STUB1 antibody
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Description
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).
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | STIP1 homology and U-box containing protein 1 (STUB1) |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Recommended Dilution | WB: 1:500-1:2000; IHC: 1:20-1:200 |
| Clonality | polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | 35 kDa |
| Purity | ≥95% as determined by SDS-PAGE |
| Purification | Immunogen affinity purified |
| Size 1 | 100µg |
| Form | liquid |
| Tested Applications | ELISA, WB, IHC |
| Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
| UniProt ID | Q9UNE7 |
| Gene ID | 10273 |
| Alias | STUB1,CHIP, HSPABP2, NY-CO-7, SCAR16, SDCCAG7, UBOX1,SCA48,C terminus of HSC70-interacting protein |
| Background | Antibody anti-STUB1 |
| Status | RUO |
| Note | Mol. Weight 35 kDa |
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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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).
Ver Producto