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Heat Shock 70 KDa (HSP70) antibody

Antigen

Heat Shock 70 KDa (HSP70)

Synonyms BIP, MIF2, GRP78, FLJ26106, Bip, Sez7, mBiP, Grp78, SEZ-7, Hsce70, AL022860, AU019543, D2Wsu17e, D2Wsu141e, hspa5a
Clonality Polyclonal
Host
Alternatives

Rabbit

Reactivity
Alternatives

Salmon (Salmonidae), Brook Trout

Application
Alternatives Western Blotting (WB), Immunoprecipitation (IP)
5 references available
Catalog no. ABIN361871
Quantity 200ug  (Variants)
Price 389.00 $   Plus shipping costs $35.00
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Availability Ships within 5 to 7 Business Days

Additional Information

Alternative name Hsp70
Immunogen Synthetic peptide conjugated to KLH. Peptide sequence specific to C-terminal part of salmonid Hsp70. The target is not present in any other Hsp70 proteins.
Format Affinity-purified
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 (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 ATPbinding 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).
Specificity Detects ~70kDa. Species cross-reactivity: Rainbow trout. This antibody is specific for salmonid Hsp70 (tested on salmon and brooktrout). It does not cross-react with Hsc70. It does not detect Hsp70 in other species.

Application Details

Application Notes Working dilution Recommended dilution for WB 1:1000 (needs to be optimized depending on the system used) IP: 5ug
Buffer Affinity Purified Rabbit IgG, Lyophilized in PBS pH7.4. (For reconstitution add 200uL of sterile water).
Storage -20°C, 1 year+, shipped on cold packs or ambient
Research Area Cancer, Heat Shock Proteins, Signaling
Restrictions For Research Use only

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, 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).