Search Thermo Fisher Scientific
Search Thermo Fisher Scientific
Immunogen sequence: MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA; Positive Samples: U-937, U-87MG, Raji, A-549, HeLa, Jurkat, MCF-7; Cellular Location: Cell membrane, Cytoplasm, Melanosome, Nucleus, nucleolus
The HSP70 family is a set of highly conserved proteins that are induced by a variety of biological stresses, including heat stress, in every organism in which the proteins have been examined. The human HSP70 family members include: HSP70, a protein which is strongly inducible in all organisms but which is also constitutively expressed in primate cells; HSP72, a 72 kDa protein that is induced exclusively under stress conditions; HSC70, or cognate protein, is a 72 kDa, constitutively expressed, protein which is involved in the uncoating of clathrin coated vesicles; GRP78, or BiP, is a glucose regulated 78 kDa protein localized in the endoplasmic reticulum; and p75, or HSP75, a 75 kDa protein that is found within the mitochondria. HSC70 (also known as HSC71, HSC73, HSP73, p72, prp73) is expressed constitutively and is slightly heat-inducible. HSC70 binds to the exposed loop of clathrin light chains to promote uncoating and can also bind the cytoskeleton which may facilitate cytoskeletal rearrangements. HSC70 has been shown to stimulate lysosomal degradation of intracellular proteins and to retard both aggregation and folding of mitochondrial precursor proteins in vitro.
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