HSP70 Antibody, Clone 1.86

Monoclonal

Blue Ice or 4ºC. All orders received in North America by 12:00 PM PST Monday to Thursday will usually be shipped out on the same day. North American customers will typically receive their orders within 1-2 business days. All shipments are F.O.B. from point of shipment, pre-paid and added to the invoice. Freight charges include but not limited to: priority service and packaging materials.Products are shipped with “cold packs” in insulated containers. There is a charge for this packaging and for the shipping costs via FedEx. Please inspect packages immediately upon receipt and inform Labscoop Customer Support of any shortage or damage within 48 hours of receipt. We can only accept returns after we have given prior authorization and issued specific shipping instructions. If a customer wishes to use their own FedEx account number please indicate this on the purchase order or during checkout.

Canada

WB, ICC/IF, ELISA

https://www.ncbi.nlm.nih.gov/gene/282254

1.86

NP_976067

Non-hazardous

Non-hazardous

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

1 mg/ml

WB (1:500), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

Mouse

IgG1

Human | Mouse | Rat | Bovine | Pig

Unconjugated

Protein G Purified

ISO 9001:2015

HSP70

Bovine HSP70

Detects 70kDa. Does not cross react with HSC70.

PBS pH7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated

https://antibodyregistry.org/search.php?q=AB_2697972

Cytoplasm

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 50% identity (2). 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 (3). 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 (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). 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 (6). 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. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.

1. Welch W.J. and Suhan J.P. (1986) J Cell Biol. 103: 2035-2050. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J.Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell 59: 591-601. 4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad.Sci. USA 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.

Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers | Cancer | Heat Shock

HSP70 1 Antibody, HSP70 2 Antibody, HSP70.1 Antibody, HSP72 Antibody, HSPA1 Antibody, HSPA1A Antibody, HSPA1B Antibody

E. coli