HSP 70/HSC 70 Antibody (W27) is a mouse monoclonal IgG2a / Антитела моноклональные мышиные IgG2a к HSP 70/HSC 70 (W27)

HSP 70/HSC 70 Antibody (W27) is a mouse monoclonal IgG_2a provided at 200 µg/ml

raised against HSP 70 protein from HeLa cells

recommended for detection of HSP 70 and HSC 70 of mouse, rat and human origin by WB, IP, IF, IHC(P) and FCM

TransCruz reagent for ChIP application, sc-24 X, 200 µg/0.1 ml

agarose conjugate for IP studies, sc-24 AC, 500 µg/0.25 ml agarose

fluorescein (sc-24 FITC) and phycoerythrin (sc-24 PE) conjugates for intracellular FCM, 100 tests

HRP conjugate, sc-24 HRP, 200 µg/ml

See 130 citations for HSP 70/HSC 70 Antibody (W27)

The HSP 70 family is composed of four highly conserved proteins: HSP 70, HSC 70, GRP 75 and GRP 78. These proteins serve a variety of roles: they act as molecular chaperones facilitating the assembly of multi-protein complexes, participate in the translocation of polypeptides across cell membranes and to the nucleus and aid in the proper folding of nascent polypeptide chains. All members of the family, except HSP 70, are constitutively expressed in primate cells. HSP 70 expression is strongly induced in response to heat stress. HSP 70 and HSC 70 play key roles in the cytosolic endoplasmic reticulum and mitochondrial import machinery and are found in both the cytosol and nucleus of mammalian cells. Both HSP 70 and HSC 70 are involved in the chaperoning of nascent polypeptide chains and in protecting cells against the accumulation of improperly folded proteins. GRP 78 is localized in the endoplasmic reticulum, where it receives imported secretory proteins and is involved in the folding and translocation of nascent peptide chains. GRP 75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin. GRP 75 and GRP 78 are unresponsive to heat stress and are induced by glucose deprivation. It has been postulated that members of the HSP 70 family act as force-generating motors, relying on the hydrolysis of ATP for their activity.

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