Mouse HSC70 (HSP73) Monoclonal Antibody | anti-HSPA8 antibody

Hsc70 (Hsp73) Antibody: PerCP

Cat. Num. AAA802453

• Gene Names: HSPA8; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, ELISA, Immunoprecipitation, Immunohistochemistry
• Synonyms: HSC70 (HSP73); Monoclonal Antibody; Hsc70 (Hsp73) Antibody: PerCP; Hsc54; Hsc71; Hsc73; Hsp71; Hsp73; HspA10; HspA8; LAP1; NIP71; anti-HSPA8 antibody

• Host: Mouse
• Reactivity: Human, Mouse, Rat
• Clonality: Monoclonal
• Isotype: IgG2a Kappa
• Clone Number: 1F2-H5
• Form/Format: Protein G Purified
• Concentration: 1mg/mL (varies by lot)
• Sequence Length: 646

• Applicable Applications for anti-HSPA8 antibody: Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP), Immunohistochemistry (IHC), PLA
• Application Notes: 1:1000 (WB)
• Conjugate: PerCP
• Storage Buffer: PBS pH7.4, 50% glycerol, 0.09% sodium azide
• Preparation and Storage: -20 degree C

Western Blot (WB)

(Western Blot analysis of Human Cell lysates showing detection of Hsc70 protein using Mouse Anti-Hsc70 Monoclonal Antibody, Clone 1F2-H5. Load: 15 ug. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsc70 Monoclonal Antibody at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT. 1: mix of 10 different human cell lines, 2: Hsp72 recombinant protein, and 3: Hsc70(Hsp73) recombinant protein.)

Immunocytochemistry/Immunofluorescence (ICC/IF)

(Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsc70 Monoclonal Antibody, Clone 1F2-H5. Tissue: HaCaT cells. Species: Human. Fixation: Cold 100% methanol for 10 minutes at -20 degree C. Primary Antibody: Mouse Anti-Hsc70 Monoclonal Antibody at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Bright cytoplasmic staining, duller nuclear staining.)

Related Product Information for anti-HSPA8 antibody

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).

Product Categories/Family for anti-HSPA8 antibody

Chaperones; Heat Shock; Trafficking

References

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

NCBI and Uniprot Product Information

• NCBI GI #: 5729877
• NCBI GeneID: 3312
• NCBI Accession #: NP_006588.1
• NCBI GenBank Nucleotide #: NM_006597.5
• UniProt Accession #: P11142; Q9H3R6
• Molecular Weight: 53,518 Da
• NCBI Official Full Name: heat shock cognate 71 kDa protein isoform 1
• NCBI Official Synonym Full Names: heat shock 70kDa protein 8
• NCBI Official Symbol: HSPA8
• NCBI Official Synonym Symbols: LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p
• NCBI Protein Information: 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
• UniProt Protein Name: Heat shock cognate 71 kDa protein
• UniProt Gene Name: HSPA8
• UniProt Synonym Gene Names: HSC70; HSP73; HSPA10; LAP-1; LPS-associated protein 1
• UniProt Entry Name: HSP7C_HUMAN

NCBI Description

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]

Uniprot Description

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: RNA-binding; Nucleolus; Chaperone; Heat shock protein

Chromosomal Location of Human Ortholog: 11q24.1

Cellular Component: extracellular space; focal adhesion; cytosol; ribonucleoprotein complex; nucleoplasm; spliceosome; membrane; melanosome; plasma membrane; nucleolus; intracellular; nucleus; ubiquitin ligase complex

Molecular Function: protein binding; enzyme binding; G-protein-coupled receptor binding; ubiquitin protein ligase binding; heat shock protein binding; ATPase activity; unfolded protein binding; ATPase activity, coupled; ATP binding

Biological Process: axon guidance; viral reproduction; transcription, DNA-dependent; chaperone cofactor-dependent protein folding; protein folding; regulation of cell cycle; RNA splicing; neurotransmitter secretion; response to unfolded protein; positive regulation of nuclear mRNA splicing, via spliceosome; nuclear mRNA splicing, via spliceosome; synaptic transmission; protein refolding; gene expression; post-Golgi vesicle-mediated transport; negative regulation of transcription, DNA-dependent