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Heat Shock 70kDa Protein 8 (HSPA8) antibody

Details for Product No. ABIN361860, Supplier: Log in to see
  • hsc54
  • hsc70
  • hsc71
  • hsp71
  • hsp73
  • hspa10
  • lap1
  • nip71
  • HSC54
  • HSC70
  • HSC71
  • HSP71
  • HSP73
  • HSPA10
  • LAP1
  • NIP71
  • Hsc70
  • 2410008N15Rik
  • Hsc71
  • Hsc73
  • Hsp73
  • Hspa10
  • wu:fb01g06
  • wu:fi48b06
Salmon (Salmonidae)
Western Blotting (WB)
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Immunogen Synthetic peptide conjugated to KLH. The peptide target is specific to the HSC70 of salmonid fish.
Specificity Detects ~73 kDa. The antibody detects HSC70, but not HSP70.
Purification Rabbit antiserum
Background HSP70 genes encode abundant heat-inducible 70- kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (1). 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 (2). 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. Polypeptide binding ability therefore resided within the C-terminal half (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed, HSP 70 is highly related to HSC70 (>90 % sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (5).
Cellular Localization: Cytoplasm | Melanosome
Gene ID 100194521
NCBI Accession NP_001133079
UniProt B5DFX7
Research Area Signaling, Heat Shock Proteins, Serum/Plasma Proteins
Application Notes Recommended Dilution: WB (1:5000)
Optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Lyophilized
Storage -20 °C
Supplier Images
 image for anti-Heat Shock 70kDa Protein 8 (HSPA8) antibody (ABIN361860) Salmon.
Product cited in: Teigen, Orczewska, McLaughlin et al.: "Cold acclimation increases levels of some heat shock protein and sirtuin isoforms in threespine stickleback." in: Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, Vol. 188, pp. 139-47, 2015 (PubMed).

Background publications Brown, Hong-Brown, Doxsey et al.: "Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment." in: The Journal of biological chemistry, Vol. 271, Issue 2, pp. 833-40, 1996 (PubMed).

Boorstein, Ziegelhoffer, Craig: "Molecular evolution of the HSP70 multigene family." in: Journal of molecular evolution, Vol. 38, Issue 1, pp. 1-17, 1994 (PubMed).

Rothman: "Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells." in: Cell, Vol. 59, Issue 4, pp. 591-601, 1990 (PubMed).

DeLuca-Flaherty, McKay, Parham et al.: "Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis." in: Cell, Vol. 62, Issue 5, pp. 875-87, 1990 (PubMed).

Bork, Sander, Valencia: "An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 16, pp. 7290-4, 1992 (PubMed).