In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.
Specificity
Natural and recombinant Mouse Heat shock 70 kDa protein 1B
Subcellular Location
Cytoplasm Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with TSC2 (By similarity). Component of a complex composed at least of CATSPER1, CATSPERB, CATSPERG2 and HSPA1B.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN A COMPLEX WITH CATSPER1 AND CATSPERB
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN A COMPLEX WITH CATSPER1; CATSPERB AND CATSPERG2
Reviews of ELISA Kit for Mouse Heat shock 70 kDa protein 1B