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HSPA8 antibody (Heat Shock 70kDa Protein 8)

Details for Product anti-HSPA8 Antibody No. ABIN361801, Supplier: Log in to see
Antigen
  • hsc54
  • hsc70
  • hsc71
  • hsp71
  • hsp73
  • hspa10
  • lap1
  • nip71
  • HSC54
  • HSC70
  • HSC71
  • HSP71
  • HSP73
  • HSPA10
  • LAP1
  • NIP71
  • Hsc70
  • 2410008N15Rik
  • Hsc71
  • Hsc73
  • Hsp73
  • Hspa10
  • wu:fb01g06
  • wu:fi48b06
  • heat shock 70kDa protein 8
  • heat shock protein 8
  • hspa8
  • HSPA8
  • Hspa8
Reactivity
Human, Mouse (Murine), Rat (Rattus)
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46
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36
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30
26
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20
5
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4
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2
2
2
2
2
2
1
1
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Host
Mouse
137
95
22
12
Clonality (Clone)
Monoclonal ()
Conjugate
This HSPA8 antibody is un-conjugated
17
14
7
6
6
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5
5
5
5
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3
3
2
1
Application
Antibody Array (AA), Binding Studies (Bind), ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Proximity Ligation Assay (PLA), Western Blotting (WB)
255
136
119
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60
59
37
19
18
18
18
16
9
7
3
3
1
1
1
Options
Supplier
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Immunogen Full length human HSC70
Clone 1F2-H5
Isotype IgG2a kappa
Specificity Detects ~73 kDa. Does not cross react with HSP70.
Sensitivity 1 µg/mL of SMC-151 was sufficient for detection of Hsc70 in 10 µg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Alternative Name HSC70 (HSP73) (HSPA8 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 (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 ATP binding domain displays multiple features of nucleotide binding proteins (5). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed, HSP 70 is highly related to HSC70 (>90 % sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).
Gene ID 3312
NCBI Accession NP_006588
UniProt P11142
Application Notes
  • WB (1:1000)
  • ICC/IF (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

1 μg/ml of SMC-151 was sufficient for detection of HSC70 in 10 μg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-HSPA8 antibody (Heat Shock 70kDa Protein 8) (ABIN361801) Hsc70 (1F2 H5) human cell line mix copy.
Product cited in: Katoh, Kubota, Kita, Nakatsu, Aoki, Mori, Maenaka, Takeda, Kidokoro: "Heat shock protein 70 regulates degradation of the mumps virus phosphoprotein via the ubiquitin-proteasome pathway." in: Journal of virology, Vol. 89, Issue 6, pp. 3188-99, 2015 (PubMed).

Shimomura, Imai, Nashida: "Characterization of cysteine string protein in rat parotid acinar cells." in: Archives of biochemistry and biophysics, Vol. 538, Issue 1, pp. 1-5, 2013 (PubMed).

Baaklini, Wong, Hantouche, Patel, Shrier, Young: "The DNAJA2 substrate release mechanism is essential for chaperone-mediated folding." in: The Journal of biological chemistry, Vol. 287, Issue 50, pp. 41939-54, 2012 (PubMed).

Kawano, Oke, Nomura, Fujita, Ohira, Nakai, Ohira: "Responses of HSC70 expression in diencephalon to iron deficiency anemia in rats." in: The journal of physiological sciences : JPS, Vol. 61, Issue 6, pp. 445-56, 2011 (PubMed).

Background publications Brown, Hong-Brown, Doxsey, Welch: "Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment." in: The Journal of biological chemistry, Vol. 271, Issue 2, pp. 833-40, 1996 (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).

Brown, Martin, Hansen, Beckmann, Welch: "The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion." in: The Journal of cell biology, Vol. 120, Issue 5, pp. 1101-12, 1993 (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).