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HSP70 antibody (Heat Shock Protein 70) (C-Term)

Details for Product anti-HSP70 Antibody No. ABIN361870, 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
Epitope
C-Term
67
37
34
33
28
17
14
14
13
13
12
12
6
5
3
3
3
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Brook Trout, Salmon (Salmonidae)
642
306
299
143
130
126
126
88
79
78
74
69
66
64
57
53
42
41
39
38
35
22
22
20
19
18
18
17
8
6
5
5
4
3
3
3
3
3
3
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
Host
Rabbit
413
321
42
18
Clonality
Polyclonal
Conjugate
This HSP70 antibody is un-conjugated
34
34
24
24
22
22
20
19
19
19
19
19
19
19
19
19
19
12
11
8
7
5
5
5
5
5
5
5
5
5
3
3
3
3
3
3
1
1
1
Application
Western Blotting (WB)
693
342
288
278
269
252
158
110
58
51
29
18
16
12
9
5
2
2
1
1
1
1
Supplier
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Immunogen Synthetic peptide conjugated to KLH. Peptide sequence specific to C-terminal part of salmonid HSP70. The target is not present in any other HSP70 proteins.
Specificity Detects ~70 kDa. It does not cross react with HSC70. It does not detect HSP70 in other species.
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 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).
Cellular Localization: Cytoplasm
Gene ID 100196655
NCBI Accession NP_001135156
UniProt B5DG30
Research Area Cancer, Heat Shock Proteins, Signaling
Application Notes Recommended Dilution: WB (1:5000)
Optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Lyophilized
Storage -20 °C
Supplier Images
 image for anti-HSP70 antibody (Heat Shock Protein 70) (C-Term) (ABIN361870) Hsp70, Rainbow trout.
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).

Ings, Oakes, Vijayan, Servos: "Temporal changes in stress and tissue-specific metabolic responses to municipal wastewater effluent exposure in rainbow trout." in: Comparative biochemistry and physiology. Toxicology & pharmacology : CBP, Vol. 156, Issue 2, pp. 67-74, 2012 (PubMed).

Ings, Servos, Vijayan: "Hepatic transcriptomics and protein expression in rainbow trout exposed to municipal wastewater effluent." in: Environmental science & technology, Vol. 45, Issue 6, pp. 2368-76, 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).

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).