Stub1 (NM_019719) Mouse Recombinant Protein

Specifications

Product Data
Species	Mouse
Expression Host	HEK293T
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) >MR204258 protein sequence Red=Cloning site Green=Tags(s) MKGKEEKEGGARLGTGGGGSPDKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALC YLKMQQPEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSAL RIAKKKRWNSIEERRIHQESELHSYLTRLIAAERERELEECQRNHEGHEDDGHIRAQQACIEAKHDKYMA DMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQ LIPNLAMKEVIDAFISENGWVEDY TRTRPLEQKLISEEDLAANDILDYKDDDDKV
Tag	C-MYC/DDK
Predicted MW	34.9 kDa
Concentration	>0.05 µg/µL as determined by microplate BCA method
Purity	> 80% as determined by SDS-PAGE and Coomassie blue staining
Buffer	25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
Note	For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
Storage	Store at -80°C after receiving vials.
Stability	Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Reference Data
RefSeq	NP_062693
Locus ID	56424
UniProt ID	Q9WUD1
Refseq Size	1672
Cytogenetics	17 12.93 cM
Refseq ORF	915
Synonyms	0610033N24Rik; 2210017D18Rik; 2310040B03Rik; AW046544; Chip
Summary	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). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Likely mediates polyubiquitination and downregulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (By similarity). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (By similarity). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (By similarity).[UniProtKB/Swiss-Prot Function]

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