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Alternatives Western Blotting (WB), Immunofluorescence (IF)
|7 references available|
|Quantity||25µg (1mg/mL) (Variants)|
|Price||203.50 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 3 to 4 Business Days|
|Immunogen||His-tagged and purified PfHsp70, C-terminus|
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. 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. 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. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. 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. 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 pasrasite in different complexes with PfHsp90 and some PfHsp40.
Synonyms: HSP70_PLAFA, Cytoplasmic antigen 74.3 kDa protein
|Characteristics||Accession Number: M19753|
Detects an 70kD protein, corresponding to P.falciparum Hsp70 on SDS PAGE immunoblot, in samples from P.Falciparum origin.
It is species specific to P.falciparum, does not cross-rect to any protein from human erythrocytes.
|Application Notes||1:2000 (WB), 1:50 (IF)|
|Purity||Protein A affinity purified.|
|Purification||Protein A Purified|
|Buffer||PBS pH7.4, 50% glycerol|
|Preservative||0.09% sodium azide|
|Storage||Store at -20° C. Shipping Temperature: Blue Ice or 4° C|
|Research Area||Heat Shock Proteins|
|Restrictions||For Research Use only|
|PfHsp70, malarial parasite lysate.|
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).
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).
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).
Boorstein, Ziegelhoffer, Craig: "Molecular evolution of the HSP70 multigene family." in: Journal of molecular evolution, Vol. 38, Issue 1, pp. 1-17, 1994 (PubMed).
Fink: "Chaperone-mediated protein folding." in: Physiological reviews, Vol. 79, Issue 2, pp. 425-49, 1999 (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).
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).
|Applications||Immunofluorescence (IF) (1), Western Blotting (WB) (1)|