HSP70/HSC70 Antibody, Clone BB70: ATTO 594

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, IHC, IP

https://www.ncbi.nlm.nih.gov/gene/423504

BB70

NP_001006686.1

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 (1:1000), IHC (1:200), ICC/IF (1:200); optimal dilutions for assays should be determined by the user.

Mouse

IgG2a

Human | Mouse | Rat | Bovine | Sheep | Dog | Beluga | Fish | Guinea Pig (Cavia porcellus) | Pig | Hamster | Rabbit | Chicken | African clawed frog (Xenopus laevis) | Fruit Fly (Drosophila melanogaster) | Yeast

ATTO 594

Protein G Purified

ISO 9001:2015

HSP70/HSC70

Chicken HSP70/HSP90 complex

Detects ~72 (HSP) and ~73kDa (HSC).

PBS pH7.2, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated

https://antibodyregistry.org/search.php?q=AB_2697856

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. Zho J. (1998) Cell 94 : 471-480. 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. Nat Acad. Sci. USA 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al, (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al. (1996) Mol. Cell. Biol. 16(11):6200-6207. 9. Fernandez-Funez et al., (2000) Nature 408(6808): 101-106.

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

HSC54 Antibody, HSC70 Antibody, HSC71 Antibody, HSP70 1 Antibody, HSP701/HSP70 2 Antibody, HSP70.1 Antibody, HSP71 Antibody, HSP72 Antibody, HSP73 Antibody, HSPA1 Antibody, HSPA10 Antibody, HSPA1A Antibody, HSPA1B Antibody, LAP1 Antibody, NIP71 Antibody

E. coli