HSPA8 antibody (Heat Shock 70kDa Protein 8)

Details for Product anti-HSPA8 Antibody No. ABIN361860, 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
Fish, Salmon (Salmonidae)
214
163
156
57
56
45
42
38
36
35
28
26
25
23
23
22
20
20
6
6
5
3
2
2
2
2
2
2
2
2
1
1
1
Host
Rabbit
136
95
20
12
Clonality
Polyclonal
Conjugate
This HSPA8 antibody is un-conjugated
17
14
7
6
6
5
5
5
5
5
5
5
5
5
4
3
3
2
1
Application
Western Blotting (WB)
251
135
118
110
60
58
37
18
18
18
18
16
9
7
3
3
1
1
1
1
Options
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Immunogen Synthetic peptide conjugated to KLH. The peptide target is specific to the HSC70 of salmonid fish.
Specificity Detects ~73 kDa. The antibody detects HSC70, but not HSP70.
Purification Rabbit Antiserum
Alternative Name HSC70 (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 5O% identity (1). 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 (2). 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 (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). 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 (5).
Gene ID 100194521
NCBI Accession NP_001133079
UniProt B5DFX7
Research Area Heat Shock Proteins, Serum/Plasma Proteins, Metabolism
Application Notes
  • WB (1:1000)
  • optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Lyophilized
Buffer Lyophilized rabbit Antiserum. For reconstitution add 100 μL of sterile water.
Storage -20 °C
Supplier Images
 image for anti-HSPA8 antibody (Heat Shock 70kDa Protein 8) (ABIN361860) Salmon.
Product cited in: Teigen, Orczewska, McLaughlin, OBrien: "Cold acclimation increases levels of some heat shock protein and sirtuin isoforms in threespine stickleback." in: Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, Vol. 188, pp. 139-47, 2015 (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).

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).