Application Note: Anti-Hsp70 Antibody has been tested in WB, IHC, IF microscopy, IP and is suitable for use in ELISA. Expect a band approximately ~70kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS PAGE immunoblots. May cross-react with Hsc70 at lower dilutions. Specific conditions for reactivity should be optimized by the end user.
Concentration Value: 85 mg/mL
ELISA Dilution: 1:200
Immunohistochemistry Dilution: User Optimized
IF Microscopy Dilution: User Optimized
Immunoprecipitation Dilution: 1:100
Western Blot Dilution: 1:25,000
General Disclaimer Note: This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.
Immunogen: Hsp70 Antibody was produced from whole rabbit serum prepared by repeated immunizations raised against full length protein Hsp70.
Physical State: Liquid (sterile filtered)
Purity and Specificity: Anti-Hsp70 Antibody was prepared from monospecific antiserum by delipidation and defibrination. A BLAST analysis was used to suggest cross-reactivity with Hsp70 from Human, mouse, rat, beluga, cow, dog, fish (carp), guinea pig, hamster, monkey, pig, sheep, coral, tomato, tobacco, spiny dogfish shark (Squalus acanthias), and Atlantic Hagfish (Myxine glutinosa) based on 100% homology with the immunizing sequence. Cross-reactivity with Hsp70 from other sources has not been determined. Heat Shock research.
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. 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.
Low Endotoxin: No
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