Product Name:
HSP70/HSC70
Product Number:
ab-nn060-12
Target Full Name: Heat shock-related 70 kDa protein 2
Target Alias: HSC54; HSC70; HSC71; HSP70 1; HSP701/HSP70 2; HSP70.1; HSP71; HSP72; HSP73; HSPA1; HSPA10; HSPA1A; HSPA1B; LAP1; NIP71
Product Type Specific: HSP70 heat shock/stress protein pan-specific antibody
Antibody Code: NN060-12
Antibody Target Type: Pan-specific
Protein UniProt: P54652
Protein SigNET: HSP70/HSC70
Antibody Type: Monoclonal
Antibody Host Species: Mouse
Antibody Ig Isotype Clone: IgG2a
Antibody Immunogen Source: Chicken HSP70/HSP90 complex (Uniprot IDs P08106 and Q04619)
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 pH7.2, 50% glycerol, 0.09% sodium azide
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 | Immunohistochemistry | Immunoprecipitation
Antibody Dilution Recommended: WB (1:1000), ICC/IF (1:200); optimal dilutions for assays should be determined by the user.
Antibody Potency: Very high potency. Detects a ~72 (HSP) and ~73 kDa protein (HSC) in cell and tissue lysates by Western blotting.
Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Monkey | Beluga | Cow | Scallop pig | Dog | Rabbit | Sheep | Guinea pig | Rat | Hamster | Mouse | Chicken | Fish | Frog | Fruit fly | Nematode worm | Plant.
Antibody Positive Control: 1 µg/ml of SMC-106 was sufficient for detection of HSP70 and HSC70 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Antibody Specificity: Very high
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) pan-specific antibody (Cat. No.: AB-NN060-13)
Related Product 4: HSP70 pan-specific antibody (Cat. No.: AB-NN060-2)
Related Product 5: HSP70 pan-specific antibody (Cat. No.: AB-NN060-3)
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)
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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.