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Astor Scientific  |  SKU: ASTP5730

Human UBE2W (Ubiquitin-Conjugating Enzyme E2 W) - Recombinant Protein

Molecule: UBE2W
Species: Human
Expression System: E.coli
Tag: N-6His
Expression Range: 1-151aa
$429.99 $549.99
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SDS-PAGE analysis of Human UBE2W (Ubiquitin-Conjugating Enzyme E2 W) - Recombinant Protein, showing >95% purity under 15% SDS-PAGE (Reduced)
Astor Scientific

Human UBE2W (Ubiquitin-Conjugating Enzyme E2 W) - Recombinant Protein

$429.99 $549.99

Product Overview

Product Name Recombinant Human UBE2W Protein
Product Overview This recombinant human UBE2W protein includes amino acids 1-151aa of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization.
Target Uniprot Id Q96B02
Recommended Name Ubiquitin-conjugating enzyme E2 W
Gene Name UBE2W
Synonyms Probable ubiquitin-conjugating enzyme E2 W, FLJ11011, hUBC-16
Species Human
Predicted Molecular Mass 19.5 kDa
Expression System E.coli
Expression Range 1-151aa
Tag N-6His
Purity >95%
Formulation Lyophilized
Buffer Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose
Storage Condition 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Reconstitution Instruction Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Applications Positive Control; Immunogen; SDS-PAGE; WB
Research Area Epigenetics And Nuclear Signaling
Target Function Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Specifically monoubiquitinates the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered N-termini. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed ubiquitination occurs also in the presence of inactive RING/U-box type E3s, i.e. lacking the active site cysteine residues to form thioester bonds with ubiquitin, or even in the absence of E3, albeit at a slower rate.
Subcellular Location Nucleus.
Protein Family Ubiquitin-conjugating enzyme family
Tissue Specificity Widely expressed, with highest expression in brain, liver, pancreas and heart.

Size

  • 100ug
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