Mouse STIP1 Homology And U-Box Containing Protein 1 (STUB1) CLIA Kit
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Description
Mouse STIP1 Homology And U-Box Containing Protein 1 (STUB1) Chemiluminescent Immunoassay (CLIA) Kit is a Sandwich Chemiluminescent Immunoassay (CLIA) Kit for use with Tissue homogenates and other biological fluids.
Documents del producto
Product specifications
| Category | CLIA Kits |
| Immunogen Target | STIP1 Homology And U-Box Containing Protein 1 (STUB1) |
| Reactivity | Mouse |
| Detection Method | Chemiluminescent |
| Assay Data | Quantitative |
| Assay Type | Sandwich |
| Test Range | 0.156 ng/ml - 10 ng/ml |
| Sensitivity | < 0.059 ng/ml |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Size 1 | 96 tests |
| Size 2 | 5 × 96 tests |
| Size 3 | 10 × 96 tests |
| Form | Lyophilized |
| Tested Applications | CLIA |
| Sample Type | Tissue homogenates and other biological fluids. |
| Availability | Shipped within 5-20 working days. |
| Storage | Shipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual. |
| Dry Ice | No |
| Alias | STUB1,CHIP, HSPABP2, NY-CO-7, SCAR16, SDCCAG7, UBOX1,SCA48,C terminus of HSC70-interacting protein |
| Background | CLIA Kits STUB1 |
| Status | RUO |
| Note | The validity for this kit is at least 6 months. Up to 12 months validity can be provided on request. This product is for research use only. The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments. Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein. |
Descripción
STUB1, also known as CHIP (C-terminus of Hsc70-interacting protein), is a co-chaperone protein and E3 ubiquitin ligase that regulates protein homeostasis by linking the molecular chaperones HSP70 and HSP90 to the ubiquitin-proteasome system. STUB1 promotes the ubiquitination and degradation of misfolded, damaged, or surplus proteins, ensuring proper protein quality control and cellular stress responses. It is broadly expressed in tissues and plays a crucial role in proteostasis, particularly under stress conditions where protein misfolding is elevated. STUB1 is also involved in signaling pathways regulating apoptosis, cell survival, and metabolic adaptation by targeting key signaling proteins for degradation. Dysregulation of STUB1 is associated with neurodegenerative disorders, such as Alzheimer’s disease, Parkinson’s disease, and ataxias, where impaired protein degradation leads to the accumulation of toxic protein aggregates. Knockout studies reveal increased protein misfolding, cellular stress, and neurodegeneration, highlighting its essential role in maintaining proteome integrity and cellular homeostasis.
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anti- STUB1 antibody
E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta(POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Negatively regulates the suppressive function of regulatory T-cells(Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner(PubMed:23973223).
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