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Heat Shock 70kDa Protein 8 (HSPA8) (AA 618-637) 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
AA 618-637
(24), (23), (18), (12), (9), (6), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Hamster, Human, Rat (Rattus)
(186), (105), (99), (33), (22), (20), (17), (12), (9), (9), (9), (8), (7), (6), (5), (4), (4), (4), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1)
(135), (61), (22), (13)
(15), (12), (5), (4), (4), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (3), (1)
Functional Studies (Func), Immunofluorescence (IF), Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunoprecipitation (IP), Western Blotting (WB)
(198), (107), (101), (84), (58), (57), (30), (19), (17), (17), (15), (4), (3), (3), (2), (1)
Pubmed 6 references available
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Immunogen Amino acids 618-637 of Human HSC70 (1)
Specificity Detects 73 kDa protein corresponding to the Molecular Mass of HSC70 on SDS PAGE immunoblots. Does not cross react with HSP70.
Purification Serum
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). 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).Synonyms: HSP73, HSPA10, Heat shock 70 kDa protein 8, Heat shock cognate 71 kDa protein
Gene ID 3312
NCBI Accession NP_006588
UniProt P11142
Application Notes Western blot (1): 1: 1500 to 1: 2000. Immunoprecipitastion (1). Immunoflourescence (1,6). Functional assays (6). Immunohistochemistry on frozen sections.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer.
Supplier Images
 image for anti-Heat Shock 70kDa Protein 8 (HSPA8) (AA 618-637) antibody (ABIN264846) anti-Heat Shock 70kDa Protein 8 (HSPA8) (AA 618-637) antibody
 image for anti-Heat Shock 70kDa Protein 8 (HSPA8) (AA 618-637) antibody (ABIN264846) anti-Heat Shock 70kDa Protein 8 (HSPA8) (AA 618-637) antibody (Image 2)
Background publications 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).

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).

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).

Catalog No. ABIN264846
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