Anti-HSPA8 Monoclonal Antibody
Cat.No:K200075M Solarbio
Reactivity:Human,Rat,Mouse
Application:WB,IHC
Clone Type:Monoclonal Antibody
Storage:Store at -20℃. Avoid freeze/thaw cycles.
Gene ID:3312
Host:Mouse
Qty:
Size:
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My CartReactivity:Human,Rat,Mouse
Application:WB,IHC
Clone Type:Monoclonal Antibody
Storage:Store at -20℃. Avoid freeze/thaw cycles.
Gene ID:3312
Host:Mouse
Qty:
Size:
Name | Anti-HSPA8 Monoclonal Antibody |
Host | Mouse |
Clone Type | Monoclonal Antibody |
Subtype | IgG1 |
Clone Number | 6C7 |
Dilution Ratio | WB 1:2000-5000. IHC 1:50-200. |
Target | HSPA8 |
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 by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21. |
Swiss Prot | P11142 |
Gene ID | 3312 |
Subcellular Location | Cytoplasm Nucleus |
Immunogen | Recombinant Protein |
Calculated MW | 71/54kDa |
Purification Method | Affinity purification |
Storage Buffer | PBS with 50% Glycerol,0.03% Proclin300,0.5% BSA,pH 7.3. |
Storage | Store at -20℃. Avoid freeze/thaw cycles. |
Unit | Piece |
Specification | 20ul 50ul 100ul |
Reactivity | Human Rat Mouse |
Application | WB IHC |
Remark:These protocols are for reference only. Solarbio does not independently validate these methods.
Kindly reminder:Quick spin before use. If you have any questions, please contact us.
Note:
1. The products are all for scientific research use only. Do not use it for medical, clinical diagnosis or treatment, food and cosmetics, etc. Do not store them in ordinary residential areas.
2. For your safety and health, please wear laboratory clothes, disposable gloves and masks.
3. The experimental results may be affected by many factors, after-sale service is limited to the product itself and does not involve other compensation.
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