antibody

HSP70 (Fish) Antibody

SPC-314B

200 µg

366.00 USD

polyclonal

domestic rabbit

nonconjugated

western blot, immunohistochemistry, immunoprecipitation

HSP70 (Fish) Antibody

Rabbit Anti-Salmon HSP70 (Fish) Polyclonal

HSP70

Unconjugated

366.00 USD

USD

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

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

200 µg

Antibodies

Polyclonal

Synthetic peptide conjugated to KLH. Peptide sequence specific to C-terminal part of salmonid HSP70. The target is not present in any other HSP70 proteins.

Salmon

NP_001135156.1

B5DG30

WB IHC IP

Rabbit

Fs Slm

Fish Salmon Brook Trout (Salvelinus fontinalis) Rainbow Trout (Oncorhynchus mykiss) Fathead minnow (Pimephales promelas)

WB (1:1000), IHC (1:100), IP (5µg); optimal dilutions for assays should be determined by the user.

Protein A Purified

Lyophilized rabbit Antiserum. For reconstitution add 200 µl of sterile water.

Detects ~70kDa. It does not cross react with HSC70. It does not detect HSP70 in other species.

-20ºC

Blue Ice or 4ºC

StressMarq Biosciences Cat# SPC-314B, RRID: AB_1501441

1 µg/ml of SPC-314 was sufficient for detection of HSP70 in 20 µg of heat shocked (25°C) salmon cytoplasmic fraction lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

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 5O% identity (1). 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 (2). 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 (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (5). Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

1. Boorstein W.R., Ziegelhoffer T., and Craig E.A. (1993) J. Mol. Evol. 38(1): 1-17. 2. Rothman J. (1989) Cell. 59: 591-601. 3. DeLuca-Flaherty et al. (1990) Cell. 62: 875-887. 4. Bork P., Sander C., and Valencia A. (1992) Proc. Natl Acad. Sci. USA. 89: 7290-7294. 5. Brown C.L. et al. (1996) J. Biol. Chem. 271(2): 833-840.

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