CST, 67399T, HSP70 (F2E4X) Rabbit Monoclonal Antibody

Monoclonal Antibody for studying HSP70. Validated for Western Blotting,Simple Western™,Immunohistochemistry (Paraffin). Available in 2 sizes. Highly specific and rigorously validated in-house, HSP70 (F2E4X) Rabbit Monoclonal Antibody (CST #67399) is ready to ship. Product Usage Information Western Blotting: 1:1000 Simple Western™: 1:50 - 1:250 Immunohistochemistry (Paraffin): 1:100 - 1:400 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting, Immunohistochemistry (Paraffin) Specificity / Sensitivity HSP70 (F2E4X) Rabbit Monoclonal Antibody recognizes endogenous levels of total HSP70 protein. This antibody does not cross-react with Heat shock-related 70 kDa protein 2 (HSPA2) or Heat shock cognate 71 kDa protein (HSC70/HSPA8). This antibody detects a 230 kDa protein of unknown identity in some cell lines. This antibody is not recommended for immunohistochemical analysis of mouse tissues. Species Reactivity: Human, Mouse, Rat, Monkey Source / Purification Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human HSP70 protein. 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 SENSITIVITY: Endogenous MW (kDa): 70 Source/Isotype: Rabbit IgG