Anti-HSP70, clone BRM-22

0.5mg/ml with 1% BSA and 0.01% sodium azide if reconstituted with 0.2ml sterile 1XPBS. Heat-shock proteins, or stress proteins, are expressed in response to heat shock and a variety of other stress stimuli including oxidative free radicals and toxic metal ions. Sargent et al. identified a duplicated HSP70 locus in the class III region of the major histocompatibility complex on 6p21.3. A duplicated locus encoding the major heat shock-induced protein HSP70 is located in the major histocompatibility complex (MHC) class III region 92 kilobases (kb) telomeric to the C2 gene. The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. Protein function: Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A. May execute multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment. Binds the Golgi-modified P2 form of CPY, and this interaction is dependent on the presence of an intact CPY vacuolar protein sorting signal. [The UniProt Consortium]