CST, 4872S, HSP70 Antibody

Polyclonal Antibody for studying HSP70. Validated for Western Blotting,Immunohistochemistry (Paraffin). Available in 2 sizes. Highly specific and rigorously validated in-house, HSP70 Antibody (CST #4872) is ready to ship. Product Usage Information Western Blotting: 1:1000 Immunohistochemistry (Paraffin): 1:150 - 1:600 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting, Immunohistochemistry (Paraffin) Specificity / Sensitivity HSP70 Antibody detects endogenous levels of total HSP70 protein (HSP70-Hom, HSP70-1) and HSC70. Species Reactivity: Human, Mouse, Rat, Monkey, Bovine Source / Purification Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser254 of human HSP70 protein. Antibodies are purified by protein A and peptide affinity chromatography. Background HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2). Alternate Names dnaK-type molecular chaperone HSP70-1; epididymis secretory protein Li 103; epididymis secretory sperm binding protein; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A; Heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1B; Heat shock 70 kDa protein 2; heat shock 70kD protein 1A; heat shock 70kD protein 1A/1B; heat shock 70kDa protein 1A; heat shock 70kDa protein 1A/1B; Heat Shock Protein 70; heat shock protein family A (Hsp70) member 1A; heat shock-induced protein; HEL-S-103; HS71A; HSP70; HSP70-1; HSP70-1/HSP70-2; HSP70-1A; HSP70-2; HSP70.1; HSP70.1/HSP70.2; HSP70.2; HSP70I; HSP71; HSP72; HSPA1; HSPA1A; HSPA1B; HSX70 Specification REACTIVITY: H M R Mk B SENSITIVITY: Endogenous MW (kDa): 72, 73 SOURCE: Rabbit