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Antigenic Specificity | Hsp70/Hsc70 |
Clone | BB70 |
Host Species | Mouse |
Reactive Species | human, mouse, rat, beluga, bovine, chicken, d. melanogaster, dog, fish, guinea pig, hamster, porcine, rabbit, scallop, sheep, Xenopus, yeast |
Isotype | IgG2a |
Format | Protein G purified |
Size | 200 µg |
Concentration | 1 mg/mL |
Applications | Immunohistochemistry, Immunoprecipitation, Western Blot |
Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
Description | Anti-Hsp70/Hsc70 Antibody was purified by Protein G chromatography. A BLAST analysis was used to suggest cross-reactivity with Hsp70/Hsc70 from Human, Mouse, Rat, Sheep, Dog, Beluga, Bovine, Fish, Guinea pig, Scallop pig, Hamster, Rabbit, Chicken, Xenopus, Drosophila, Yeast sources based on 100% homology with the immunizing sequence. Cross-reactivity with Hsp70/Hsc70 from other sources has not been determined. Heat Shock research. 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.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. 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. |
Immunogen | Hsp70/Hsc70 Antibody was produced in mice by repeated immunizations raised against chicken Hsp70/Hsp90 complex. |
Other Names | Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B, Heat shock 70 kDa protein 1A/1B, Heat shock 70 kDa protein 1/2, HSP70-1/HSP70-2 |
Gene, Accession # | HSPA1A, Gene ID: 3303, NCBI: NP_005336.3, UniProt: P0DMV8 |
Catalog # | 200-301-F64 |
Price | $485 |
Order / More Info | Hsp70/Hsc70 Antibody from ROCKLAND IMMUNOCHEMICALS INC. |
Product Specific References | n/a |