Product Name:
HSP70
Product Number:
ab-nn060-3
Target Full Name: Heat shock 70 kDa protein 1A
Target Alias: Hsp70 1; Hsp70 2; Hsp70.1; Hsp72; Hsp73; HSPA1; HSPA1A; HSPA1B
Product Type Specific: HSP70 heat shock/stress protein pan-specific antibody
Antibody Code: NN060-3
Antibody Target Type: Pan-specific
Protein UniProt: P0DMV8
Protein SigNET: HSP70
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Immunogen Source: Full length human protein HSP70
Production Method: Rabbit antiserum
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Storage Buffer: Rabbit antiserum
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting, Immunoprecipitation, ELISA, Immunohistochemistry, ICC, Immunofluorescence
Antibody Dilution Recommended: 1:25,000 (ECL) (WB), 1:100 (IP)
Antibody Potency: Detects a ~70kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS-PAGE immunoblots.
Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Monkey | Beluga | Cow | Dog | Pig | Sheep | Guinea Pig | Rat | Mouse | Hamster | Fish (carp) | Spiny dogfish shark (Squalus acanthias) | Atlantic Hagfish (Myxine glutinosa) | Rainbow Trout | Tomato | Tobacco |Coral.
Antibody Positive Control: A 1:10,000 dilution of SPC-103 was sufficient for detection of hsp70 in 20μg of HeLa cell lysate by ECL immunoblot analysis.
Antibody Cross Reactivity: May cross-react with Hsc70 at lower dilutions.
Related Product 1: HSP70 pan-specific antibody (Cat. No.: AB-NN060-10)
Related Product 2: HSP70/HSC70 pan-specific antibody (Cat. No.: AB-NN060-11)
Related Product 3: HSP70/HSC70 pan-specific antibody (Cat. No.: AB-NN060-12)
Related Product 4: HSP70/HSC70 (pan) pan-specific antibody (Cat. No.: AB-NN060-13)
Related Product 5: HSP70 pan-specific antibody (Cat. No.: AB-NN060-2)
Related Product 6: HSP70 (Crab) pan-specific antibody (Cat. No.: AB-NN060-5)
Related Product 7: HSP70 (P. Falciparum) pan-specific antibody (Cat. No.: AB-NN060-6)
Related Product 8: HSP70 pan-specific antibody (Cat. No.: AB-NN060-7)
Related Product 9: HSP70 pan-specific antibody (Cat. No.: AB-NN060-8)
Related Product 10: HSP70 pan-specific antibody (Cat. No.: AB-NN060-9)
Scientific Background: HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family (1). They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. It assists in protein folding, stabilizes unfolded proteins to prevent aggregation, and handles misfolded proteins under stress conditions. Hsp70 is crucial for cellular repair, aiding in translocation and acting as an anti-apoptotic agent. The HSP70 genes show a high degree of conservation, having at least 5O% identity (2). The proteins features an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). They use ATP hydrolysis to bind (ADP-bound) and release (ATP-bound) substrates, aiding in their folding. When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Their polypeptide binding ability resides within the C-terminal half, and they bind to hydrophobic regions of unfolded proteins (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. This description may include information annotated by UniProt and/or Google AI.