Hspa8 Rabbit Polyclonal Antibody

CAT#: TA362978

HSPA8 Antibody - middle region

Product Images

Host: Rabbit Target Name: HSPA8 Sample Tissue: Mouse Heart lysates Antibody Dilution: 1ug/ml

Specifications

Product Data

• Applications: WB
• Reactivities: Mouse
• Host: Rabbit
• Clonality: Polyclonal
• Immunogen: The immunogen is a synthetic peptide directed towards the middle region of mouse HSPA8
• Specificity: Expected reactivity: Mouse
• Formulation: Liquid. Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
  Note that this product is shipped as lyophilized powder to China customers.
• Concentration: lot specific
• Purification: Affinity purified
• Conjugation: Unconjugated
• Storage: For short term use, store at 2-8°C up to 1 week. For long term storage, store at -20°C in small aliquots to prevent freeze-thaw cycles.
• Stability: Shelf life: one year from despatch.
• Predicted Protein Size: 71 kDa
• Gene Name: heat shock protein 8
• Database Link:
  NP_112442.2
  Entrez Gene 15481 Mouse
  UniProt ID P63017
• Background: 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. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. 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. 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. 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. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1.
• Synonyms: HSC54; HSC70; HSC71; HSP71; HSP73; HSPA10; LAP1; MGC29929; MGC131511; NIP71