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Heat Shock 70kDa Protein 8 (HSPA8) antibody

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Synonyms 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
Artemia sp. (Brine shrimp), Beluga, Cow (Bovine), Dog (Canine), Chicken, Fruit Fly (Drosophila melanogaster), Fish, Guinea Pig, Hamster, Human, Mouse (Murine), Oyster, Pig (Porcine), Rabbit, Rat (Rattus), Scallop, Sheep (Ovine), Xenopus laevis, Yeast
(186), (105), (98), (33), (21), (19), (16), (11), (9), (8), (8), (7), (6), (6), (4), (4), (3), (3), (3), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1)
(136), (60), (22), (13)
Clonality (Clone)
Monoclonal ()
(15), (12), (5), (4), (4), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (1)
Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB)
(198), (107), (101), (84), (58), (57), (31), (19), (17), (17), (15), (4), (3), (3), (2), (2)
Pubmed 9 references available
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Quantity 0.2 mg
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Immunogen Chicken Hsp70/Hsp90 complex (1)
Clone BB70
Isotype IgG2a
Specificity Detects 72 and 73 kDa proteins corresponding to the Molecular Mass of inducible HSP and HSC70 on SDS PAGE Immunoblots.
Characteristics Synonyms: HSP73, HSPA10, Heat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8
Purification Affinity Chromatography on Protein G
Alternative Name HSPA8 / HSC70 (HSPA8 Antibody Abstract)
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 (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). All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. 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.Synonyms: HSP73, HSPA10, Heat shock 70 kDa protein 8, Heat shock cognate 71 kDa protein
Gene ID 3312
UniProt P11142
Application Notes Western blot (7): 1 μg/mL was sufficient for detection of hsp70/Hsc70 in 20 g of HeLalysate.
Restrictions For Research Use only
Concentration 1.0 mg/mL
Buffer PBS pH 7.2, 0.09 % Sodium Azide, 50 % Glycerol
Preservative Sodium azide
Precaution of Use WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store the antibody at 2 - 8 °C up to one month or (in aliquots) at -20 °C for longer.
Shelf life: one year from despatch.
Expiry Date 12 months
Background publications Rice, Zhang, Chen et al.: "Differential, phosphorylation dependent trafficking of AQP2 in LLC-PK1 cells." in: PLoS ONE, Vol. 7, Issue 2, pp. e32843, 2012 (PubMed).

Fernandez-Funez, Nino-Rosales, de Gouyon et al.: "Identification of genes that modify ataxin-1-induced neurodegeneration." in: Nature, Vol. 408, Issue 6808, pp. 101-6, 2000 (PubMed).

Fink: "Chaperone-mediated protein folding." in: Physiological reviews, Vol. 79, Issue 2, pp. 425-49, 1999 (PubMed).

Zou, Guo, Guettouche et al.: "Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1." in: Cell, Vol. 94, Issue 4, pp. 471-80, 1998 (PubMed).

Prapapanich, Chen, Toran et al.: "Mutational analysis of the hsp70-interacting protein Hip." in: Molecular and cellular biology, Vol. 16, Issue 11, pp. 6200-7, 1996 (PubMed).

Smith, Sullivan, Marion et al.: "Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70." in: Molecular and cellular biology, Vol. 13, Issue 2, pp. 869-76, 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).

Catalog No. ABIN263941
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