Rabbit HSPA8 Polyclonal Antibody | anti-HSPA8 antibody

HSPA8 Antibody (C-term)

Cat. Num. AAA9208423

• Gene Names: HSPA8; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p
• Reactivity: Human (Predicted Reactivity: Bovine, Hamster, Mouse, Rat)
• Applications: Immunofluorescence, ELISA, Immunohistochemistry, Flow Cytometry, Functional Assay, Western Blot
• Purity: Purified Rabbit Polyclonal Antibody (Pab)
• Synonyms: HSPA8; Polyclonal Antibody; HSPA8 Antibody (C-term); Heat shock cognate 71 kDa protein; Heat shock 70 kDa protein 8; Lipopolysaccharide-associated protein 1; LAP-1; LPS-associated protein 1; HSC70; HSP73; HSPA10; anti-HSPA8 antibody

• Host: Rabbit
• Reactivity: Human (Predicted Reactivity: Bovine, Hamster, Mouse, Rat)
• Clonality: Polyclonal
• Isotype: Rabbit Ig
• Specificity: This HSPA8 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 539-569 amino acids from the C-terminal region of human HSPA8.
• Purity/Purification: Purified Rabbit Polyclonal Antibody (Pab)
• Form/Format: Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
• Sequence Positions: 539-569
• Sequence Length: 493

• Applicable Applications for anti-HSPA8 antibody: Immunofluorescence (IF), ELISA (EIA), Immunohistochemistry (IHC), Flow Cytometry (FC/FACS), Western Blot (WB)
• Application Notes: WB~~1:1000; IF~~1:10~50; IHC-P~~1:10~50; FC~~1:10~50
• Function: Molecular chaperone implicated in a widevariety of cellular processes, includingprotection of the proteome from stress,folding and transport of newly synthesizedpolypeptides, activation of proteolysis ofmisfolded proteins and the formation anddissociation of protein complexes. Plays apivotal role in the protein quality controlsystem, ensuring the correct folding ofproteins, the re-folding of misfolded proteinsand controlling the targeting of proteins forsubsequent degradation (PubMed:21150129, PubMed:21148293,PubMed:24732912, PubMed:27916661,PubMed:23018488). This isachieved through cycles of ATP binding, ATPhydrolysis and ADP release, mediated byco-chaperones (PubMed:21150129, PubMed:21148293,PubMed:24732912, PubMed:27916661,PubMed:23018488). Theco-chaperones have been shown to not onlyregulate different steps of the ATPase cycle ofHSP70, but they also have an individualspecificity such that one co-chaperone maypromote folding of a substrate while anothermay promote degradation (PubMed:21150129, PubMed:21148293,PubMed:24732912, PubMed:27916661,PubMed:23018488). Theaffinity of HSP70 for polypeptides is regulatedby its nucleotide bound state. In theATP-bound form, it has a low affinity forsubstrate proteins. However, upon hydrolysisof the ATP to ADP, it undergoes aconformational change that increases itsaffinity for substrate proteins. HSP70 goesthrough repeated cycles of ATP hydrolysisand nucleotide exchange, which permitscycles of substrate binding and release. TheHSP70-associated co-chaperones are of threetypes: J- domain co-chaperones HSP40s(stimulate ATPase hydrolysis by HSP70), thenucleotide exchange factors (NEF) such asBAG1/2/3 (facilitate conversion of HSP70 fromthe ADP-bound to the ATP- bound statethereby promoting substrate release), andthe TPR domain chaperones such as HOPXand STUB1 (PubMed:24318877, PubMed:27474739,PubMed:24121476, PubMed:26865365). Actsas a repressor of transcriptional activation.Inhibits the transcriptional coactivator activityof CITED1 on Smad-mediated transcription.Component of the PRP19-CDC5L complex thatforms an integral part of the spliceosome andis required for activating pre-mRNA splicing.May have a scaffolding role in thespliceosome assembly as it contacts all othercomponents of the core complex. Bindsbacterial lipopolysaccharide (LPS) andmediates LPS-induced inflammatoryresponse, including TNF secretion bymonocytes (PubMed:10722728, PubMed:11276205).Participates in the ER- associated degradation(ERAD) quality control pathway in conjunctionwith J domain-containing co-chaperones andthe E3 ligase STUB1 (PubMed:23990462).
• Cellular Location: Cytoplasm. Melanosome. Nucleus, nucleolus.Cell membrane. Note=Localized incytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidlyfrom the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.
• Tissue Location: Ubiquitous.
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 2 weeks. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Western Blot (WB)

(Western blot analysis of lysates from H-4-II-E, mouse NIH/3T3 cell line (from left to right), using HSPA8 Antibody (C-term). MBS9208423 was diluted at 1:1000 at each lane. A goat anti-rabbit IgG H&L(HRP) at 1:5000 dilution was used as the secondary antibody. Lysates at 35ug per lane.)

Immunofluorescence (IF)

(Confocal immunofluorescent analysis of HSPA8 Antibody (C-term) with Hela cell followed by Alexa Fluor 488-conjugated goat anti-rabbit lgG (green). Actin filaments have been labeled with Alexa Fluor 555 phalloidin (red).)

Immunohistochemistry (IHC)

(HSPA8 Antibody (C-term) immunohistochemistry analysis in formalin fixed and paraffin embedded human stomach tissue followed by peroxidase conjugation of the secondary antibody and DAB staining.This data demonstrates the use of HSPA8 Antibody (C-term) for immunohistochemistry. Clinical relevance has not been evaluated.)

Flow Cytometry (FC/FACS)

(HSPA8 Antibody (C-term) flow cytometric analysis of Hela cells (right histogram) compared to a negative control cell (left histogram).FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.)

Related Product Information for anti-HSPA8 antibody

HSPA8 belongs to the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. HSPA8 is a heat-shock cognate protein. This protein binds to nascent polypeptides to facilitate correct folding. The protein also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell.

Product Categories/Family for anti-HSPA8 antibody

Crown Antibodies; Signal Transduction

References

Tsukahara F., Yoshioka T.Mol. Pharmacol. 58:1257-1263(2000)
Egerton M., Moritz R.L.Biochem. Biophys. Res. Commun. 224:666-674(1996)

NCBI and Uniprot Product Information

• NCBI GI #: 5729877
• NCBI GeneID: 3312
• NCBI Accession #: NP_006588.1; NP_694881.1
• NCBI GenBank Nucleotide #: NM_006597.5
• UniProt Accession #: P11142; Q9H3R6
• Molecular Weight: 70898
• 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
• 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: Nucleolus; Chaperone; RNA-binding; Heat shock protein

Chromosomal Location of Human Ortholog: 11q24.1

Cellular Component: extracellular space; focal adhesion; ribonucleoprotein complex; cytosol; nucleoplasm; spliceosome; membrane; melanosome; plasma membrane; nucleolus; intracellular; 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; viral reproduction; chaperone cofactor-dependent protein folding; protein folding; transcription, DNA-dependent; 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