Heat Shock Protein Cognate 4 (HSC70-4) antibody

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BAP74, CG4264, Dmel\\CG4264, E(csp)1545, E(nd)195, HSC-70, HSC4, HSC70, HSC70-4, Hsc-4, Hsc4, Hsc4p, Hsc70, Hsp-c4, Hsp70, anon-WO0118547.237, bs17d06.y1, dhsc70, hsc4, hsc70, hsc70-4, hsp70, i190, l( ... show more
BAP74, CG4264, Dmel\\CG4264, E(csp)1545, E(nd)195, HSC-70, HSC4, HSC70, HSC70-4, Hsc-4, Hsc4, Hsc4p, Hsc70, Hsp-c4, Hsp70, anon-WO0118547.237, bs17d06.y1, dhsc70, hsc4, hsc70, hsc70-4, hsp70, i190, l(3)03550, l(3)L3929, l(3)j7A4, scd show less
Human, Rat (Rattus), Cow (Bovine), Caenorhabditis elegans (C. elegans), Beluga, Dog (Canine), Chicken, Fruit Fly (Drosophila melanogaster), Fish, Guinea Pig, Hamster, Monkey, Pig (Porcine), Cucumber, Pea (Pisum sativum), Rabbit, Sheep (Ovine), Xenopus laevis
(10), (10), (9), (9), (8), (8), (7), (7), (7), (6), (6), (6), (6), (5), (5), (4), (4), (4), (3), (3), (2), (1), (1), (1), (1), (1), (1), (1)
(13), (5)
Clonality (Clone)
Monoclonal ()
Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), Flow Cytometry (FACS), Immunoelectron Microscopy (IEM)
(18), (9), (5), (5), (5), (4), (3)
Pubmed 12 references available
Catalog no. ABIN361705
Quantity 50 µg
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Immunogen Recombinant Hsp70/hsc70
Clone N27F3-4
Isotype IgG
Specificity Detects 72 and 73 kDa proteins corresponding to the molecular mass of inducible Hsp and Hsc on SDS PAGE immunoblots.
Sensitivity 1 µg/mL of SMC-104 was sufficient for detection of Hsp70/Hsc70 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/Hsc70
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_005336.3
UniProt P08107
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: 1 µg/mL was sufficient for detection of hsp/hsc70 in 20 µg of HeLa lysate.
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 Cognate 4 (HSC70-4) antibody Hsp70 (N27), cell lines.
Product cited in: Sun, Prince, Manjarrez et al.: "Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins." in: Biochimica et biophysica acta, Vol. 1823, Issue 6, pp. 1092-101, 2012 (PubMed).

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).

Hang, Fox: "Expression of hsp70 induced in CHO cells by 45.0 degrees C hyperthermia is cell cycle associated and DNA synthesis dependent." in: Cytometry, Vol. 19, Issue 2, pp. 119-25, 1995 (PubMed).

Schnell, Kessler, Blobel: "Isolation of components of the chloroplast protein import machinery." in: Science (New York, N.Y.), Vol. 266, Issue 5187, pp. 1007-12, 1994 (PubMed).

Polanowska-Grabowska, Simon, Falchetto et al.: "Platelet adhesion to collagen under flow causes dissociation of a phosphoprotein complex of heat-shock proteins and protein phosphatase 1." in: Blood, Vol. 90, Issue 4, pp. 1516-26, 1997 (PubMed).

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

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

Ricart, Egea, Izquierdo et al.: "Subcellular structure containing mRNA for beta subunit of mitochondrial H+-ATP synthase in rat hepatocytes is translationally active." in: The Biochemical journal, Vol. 324 ( Pt 2), pp. 635-43, 1997 (PubMed).

Kabakov, Budagova, Latchman et al.: "Stressful preconditioning and HSP70 overexpression attenuate proteotoxicity of cellular ATP depletion." in: American journal of physiology. Cell physiology, Vol. 283, Issue 2, pp. C521-34, 2002 (PubMed).

Hosts (13), (5)
Reactivities (10), (10), (9), (9), (8), (8), (7), (7), (7), (6), (6), (6), (6), (5), (5), (4), (4), (4), (3), (3), (2), (1), (1), (1), (1), (1), (1), (1)
Applications (18), (9), (5), (5), (5), (4), (3)
Epitopes (1), (1), (1)
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