Product Name:

Hsc70 (Hsp73)


Product Number:

ab-nn054-2

Price:

Regular price
$89.00
Regular price
Sale price
$89.00

Download Product PDF

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: NN054-2

Antibody Target Type: Pan-specific

Protein UniProt: P11142

Protein SigNET: Hsc70 (Hsp73)

Antibody Type: Polyclonal

Antibody Host Species: Rabbit

Antibody Immunogen Source: Human HSC70

Antibody Immunogen Sequence: PGGMPGGFPGGGAPPSGGAS

Antibody Immunogen Description: Corresponds to amino acid residues P618-S637.

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.

Antibody Dilution Recommended: 1:1500-2000 (WB), 1:250 (IF)

Antibody Potency: Detects a 73 kDa protein corresponding to the molecular mass of hsc70 on SDS-PAGE immunoblots. Does not cross-react with hsp70.

Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Dog | Hamster | Rat.

Antibody Positive Control: 0.5 μg/ml of SPC-102 was sufficient for detection of Hsc70 20μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Antibody Cross Reactivity: Does not cross-react with hsp70.

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.