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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
  • HSP70
  • HEAT SHOCK PROTEIN 70
  • HEAT SHOCK PROTEIN 70-7
  • HSC70-7
  • K9P8.5
  • K9P8_5
  • chloroplast heat shock protein 70-2
  • cpHsc70-2
  • F19K16.12
  • F19K16_12
  • LOC100305036
  • hsc70
  • CG31354
  • Hsp70Bb
  • hsp70B
  • hsp70Bb-prime
  • DmelCG5834
  • CG5834
  • APG-2
  • HS24/P52
  • HSPH2
  • RY
  • hsp70
  • hsp70RY
  • hsc71
  • Hsp70
  • Hsp70-1
  • Hsp70.1
  • hsp68
  • Hsp110
  • irp94
  • HSPA1
  • HSP70B'
  • HSPA6
  • ARABIDOPSIS HEAT SHOCK PROTEIN 70
  • ATHSP70
  • heat shock protein 70
  • hsp70-5
  • heat shock 70 kD protein cognate
  • heat shock protein 70-2
  • Heat shock protein 70
  • heat shock protein 70
  • CG5834 gene product from transcript CG5834-RA
  • heat shock 70kDa protein 1A
  • heat shock 70kDa protein 2
  • heat shock 70kDa protein 4
  • heat shock cognate protein 70a
  • heat shock protein 1B
  • heat shock protein 4
  • heat shock protein 70-4
  • heat shock protein1
  • Protein HSP-70
  • LOC692373
  • CPHSC70-2EAT SHOCK PROTEIN 70-2
  • AT1G79920
  • HSP70
  • PCC7424_2419
  • Isop_1041
  • CGB_C3390W
  • Bacsa_1698
  • dnaK-B
  • LOC100305036
  • Hsp70Bbb
  • HSPA1A
  • HSPA2
  • HSPA4
  • hsc70a
  • Hspa1b
  • Hspa4
  • hsp1
  • hsp-70
Epitope
C-Term
42
35
31
20
20
18
17
15
15
12
3
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
1
1
Reactivity
Fish, Salmon (Salmonidae)
627
431
430
203
189
177
172
151
117
113
104
103
97
87
87
76
59
55
51
39
39
36
26
25
20
20
18
17
9
8
5
5
4
4
3
3
3
3
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Host
Rabbit
386
310
41
19
Clonality
Polyclonal
Conjugate
This HSP70 antibody is un-conjugated
35
34
25
23
22
21
20
20
20
20
20
20
20
20
20
20
11
9
7
6
5
5
5
5
5
5
4
4
4
3
3
2
Application
Western Blotting (WB)
672
296
286
279
264
239
149
107
72
62
51
26
19
11
9
4
2
2
1
Options
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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). Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
Gene ID 100196655
NCBI Accession NP_001135156
UniProt B5DG30
Research Area Heat Shock Proteins
Application Notes
  • WB (1:5000)
  • optimal dilutions for assays should be determined by the user.
Comment

0.2 μl/ml of SPC-313 was sufficient for detection of HSP70 in 20 μg of heat shocked (25°C) rainbow trout cytoplasmic fraction lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

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-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).