{{cart_num}}
My Cart> Protein and Immunity > Blocking Peptides > HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B Antibody Blocking PeptideStorage：Store at -20℃，2 years.Avoid freeze/thaw cycles.
Appearance：Lyophilized powder
Gene ID：3305/3303/3304
Application：Blocking Peptide of K109870P Antibody
Qty：
Size：
| Name | HS71L/HSPA1A/HSPA1B HSPA1L/HSPA1A/HSPA1B Antibody Blocking Peptide |
| Appearance | Lyophilized powder |
| Storage | Store at -20℃，2 years.Avoid freeze/thaw cycles. |
| Swiss Prot | P34931/P0DMV8/P0DMV9 |
| Gene ID | 3305/3303/3304 |
| 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 affinity 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.It goes through repeated cycles of ATP hydrolysis and nucleotide exchange， which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria.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， 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 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange， which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as 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. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response， the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding， thereafter， it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis， and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response.(Microbial infection) In case of rotavirus A infection， serves as a post-attachment receptor for the virus to facilitate entry into the cell.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， 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 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. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange， which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as 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. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response， the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding， thereafter， it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis， and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation.(Microbial infection)In case of rotavirus A infection， serves as a post-attachment receptor for the virus to facilitate entry into the cell. |
| Application | Blocking Peptide of K109870P Antibody |
| Source | Synthetic |
| Purification Method | HPLC |
| Biological Activity | Not tested |
| Unit | Piece |
| Specification | 500ug |
Remark：These protocols are for reference only. Solarbio does not independently validate these methods.
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.
Sorry, there is no experimental images.
Sorry, there is no more information.
Sorry, there is no more information.
Manual Download
