Add to Basket
|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Heat Shock 70kDa Protein 4 (HSPA4) antibody (FITC)
Human, Mouse (Murine), Rat (Rattus), Cow (Bovine), Dog (Canine), Chicken, Fruit Fly (Drosophila melanogaster), Carp, Guinea Pig, Hamster, Monkey, Pig (Porcine), Rabbit, Sheep (Ovine)
Alternatives Flow Cytometry (FACS)
|12 references available|
|Price||211.20 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 3 to 4 Business Days|
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.
Synonyms: Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B
|Characteristics||Accession Number: NP_005336.3|
|Specificity||Detects a ~70kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS PAGE immunoblots. The mapped epitope is in the region of amino acid residues 436-503. Does not cross-react with Hsc70 (Hsp73).|
|Sensitivity||100 µg/mL of SMC-103 was sufficient for detection of Hsp70 in human Jurkat cells by FACS analysis.|
|Application Notes||Dilution: 1:1000|
|Purification||Protein G Purified|
|Buffer||PBS pH7.2, 50% glycerol|
|Storage||Store at 4° C. Shipping Conditions: Blue Ice or 4° C|
|Storage Shipping Temp Max||Blue Ice or 4 °C|
|Research Area||Heat Shock Proteins, Cancer, Signaling|
|Restrictions||For Research Use only|
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).
Welch, Suhan: "Cellular and biochemical events in mammalian cells during and after recovery from physiological stress." in: The Journal of cell biology, Vol. 103, Issue 5, pp. 2035-52, 1987 (PubMed).
Misaki, Takeuchi, Miyamoto et al.: "Induction in vitro of 72-kD heat shock protein in a continuous culture of rat thyroid cells, FRTL5." in: Clinical and experimental immunology, Vol. 98, Issue 2, pp. 234-9, 1994 (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).
Pockley, Shepherd, Corton: "Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serum of normal individuals." in: Immunological investigations, Vol. 27, Issue 6, pp. 367-77, 1999 (PubMed).
Fink: "Chaperone-mediated protein folding." in: Physiological reviews, Vol. 79, Issue 2, pp. 425-49, 1999 (PubMed).
Dressel, Elsner, Quentin et al.: "Heat shock protein 70 is able to prevent heat shock-induced resistance of target cells to CTL." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 164, Issue 5, pp. 2362-71, 2000 (PubMed).
Kondo, Matsuda, Tashima et al.: "Suppression of heat shock protein-70 by ceramide in heat shock-induced HL-60 cell apoptosis." in: The Journal of biological chemistry, Vol. 275, Issue 12, pp. 8872-9, 2000 (PubMed).
Galuan, Garcuia-Bermejo, Troyano et al.: "Stimulation of p38 mitogen-activated protein kinase is an early regulatory event for the cadmium-induced apoptosis in human promonocytic cells." in: The Journal of biological chemistry, Vol. 275, Issue 15, pp. 11418-24, 2000 (PubMed).
Moon, Park, Schenker et al.: "Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses." in: Cerebral cortex (New York, N.Y. : 1991), Vol. 11, Issue 3, pp. 238-48, 2001 (PubMed).