Product Name:
Hsc70 (HSP73)
Product Number:
ab-nn054-3
Target Full Name: Heat shock cognate 71 kDa protein
Target Alias: Hsc54; Hsc71; Hsc73; Hsp71; Hsp73; HspA10; HspA8; LAP1; NIP71
Product Type Specific: HSP70 heat shock/stress protein pan-specific antibody
Antibody Code: NN054-3
Antibody Target Type: Pan specific
Protein UniProt: P11142
Protein SigNET: Hsc70 (HSP73)
Antibody Type: Monoclonal
Antibody Host Species: Mouse
Antibody Ig Isotype Clone: 1F2-H5/IgG2a Kappa
Antibody Immunogen Source: Human HSC70
Production Method: Protein G purified
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Antibody Concentration: 1 mg/ml
Storage Buffer: Phosphate buffered saline, pH 7.4, 50% glycerol, 0.09% sodium azide
Storage Conditions: -20°C
Storage Stability: > 1 year
Product Use: Western blotting, Enzyme-linked immunosorbent assays (ELISA), Immunoprecipitation (IP), Immunohistochemistry (IHC)
Antibody Potency: Very strong
Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Rat | Mouse.
Antibody Specificity: Very high
Antibody Cross Reactivity: Target protein strongly detected in only rat testes. No detectable cross-reactivities in test blots.
Related Product 1: Hsc70 (Hsp73) expression antibody (Cat. No.: AB-NN054-2)
Related Product 2: HSC70 (HSP73) expression antibody (Cat. No.: AB-NN054-4)
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.