Heat Shock Protein 8 (HSPA8) antibody

Antigen: Heat Shock Protein 8 (HSPA8)

Synonyms: Hsc70, MGC114311, BiP, CG1579, Grp78, HSC-70, HSC3, HSC70, Hsc3p, anon-WO0138581.7, dhsc70, dmHsc72, hsc70-3, hsc72, l(1)G0102, l(1)G0111, l(1)G0292, l(1)G0341, l(1)G0407, l(1)G0466, DmelCG4147, CG4147, HSC5, l(2)k04907, DmelCG8542, CG8542, 143191_at, BcDNA:RH49358, HSC1, DmelCG8937, CG8937, 0041/12, 0318/20, 1342/17, 1348/02, 1485/13, BEST:LD32772, LD32772, anon-WO0118547.302, hsc70Cb, l(3)00082, l(3)07621, l(3)134217, l(3)148513, l(3)70Ca, l(3)70Cb, l(3)S134217, l(3)S134802, l(3)S148513, DmelCG6603, CG6603, HSC2, Hsc70.2, DmelCG7756, CG7756, HSPA10, MGC128130, hsc70, hsc70.I, MGC52655, MGC55272, wu:fb01g06, wu:fi48b06, ARABIDOPSIS THALIANA HEAT SHOCK COGNATE PROTEIN 70-1, AT-HSC70-1, HEAT SHOCK COGNATE PROTEIN 70, HEAT SHOCK COGNATE PROTEIN 70-1, HEAT SHOCK PROTEIN 70-1, HSC70-1, HSP70-1, T22P11.90, T22P11_90, hsc6, dyak_GLEANR_7992, DyakGE24282, GE24282, Hsc70-4, dsim_GLEANR_2803, DsimGD18998, GD18998, hspa1l, NV11212

Clonality: Monoclonal (1F2-H5)

Host: Mouse

Reactivity: Human, Mouse (Murine), Rat (Rattus)

Application: Western Blotting (WB), ELISA, Immunoprecipitation (IP), Immunohistochemistry (IHC)

Catalog no.: ABIN361800

Additional Information

Characteristics: Detects ~73kDa. Does not cross react with Hsp70

Alternative name: Hsc70 (Hsp73)

Gene ID: 3312

Swiss-Prot: P11142

Immunogen: Human Hsc70

Format: Liquid

Isotype: IgG2a kappa  (Matching secondary antibodies)

Clone: 1F2-H5

Description: 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 . 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. 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. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. 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.
Synonyms: Hsc54, Hsc71, Hsc73, Hsp71, Hsp73, HspA10, HspA8, LAP1, NIP71

Specificity: Detects 73kDa protein corresponding to the molecular mass of hsc70 on SDS PAGE immunoblots. Does not cross react with hsp70. Species cross-reactivity: Human, Mouse, Rat. Other species not yet tested.

Sensitivity: 1 µg/mL of SMC-151 was sufficient for detection of Hsc70 in 10µg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Synonyms: Hsc70, MGC114311, BiP, CG1579, Grp78, HSC-70, HSC3, HSC70, Hsc3p, anon-WO0138581.7, dhsc70, dmHsc72, hsc70-3, hsc72, l(1)G0102, l(1)G0111, l(1)G0292, l(1)G0341, l(1)G0407, l(1)G0466, DmelCG4147, CG4147, HSC5, l(2)k04907, DmelCG8542, CG8542, 143191_at, BcDNA:RH49358, HSC1, DmelCG8937, CG8937, 0041/12, 0318/20, 1342/17, 1348/02, 1485/13, BEST:LD32772, LD32772, anon-WO0118547.302, hsc70Cb, l(3)00082, l(3)07621, l(3)134217, l(3)148513, l(3)70Ca, l(3)70Cb, l(3)S134217, l(3)S134802, l(3)S148513, DmelCG6603, CG6603, HSC2, Hsc70.2, DmelCG7756, CG7756, HSPA10, MGC128130, hsc70, hsc70.I, MGC52655, MGC55272, wu:fb01g06, wu:fi48b06, ARABIDOPSIS THALIANA HEAT SHOCK COGNATE PROTEIN 70-1, AT-HSC70-1, HEAT SHOCK COGNATE PROTEIN 70, HEAT SHOCK COGNATE PROTEIN 70-1, HEAT SHOCK PROTEIN 70-1, HSC70-1, HSP70-1, T22P11.90, T22P11_90, hsc6, dyak_GLEANR_7992, DyakGE24282, GE24282, Hsc70-4, dsim_GLEANR_2803, DsimGD18998, GD18998, hspa1l, NV11212

Application Details

Application Notes: 1:1000 (WB)

Concentration: 1 mg/mL

Purification: Protein G Purified

Buffer: PBS pH7.4, 50% glycerol

Storage: -20 °C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Serum/Plasma Proteins, Heat Shock Proteins

Restrictions: For Research Use only

Images

Hsc70 (1F2-H5) human cell line mix(1), rHsp70 , rHsc70 (3)

Publications

Publications: 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).

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).

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).

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

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).