Mouse STIP1 Homology And U-Box Containing Protein 1 (STUB1) Protein
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Description
Mouse STIP1 Homology And U-Box Containing Protein 1 (STUB1) Protein is a Recombinant Mouse protein expressed in E. coli.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | STIP1 Homology And U-Box Containing Protein 1 (STUB1) |
| Host | E. coli |
| Origin | Mouse |
| Conjugation | Unconjugated |
| Observed MW | Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Please enquire. Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 90% |
| Size 1 | 1 mg |
| Size 2 | 5 mg |
| Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
| Availability | Shipped within 1-2 months. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Alias | STUB1,CHIP, HSPABP2, NY-CO-7, SCAR16, SDCCAG7, UBOX1,SCA48,C terminus of HSC70-interacting protein |
| Background | Protein STUB1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
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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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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