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Details for Product No. ABIN361820

Heat Shock Protein 70 (HSP70) antibody

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HSP70, hsc71, ARABIDOPSIS HEAT SHOCK PROTEIN 70, ATHSP70, heat shock protein 70, hsp70, hsp70-5, HEAT SHOCK PROTEIN 70, HEAT SHOCK PROTEIN 70-7, HSC70-7, K9P8.5, K9P8_5, chloroplast heat shock protein ... show more
»Alternatives Human, Mouse (Murine), Rat (Rattus), Beluga, Cow (Bovine), Dog (Canine), Crab, Guinea Pig, Hamster, Monkey, Pig (Porcine), Sheep (Ovine), Coral, Tomato (Solanum lycopersicum), Nicotiana benthamiana, Dogfish (Squalus), Atlantic Hagfish (Myxine glutinosa)
»Alternatives Rabbit
Clonality Polyclonal
»Alternatives Un-conjugated
»Alternatives Western Blotting (WB), Immunoprecipitation (IP), ELISA, Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunofluorescence (IF)
Pubmed 10 references available
Catalog no. ABIN361820
Quantity 25 µL
203.50 $   Plus shipping costs $45.00
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Immunogen Full length protein Hsp70
Isotype IgG
Specificity Detects a approx. 70 kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS PAGE immunoblots.
Cross-Reactivity (Details) May cross-react with Hsc70 at lower dilutions.
Alternative Name Hsp70
Background Synonyms:
Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B
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 ATPbinding 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.
Gene ID 3303
NCBI Accession NP_005336.3
UniProt P08107
Research Area Cancer, Heat Shock Proteins, Signaling
Application Notes Recommended Dilution: 1:25,000 (ECL) (WB), 1:100 (IP)
Restrictions For Research Use only
Background publications 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).

Welch, Suhan: "Cellular and biochemical events in mammalian cells during and after recovery from physiological stress." in: The Journal of cell biology, Vol. 103, Issue 5, pp. 2035-52, 1987 (PubMed).

Fink: "Chaperone-mediated protein folding." in: Physiological reviews, Vol. 79, Issue 2, pp. 425-49, 1999 (PubMed).

Trentin, Yin, Tahir et al.: "A mouse homologue of the Drosophila tumor suppressor l(2)tid gene defines a novel Ras GTPase-activating protein (RasGAP)-binding protein." in: The Journal of biological chemistry, Vol. 276, Issue 16, pp. 13087-95, 2001 (PubMed).

Hung, Skepper, Burton: "In vitro ischemia-reperfusion injury in term human placenta as a model for oxidative stress in pathological pregnancies." in: The American journal of pathology, Vol. 159, Issue 3, pp. 1031-43, 2001 (PubMed).

Ianaro, Ialenti, Maffia et al.: "Role of cyclopentenone prostaglandins in rat carrageenin pleurisy." in: FEBS letters, Vol. 508, Issue 1, pp. 61-6, 2001 (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).

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

Locke: "Heat shock transcription factor activation and hsp72 accumulation in aged skeletal muscle." in: Cell stress & chaperones, Vol. 5, Issue 1, pp. 45-51, 2000 (PubMed).

Alternatives for antigen "Heat Shock Protein 70 (HSP70)", type "Antibodies"
Hosts (154), (118), (3)
Reactivities (245), (130), (125), (80), (76), (56), (56), (45), (36), (35), (23), (22), (20), (19), (15), (13), (10), (9), (6), (6), (5), (5), (4), (4), (3), (3), (3), (3), (3), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Applications (207), (108), (80), (60), (53), (46), (44), (39), (24), (24), (5), (3), (3), (2), (2), (2), (2), (1), (1)
Conjugates (12), (10), (5), (5), (5), (5), (5), (4), (4), (4), (4), (1), (1)
Epitopes (25), (14), (14), (13), (12), (8), (3), (3), (3), (3), (1), (1), (1), (1), (1), (1), (1), (1)