Recombinant Human STUB1

Este producto es parte de STUB1 - STIP1 Homology And U-Box Containing Protein
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935106861
info@markelab.com
name
Recombinant Human STUB1
category
Proteins and Peptides
provider
FineTest
reference
P6987
tested applications
Western Blot,ELISA

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Product specifications

CategoryProteins and Peptides
Immunogen Target1-303
HostE.Coli
OriginHuman
Observed MW33.2 kDa
ExpressionRecombinant
PurityGreater than 95% by SDS-PAGE gel analyses
PurificationHis tag
Size 150μg
Size 2200μg
Size 31mg
FormLyophilized from a 0.2um filtered solution in PBS with 5% trehalose, pH7.4
Tested ApplicationsWestern Blot,ELISA
BufferReconstitute with Sterile distilled water
Availability3-4 weeks
Storage-20°C for 12 months as lyophilized;2-8°C for 1 month under sterile conditions after reconstitution
UniProt IDQ9UNE7
AliasSTUB1,CHIP, HSPABP2, NY-CO-7, SCAR16, SDCCAG7, UBOX1,SCA48,C terminus of HSC70-interacting protein
BackgroundProteins STUB1
StatusRUO
NoteThis product is for research use only.

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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