with a 6His tag at the N-terminus. Sequence: Met 1-Glu313. Fusion tag: N-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 35 kDa. Protein function: Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein a (SGTA) is an ubiquitously expressed protein which belongs to the SGT Family. SGTA contains three TPR Protein-Protein Interaction Duplicates. SGTA is a co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity. SGTA is capable of interacting with the major nonstructural protein of Parvovirus H-1 and 70-kDa heat shock cognate protein. It interacts with NS1 from Parvovirus H-1, with Vpu and Gag from HIV-1. It also interacts with SARS-CoV Accessory Protein 7a, DNAJC5 and DNAJC5B. However, its function is not known. Since this transcript is expressed ubiquitously in various tissues, SGTA may serve a housekeeping function. Protein function: Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails (PubMed:28104892). Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module (PubMed:28104892). Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins (PubMed:28104892, PubMed:25535373). It is also involved in the regulation of the endoplasmic reticulum- associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states (PubMed:23129660, PubMed:25179605). Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex (PubMed:27193484). Binds directly to HSC70 and HSP70 and regulates their ATPase activity (PubMed:18759457). [The UniProt Consortium]