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HSP70 antibody (Heat Shock Protein 70)

Details for Product anti-HSP70 Antibody No. ABIN361820, Supplier: Log in to see
Antigen
  • APG-2
  • ARABIDOPSIS HEAT SHOCK PROTEIN 70
  • ATHSP70
  • CG5834
  • CG31354
  • chloroplast heat shock protein 70-2
  • cpHsc70-2
  • DmelCG5834
  • F19K16.12
  • F19K16_12
  • HEAT SHOCK PROTEIN 70
  • heat shock protein 70
  • HEAT SHOCK PROTEIN 70-7
  • HS24/P52
  • hsc70
  • HSC70-7
  • hsc71
  • hsp68
  • hsp70
  • Hsp70
  • HSP70
  • Hsp70-1
  • hsp70-5
  • Hsp70.1
  • hsp70B
  • HSP70B'
  • Hsp70Bb
  • hsp70Bb-prime
  • hsp70RY
  • Hsp110
  • HSPA1
  • HSPA6
  • HSPH2
  • irp94
  • K9P8.5
  • K9P8_5
  • LOC100305036
  • RY
Reactivity
Beluga, Carp, Coral, Cow (Bovine), Dog (Canine), Fish, Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Pig (Porcine), Plant, Rat (Rattus), Shark, Sheep (Ovine)
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Host
Rabbit
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292
40
18
Clonality
Polyclonal
Conjugate
This HSP70 antibody is un-conjugated
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Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
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90
74
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51
25
18
12
9
2
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Supplier
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Immunogen Full length protein HSP70
Specificity Detects a ~70 kDa. May cross-react with HSC70 at lower dilutions.
Purification Rabbit Antiserum
Alternative Name HSP70 (HSP70 Antibody Abstract)
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 50 % identity (1, 2). 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 (3). 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 (4). The structure of this ATPbinding domain displays multiple features of nucleotide binding proteins (5). 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 (6). 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.
Cellular Localization: Cytoplasm
Gene ID 3303
NCBI Accession NP_005336
UniProt P08107
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:10000), IHC (1:100), ICC/IF (1:100), IP (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Buffer Rabbit Antiserum
Storage -20 °C
Supplier Images
 image for anti-HSP70 antibody (Heat Shock Protein 70) (ABIN361820) Hsp70, human cell lines, polyclonal
 image for anti-HSP70 antibody (Heat Shock Protein 70) (ABIN361820) Hsp70, Pam212 cell lysate
Product cited in: Silverstein, Ordanes, Wylie, Files, Milligan, Presley, Kavanagh: "Inducing Muscle Heat Shock Protein 70 Improves Insulin Sensitivity and Muscular Performance in Aged Mice." in: The journals of gerontology. Series A, Biological sciences and medical sciences, Vol. 70, Issue 7, pp. 800-8, 2015 (PubMed).

Background publications 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, Pisano, Di Rosa: "Role of cyclopentenone prostaglandins in rat carrageenin pleurisy." in: FEBS letters, Vol. 508, Issue 1, pp. 61-6, 2001 (PubMed).

Trentin, Yin, Tahir, Lhotak, Farhang-Fallah, Li, Rozakis-Adcock: "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).

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).

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

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).

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).

DeLuca-Flaherty, McKay, Parham, Hill: "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).

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).