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Heat Shock 70kDa Protein 8 (HSPA8) (AA 650-670) antibody

Details for Product No. ABIN361819, 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
AA 650-670
Hamster, Human, Mouse (Murine), Rat (Rattus)
BioImaging (BI), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
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Immunogen Amino acids 650-670 of human HSP73
Specificity Detects 73 kDa. Does not cross-react with 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 50 % identity (2). 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). 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 (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). 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 (6).
Cellular Localization: Cytoplasm | Melanosome
Gene ID 3312
NCBI Accession NP_006588
UniProt P11142
Research Area Metabolism, Heat Shock Proteins, Serum/Plasma Proteins
Application Notes Recommended Dilution: WB (1:2000), IHC (1:100), ICC/IF (1:250), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Buffer Rabbit Antiserum
Storage 4 °C
Supplier Images
Western Blotting (WB) image for anti-Heat Shock 70kDa Protein 8 (HSPA8) (AA 650-670) antibody (ABIN361819) Hsc70 human Cell line mix 10ug 1 in 1000 Western Blotting.
Product cited in: Preusse-Prange, Modrow, Schwark et al.: "Detection of constitutive and inducible HSP70 proteins in formalin fixed human brain tissue." in: Forensic science international, Vol. 235, pp. 62-7, 2014 (PubMed).

Gong, Kobayashi, Sugi et al.: "Characterization and binding analysis of a microneme adhesive repeat domain-containing protein from Toxoplasma gondii." in: Parasitology international, Vol. 63, Issue 2, pp. 381-8, 2014 (PubMed).

Hatakeyama, Dai, Harada et al.: "Connexin43 functions as a novel interacting partner of heat shock cognate protein 70." in: Scientific reports, Vol. 3, pp. 2719, 2013 (PubMed).

Zhang, Ciciriello, Anjos et al.: "Ouabain Mimics Low Temperature Rescue of F508del-CFTR in Cystic Fibrosis Epithelial Cells." in: Frontiers in pharmacology, Vol. 3, pp. 176, 2012 (PubMed).

Shiota, Kusakabe, Izumi et al.: "Heat shock cognate protein 70 is essential for Akt signaling in endothelial function." in: Arteriosclerosis, thrombosis, and vascular biology, Vol. 30, Issue 3, pp. 491-7, 2010 (PubMed).

Zwang, Hoffert, Pisitkun et al.: "Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry." in: Journal of proteome research, Vol. 8, Issue 3, pp. 1540-54, 2009 (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).

Brown, Martin, Hansen et al.: "The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion." in: The Journal of cell biology, Vol. 120, Issue 5, pp. 1101-12, 1993 (PubMed).

Cluett, Wood, Banta et al.: "Tubulation of Golgi membranes in vivo and in vitro in the absence of brefeldin A." in: The Journal of cell biology, Vol. 120, Issue 1, pp. 15-24, 1993 (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).