Antibodies - Heat Shock Proteins, Oxydative Stress, Apoptosis, Cell Signaling

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Product Name: Hsp70/Hsc70
Catalog #: SMC-104B
Alternative Names: Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, HSPA1, HSPA1A, HSPA1B
Clone Number: N27F3-4
Immunogen: Recombinant Hsp70/hsc70
Accession Number: NP_005336.3
Gene ID: 3303
SwissProt: P08107
Applications: WB, IP, IHC, Flow Cytometry, IEM
Host Species: Mouse
Isotype: IgG1
Species Reactivity: Human, Mouse, Rat, Bovine, C.elegans, Beluga, Canine, Chicken, Drosophila, Fish, Guinea pig, Hamster, Monkey, Pig, Plant, Rabbit, Sheep, Xenopus
Recommended Dilutions: 1µg/ml was sufficient for detection of hsp/hsc70 in 20µg of HeLa lysate.
Form: Protein G Purified
Storage Buffer: PBS pH7.2, 50% glycerol
Concentration: 1mg/mL
Background Info: Detects 72 and 73kDa proteins corresponding to the molecular mass of inducible Hsp and Hsc on SDS PAGE immunoblots.
Conjugate: N/A
Package Size: 200ug
Storage Temp: -20°C
Shipping Temp: Blue Ice or 4°C
Datasheet: SMC 104 Heat Shock Protein Heat Shock Cognate 70 (Hsp Hsc70)
Research Area: Chaperones, Heat Shock, Trafficking
Certificate of Analysis: 1 μg/mL of SMC-104 was sufficient for detection of Hsp70/Hsc70 in 20μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Price: $311.00 USD Add to Cart

Western Blot analysis of Hsp70/Hsc70 in human cell line lysates at 1:1000 dilution of SMC-104.

Research 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 (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.
References: 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.
7. Polanonka-Grabowska R. et. al. (1997) Blood. 90: 1516-1526.
8. Schnell D.J., et. al. (1994) Science. 266: 1007-1012.
9. Kabakov A.E., et. al. (2002) Am. J.Physiol. 283(2): C521-C534.
10. Ricart J., et. al. (1997) Biochem. J. 324: 635-643.
11. Hang H. and Fox M.H. (1995) Cytometry 19(2): 119-125.
Cited References: 1. Lorraine Z. Mutsvunguma, Boitumelo Moetlhoa, Adrienne L. Edkins, Garry A. Luke, Gregory L. Blatch and Caroline Knox. Theiler’s murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin. Cell Stress and Chaperones. Volume 16, Number 5, 505-515, DOI: 10.1007/s12192-011-0262-x

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