Rabbit HSPA8/HSC70 Polyclonal Antibody | anti-HSPA8/HSC70 antibody

Anti-HSPA8/HSC70 Antibody

Cat. Num. AAA2400763

• Gene Names: HSPA8; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p
• Reactivity: Human; Predicted: Rabbit, Mouse, Bovine, Rat, Hamster, Monkey
• Applications: Immunohistochemistry, Western Blot
• Purity: Affinity Purified
• Synonyms: HSPA8/HSC70; Polyclonal Antibody; Anti-HSPA8/HSC70 Antibody; Rat Monoclonal (IgG2b) to Hamster HSPA8/HSC70; HSPA8; Heat shock 70 kDa protein 8; Heat shock 70kd protein 10; Heat shock 70kD protein 8; Heat shock cognate protein 54; HSP71; HSPA10; HSC71; HSP73; LPS-associated protein 1; Heat shock 70kDa protein 8; NIP71; HSC54; HSC70; LAP1; anti-HSPA8/HSC70 antibody

• Host: Rabbit
• Reactivity: Human; Predicted: Rabbit, Mouse, Bovine, Rat, Hamster, Monkey
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: The antibody detects a 71 kD Hsc70. A ~40 kD band can also be detected in human samples. Jurkat cell lysate and mouse small intestine lysate can be used as positive controls. Blocking peptide is also available.
• Purity/Purification: Affinity Purified
• Form/Format: PBS, pH 7.2, 30% glycerol, 0.5% BSA, 0.01% Thimerosal.
• Sequence Length: 646

• Applicable Applications for anti-HSPA8/HSC70 antibody: Immunohistochemistry (IHC) Paraffin, Western Blot (WB)
• Application Notes: IHC-P: 5 ug/ml; WB: 0.5-4 ug/ml
• Immunogen: Synthetic peptide surrounding amino acid 559 of human Hsc70.
• Conjugation: Unconjugated
• Preparation and Storage: Short term: 4 degree C; Long term: -20 degree C.; Avoid freeze-thaw cycles.

Immunohistochemistry (IHC)

(Anti-HSPA8/HSC70 antibody IHC of human brain, cortex. Immunohistochemistry of formalin-fixed, paraffin-embedded tissue after heat-induced antigen retrieval. Antibody dilution 5 ug/ml.)

Western Blot (WB)

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Related Product Information for anti-HSPA8/HSC70 antibody

Acts as a repressor of transcriptional activation. Inhibits thetranscriptional coactivator activity of CITED1 on Smad-mediatedtranscription. Chaperone. Component of the PRP19-CDC5L complex thatforms an integral part of the spliceosome and is required for activatingpre-mRNA splicing. May have a scaffolding role in the spliceosomeassembly as it contacts all other components of the core complex.

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 protein family A (Hsp70) member 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

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

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).