Heat Shock Protein 70 (HSP70) antibody

Details for Product No. ABIN361735
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Antigen
Synonyms
HSP70, HEAT SHOCK PROTEIN 70, HEAT SHOCK PROTEIN 70-7, HSC70-7, K9P8.5, K9P8_5, chloroplast heat shock protein 70-2, cpHsc70-2, F19K16.12, F19K16_12, LOC100305036, hsc70, CG31354, Hsp70Bb, hsp70B, hsp ... show more
HSP70, HEAT SHOCK PROTEIN 70, HEAT SHOCK PROTEIN 70-7, HSC70-7, K9P8.5, K9P8_5, chloroplast heat shock protein 70-2, cpHsc70-2, F19K16.12, F19K16_12, LOC100305036, hsc70, CG31354, Hsp70Bb, hsp70B, hsp70Bb-prime, DmelCG5834, CG5834, APG-2, HS24/P52, HSPH2, RY, hsp70, hsp70RY, hsc71, Hsp70, Hsp70-1, Hsp70.1, hsp68, Hsp110, irp94, HSPA1, HSP70B', HSPA6, ARABIDOPSIS HEAT SHOCK PROTEIN 70, ATHSP70, heat shock protein 70, hsp70-5 show less
Reactivity
Human, Rat (Rattus), Amphibian, Chicken, Fish, Yeast (Saccharomyces cerevisiae), Fruit Fly (Drosophila melanogaster)
(413), (144), (139), (111), (92), (58), (58), (43), (30), (29), (23), (23), (23), (22), (18), (16), (11), (9), (8), (8), (7), (6), (6), (6), (5), (4), (4), (4), (4), (3), (3), (3), (3), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Host
Mouse
(259), (239), (21)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(26), (22), (13), (11), (10), (9), (9), (9), (9), (9), (9), (9), (9), (9), (9), (9), (9), (6), (6), (6), (6), (6), (6), (6), (6), (4), (3), (1), (1), (1), (1), (1), (1)
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blotting (WB), Immunoprecipitation (IP)
(416), (168), (150), (137), (115), (106), (87), (85), (60), (36), (26), (4), (3), (2), (2), (2), (1), (1)
Pubmed 6 references available
Quantity 25 μg
Options
Shipping to United States (Change)
Availability Will be delivered in 3 to 4 Business Days
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Catalog No. ABIN361735
213.40 $
Plus shipping costs $45.00

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen Human Recombinant Hsp70 overexpressed in E.coli
Clone 5A5
Isotype IgG1
Specificity Detects several members of the heat shock protein 70 kDa gene family including Hsp70, Hsc70, Grp78 and following heat shock, Hsp72. IF staining of Hsp70 in heat shocked HeLa cells results in cytoplasmic staining.
Sensitivity 1 µg/mL of SMC-162 was sufficient for detection of Hsp70 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Alternative Name Hsp70
Background Synonyms:
Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, 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 proteinsand 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.
Gene ID 3303
NCBI Accession NP_005336
UniProt P08107
Research Area Cancer, Heat Shock Proteins, Signaling
Application Notes Recommended Dilution: ICC/IF: 1/500, WB: 1/1000 (ECL), IP: 1 µg
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Storage -20 °C
Supplier Images
anti-Heat Shock Protein 70 (HSP70) antibody Hsp70 (5A5), rat lysate
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).

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

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

Balashova, Chang, Lamothe et al.: "Characterization of a novel type of endogenous activator of soluble guanylyl cyclase." in: The Journal of biological chemistry, Vol. 280, Issue 3, pp. 2186-96, 2005 (PubMed).

General 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).

Validation Images
Did you look for something else?
back to top