Hspa8 Mouse siRNA Oligo Duplex (Locus ID 15481)
CAT#: SR418633
Hspa8 (Mouse) - 3 unique 27mer siRNA duplexes - 2 nmol each
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CNY 4,090.00
货期*
7周
规格
Cited in 1 publication. |
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经常一起买 (3)
Specifications
Product Data | |
Purity | HPLC purified |
Quality Control | Tested by ESI-MS |
Sequences | Available with shipment |
Stability | One year from date of shipment when stored at -20°C. |
# of transfections | Approximately 330 transfections/2nmol in 24-well plate under optimized conditions (final conc. 10 nM). |
Note | Single siRNA duplex (10nmol) can be ordered. |
Reference Data | |
RefSeq | NM_031165, NM_001364480 |
Synonyms | 2410008N15Rik; Hsc70; Hsc71; Hsc73; Hsp73; Hspa10 |
Components | Hspa8 (Mouse) - 3 unique 27mer siRNA duplexes - 2 nmol each (Locus ID 15481)Included - SR30004, Trilencer-27 Universal Scrambled Negative Control siRNA Duplex - 2 nmolIncluded - SR30005, RNAse free siRNA Duplex Resuspension Buffer - 2 ml |
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] |
Performance Guranteed | OriGene guarantees that at least two of the three Dicer-Substrate duplexes in the kit will provide at least 70% or more knockdown of the target mRNA when used at 10 nM concentration by quantitative RT-PCR when the TYE-563 fluorescent transfection control duplex (cat# SR30002) indicates that >90% of the cells have been transfected and the HPRT positive control (cat# SR30003) provides 90% knockdown efficiency. For non-conforming siRNA, requests for replacement product must be made within ninety (90) days from the date of delivery of the siRNA kit. To arrange for a free replacement with newly designed duplexes, please contact Technical Services at techsupport@origene.com. Please provide your data indicating the transfection efficiency and measurement of gene expression knockdown compared to the scrambled siRNA control (quantitative RT-PCR data required). |
Citations (1)
The use of this RNAi has been cited in the following citations: |
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The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome
,null,
Free radical biology & medicine
,PubMed ID 27498116
[Hspa8]
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