Rabbit Hsc70 Polyclonal Antibody | anti-HSPA8 antibody

Hsc70 Rabbit pAb

Cat. Num. AAA4752019

• Gene Names: HSPA8; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; NIP71; HSPA10
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunohistochemistry, Immunocytochemistry, Immunofluorescence, Flow Cytometry, Functional Assay, Immunoprecipitation
• Purity: Affinity purified
• Synonyms: Hsc70; Polyclonal Antibody; Hsc70 Rabbit pAb; Heat shock cognate 71kDa protein; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p; anti-HSPA8 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: Ubiquitous.
• Purity/Purification: Affinity purified
• Form/Format: Supplied in 50nM Tris-Glycine (pH7.4), 0.15M Nacl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

• Applicable Applications for anti-HSPA8 antibody: Western Blot (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunofluorescence (IF), Flow Cytometry (FC/FACS), Immunoprecipitation (IP)
• Application Notes: WB: 1:1000; IHC: 1:20; ICC/IF: 1:20-1:50; FC/FACS: 1:20; IP: 1:20
• Immunogen: A synthetic peptide of human Hsc70
• Conjugation: Unconjugated
• Modification: Unmodification
• Subcellular Location: Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Western Blot (WB)

(Western blot detection of Hsc70 in Hela cell lysates using Hsc70 Rabbit pAb(1:1000 diluted). Predicted band size:71KDa. Observed band size:71KDa.)

Western Blot (WB)

(Western blot detection of Hsc70 in Jurkat,Rat Brain,C6,CHO-K1,Hela cell lysates using Hsc70 Rabbit pAb(1:1000 diluted). Predicted band size:71kDa. Observed band size:71kDa.)

Related Product Information for anti-HSPA8 antibody

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]
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462).

NCBI and Uniprot Product Information

• NCBI GI #: 5729877
• NCBI GeneID: 3312
• NCBI Accession #: NP_006588.1
• NCBI GenBank Nucleotide #: NM_006597.4
• UniProt Accession #: P11142; Q9H3R6
• Molecular Weight: 70,898 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; NIP71; HSPA10
• NCBI Protein Information: heat shock cognate 71 kDa protein; LPS-associated protein 1; heat shock 70kd protein 10; heat shock cognate protein 54; constitutive heat shock protein 70; lipopolysaccharide-associated protein 1; N-myristoyltransferase inhibitor protein 71
• UniProt Protein Name: Heat shock cognate 71 kDa protein
• Protein Family: Hsc70-interacting protein
• UniProt Gene Name: HSPA8
• UniProt Synonym Gene Names: HSC70; HSP73; HSPA10
• 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; Chaperone; Heat shock protein; Nucleolus

Chromosomal Location of Human Ortholog: 11q24.1

Cellular Component: nucleoplasm; spliceosome; extracellular space; focal adhesion; membrane; melanosome; nucleolus; plasma membrane; intracellular; ribonucleoprotein complex; nucleus; cytosol; 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; viral reproduction; chaperone cofactor-dependent protein folding; protein folding; transcription, DNA-dependent; regulation of cell cycle; neurotransmitter secretion; RNA splicing; response to unfolded protein; nuclear mRNA splicing, via spliceosome; positive regulation of nuclear mRNA splicing, via spliceosome; synaptic transmission; gene expression; protein refolding; post-Golgi vesicle-mediated transport; negative regulation of transcription, DNA-dependent