Hspa8 Mouse shRNA Plasmid (Locus ID 15481)

SKU TR501001

Hspa8 - Mouse, 4 unique 29mer shRNA constructs in retroviral untagged vector, 5µg of each construct provided

Product Data

• Locus ID: 15481
• Synonyms: 2410008N15Rik; Hsc70; Hsc71; Hsc73; Hsp73; Hspa10
• Vector: pRS
• E. coli Selection: Ampicillin
• Format: Retroviral plasmids
• Components: Hspa8 - Mouse, 4 unique 29mer shRNA constructs in retroviral untagged vector(Gene ID = 15481). 5µg purified plasmid DNA per construct; 29-mer scrambled shRNA cassette in pRS Vector, TR30012, included for free.
• RefSeq: BC006722, BC066191, BC085486, BC089322, BC089457, BC094900, BC106193, NM_031165, NM_031165.1, NM_031165.2, NM_031165.3, NM_031165.4, BC106169, NM_001364480
• UniProt ID: P63017
• Summary: 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.[UniProtKB/Swiss-Prot Function]
• shRNA Design: These shRNA constructs were designed against multiple splice variants at this gene locus. To be certain that your variant of interest is targeted, please contact techsupport@origene.com. If you need a special design or shRNA sequence, please utilize our custom shRNA service.
• Shipping: Ambient