antibody

Hsc70 (Hsp73) Antibody: Biotin

MBS800006

0.2 mg

500 USD

monoclonal

mouse

biotin

1F2-H5

human, mouse, rat

western blot, ELISA, immunohistochemistry, immunoprecipitation, enzyme immunoassay, proximity ligation assay

Antibody

Hsc70 (Hsp73) Antibody: Biotin

HSC70 (HSP73)

Hsc54; Hsc71; Hsc73; Hsp71; Hsp73; HspA10; HspA8; LAP1; NIP71

heat shock cognate 71 kDa protein isoform 1; Heat shock cognate 71 kDa protein; heat shock cognate 71 kDa protein; LPS-associated protein 1; heat shock 70kd protein 10; epididymis luminal protein 33; heat shock cognate protein 54; constitutive heat shock protein 70; lipopolysaccharide-associated protein 1; N-myristoyltransferase inhibitor protein 71; epididymis secretory sperm binding protein Li 72p; heat shock 70kDa protein 8; Heat shock 70 kDa protein 8; Lipopolysaccharide-associated protein 1; LAP-1; LPS-associated protein 1

HSPA8; HSPA8; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p; HSC70; HSP73; HSPA10; LAP-1; LPS-associated protein 1

HSP7C_HUMAN

Monoclonal

IgG2a Kappa

1F2-H5

Mouse

Human, Mouse, Rat

646

Detects ~73kDa, Does not cross react with HSP70.

Protein G Purified

1mg/mL

-20 degree C; 1 year + Avoid freeze/thaw cycle.

Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP), Immunohistochemistry (IHC), PLA

WB: 1:1000. ICC/IF: 1:100. Optimal dilutions for assays should be determined by the user.

Conjugate: Biotin. Immunogen: Full length human HSC70

Storage Buffer: PBS pH7.4, 50% glycerol, 0.09% sodium azide. Certificate of Analysis: 1 ug/ml of SMC-151 was sufficient for detection of HSC70 in 10 ug of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG: HRP as the secondary antibody. Research Area(s): Cancer Heat Shock. Cellular Localization: Cytoplasm Melanosome.

Chaperones, Heat Shock, Trafficking

Background Info: Detects ~73kDa. Does not cross react with Hsp70. Scientific 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). 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 (6).

1. Brown C.L. et al. (1993) J.Cell Biol., 120 (5): 1101-1112. 2. Boorstein W.R., Ziegelhoffer T., and 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., and Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294. 6. Brown C.L. et al. (1996) J. Biol. Chem. 271(2): 833- 840. 1. Shiota, M. et al. (2009). Heat Shock Cognate Protein 70 Is Essential for Akt Signaling in Endothelial Function. Arteriosclerosis, Thrombosis, and Vascular Biology. 30, 491-497. doi: 10.1161/‹ATVBAHA.109.193631. 2. Kawano, F. et al. (2011). Responses of HSC70 expression in diencephalon to iron deficiency anemia in rats. J Physiol Sci. 61 (6), 445-456. doi:10.1007/s12576-011-0164-9. 3. Baaklini, I. et al. (2012). The DNAJA2 Substrate Release Mechanism Is Essential for Chaperone-mediated Folding. J Biol Chem. 287, 41939-41954. doi: 10.1074/jbc.M112.413278. 4. Shimomura, H., Imai, A., Nashida, T. (2013) Characterization of cysteine string protein in rat parotid acinar cells. Archives of Biochemistry and Biophysics. Available online 10 August 2013. doi: 10.1016/j.abb.2013.08.001

5729877

NP_006588.1

NM_006597.5

P11142

53,518 Da

AUF1 (hnRNP D0) Destabilizes MRNA Pathway (187212); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Attenuation Phase Pathway (980473); Axon Guidance Pathway (105688); C-MYB Transcription Factor Network Pathway (138073); CHL1 Interactions Pathway (161007); Cellular Response To Heat Stress Pathway (980470); Cellular Responses To Stress Pathway (645258); Clathrin Derived Vesicle Budding Pathway (119545)

This gene encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members. This protein belongs to the latter group, which are also referred to as heat-shock cognate proteins. It functions as a chaperone, and binds to nascent polypeptides to facilitate correct folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011]

HSC70: Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co- chaperones. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with PACRG and TSC2. Interacts with BAG1. Interacts with SV40 VP1. Interacts with DNAJC7. Interacts with HERC5. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Constitutively synthesized. Ubiquitous. Belongs to the heat shock protein 70 family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Chaperone; Nucleolus; Heat shock protein; RNA-binding. Chromosomal Location of Human Ortholog: 11q24.1. Cellular Component: nucleoplasm; spliceosome; extracellular space; focal adhesion; membrane; melanosome; nucleolus; plasma membrane; intracellular; ribonucleoprotein complex; cytosol; nucleus; ubiquitin ligase complex. Molecular Function: protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; ubiquitin protein ligase binding; ATPase activity; unfolded protein binding; ATPase activity, coupled; ATP binding. Biological Process: axon guidance; chaperone cofactor-dependent protein folding; viral reproduction; transcription, DNA-dependent; protein folding; regulation of cell cycle; RNA splicing; neurotransmitter secretion; response to unfolded protein; nuclear mRNA splicing, via spliceosome; positive regulation of nuclear mRNA splicing, via spliceosome; synaptic transmission; protein refolding; gene expression; post-Golgi vesicle-mediated transport; negative regulation of transcription, DNA-dependent

0.2 mg

500 USD