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HSP70 antibody (Heat Shock Protein 70) (AA 365-681)

Details for Product anti-HSP70 Antibody No. ABIN361729, Supplier: Log in to see
Antigen
Epitope
AA 365-681, C-Term
55
36
34
26
17
15
13
13
12
4
4
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
Plasmodium falciparum
550
256
254
110
108
97
94
70
62
59
58
56
53
48
47
40
38
35
35
25
24
22
20
18
18
18
8
6
6
5
4
4
4
3
3
3
3
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
Host
Rabbit
355
291
40
18
Clonality
Polyclonal
Conjugate
This HSP70 antibody is un-conjugated
32
32
24
21
21
19
19
19
19
19
19
19
19
19
19
19
17
7
6
5
5
5
5
5
5
5
2
1
1
1
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB)
618
275
251
250
237
218
90
75
55
51
25
18
12
9
3
2
2
1
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Immunogen His-tagged and purified PfHSP70, C-terminus (AA 365-681)
Specificity Detects ~ 70 kDa. Specific to P. Falciparum and does not cross-react to any protein from Human erythrocytes.
Purification Protein A Purified
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). 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 (5). 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. PfHSP70-I (PF08_0054) is the major cytosolic HSP70 in Plasmodium falciparum. It is abundantly expressed in the blood stages of the parasite and is thought to constitute 1-2 % of total parasite protein. It is induced upon heat shock. It is present in the parasite in different complexes with PfHSP90 and some PfHSP40 (6, 7).
Cellular Localization: Cytoplasm
UniProt P11144
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:2000), ICC/IF (1:50), optimal dilutions for assays should be determined by the user.
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-HSP70 antibody (Heat Shock Protein 70) (AA 365-681) (ABIN361729) PfHsp70, malarial parasite lysate.
Product cited in: Boes, Spiegel, Voepel et al.: "Analysis of a Multi-component Multi-stage Malaria Vaccine Candidate-Tackling the Cocktail Challenge." in: PLoS ONE, Vol. 10, Issue 7, pp. e0131456, 2015 (PubMed).

Goel, Palmkvist, Moll et al.: "RIFINs are adhesins implicated in severe Plasmodium falciparum malaria." in: Nature medicine, Vol. 21, Issue 4, pp. 314-7, 2015 (PubMed).

Sanz, Bandini, Ospina et al.: "Biosynthesis of GDP-fucose and other sugar nucleotides in the blood stages of Plasmodium falciparum." in: The Journal of biological chemistry, Vol. 288, Issue 23, pp. 16506-17, 2013 (PubMed).

Background publications Pesce, Acharya, Tatu et al.: "The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns." in: The international journal of biochemistry & cell biology, Vol. 40, Issue 12, pp. 2914-26, 2008 (PubMed).

Pavithra, Banumathy, Joy et al.: "Recurrent fever promotes Plasmodium falciparum development in human erythrocytes." in: The Journal of biological chemistry, Vol. 279, Issue 45, pp. 46692-9, 2004 (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).

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 et al.: "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).

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).