WWOX recombinant protein

WWOX, 1-234aa, Human, His tag, E Coli

Cat. Num. AAA203331

• Gene Names: WWOX; FOR; WOX1; EIEE28; FRA16D; SCAR12; HHCMA56; PRO0128; SDR41C1; D16S432E
• Applications: SDS-Page
• Purity: > 85% by SDS-PAGE
• Synonyms: WWOX; 1-234aa; Human; His tag; E Coli; WW domain containing oxidoreductase; D16S432E; FOR; FRA16D; HHCMA56; PRO0128; SDR41C1; WOX1; WW domain containing oxidoreductase 5330426P09Rik; 9030416C10Rik; EC 1.1.1.- Fragile site FRA16D Oxireductase; MGC55975; Putative oxidoreductase; zgc:55975; Short chain dehydrogenase/reductase family 41C; member 1; WW domain-containing protein WWOX.; WWOX recombinant protein

• Host: E Coli
• Purity/Purification: > 85% by SDS-PAGE
• Form/Format: Liquid. In 20 mM Tris-HCl Buffer (pH 8.0) containing 10% glycerol
• Concentration: 1 mg/ml (determined by Bradford assay) (varies by lot)
• Sequence: MGSSHHHHHH SSGLVPRGSH MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG KRKRVAGDLP YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK PTTRQRYDGS TTAMEILQGR DFTGKVVVVT GANSGIGFET AKSFALHGAH VILACRNMAR ASEAVSRILE EWQQGAATTV YCAAVPELEG LGGMYFNNCC RCMPSPEAQS EETARTLWAL SERLIQERLG SQSG
• Sequence Length: 234

• Applicable Applications for WWOX recombinant protein: SDS-PAGE
• Antigen Species: Human
• Tag Information: His-tag
• Preparation and Storage: Can be stored at 4 degree C short term (1-2 weeks).; For long term storage, aliquot and store at -20 degree C or -70 degree C.; Avoid repeated freezing and thawing cycles.

SDS-Page

Related Product Information for WWOX recombinant protein

WWOX, also known as WW domain containing oxidoreductase, is a proapoptotic protein and a tumor suppressor protein. WWOX is found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This protein may function synergistically with TP53/p53 to control genotoxic stress-induced cell death. It also plays a role in tumor necrosis factor (TNF)-mediated cell death. Recombinant human WWOX protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography.

Product Categories/Family for WWOX recombinant protein

Redox Proteins

References

Bouteille N., et al. (2009), Oncogene. 28 (28):2569-80.; Gourley C., et al. (2009). Cancer Res. 69 (11):4835-42.;

NCBI and Uniprot Product Information

• NCBI GI #: 13112021
• NCBI GeneID: 51741
• Molecular Weight: 28.3 kDa (254aa), confirmed by MALDI-TOF.
• NCBI Official Full Name: WWOX protein
• NCBI Official Synonym Full Names: WW domain containing oxidoreductase
• NCBI Official Symbol: WWOX
• NCBI Official Synonym Symbols: FOR; WOX1; EIEE28; FRA16D; SCAR12; HHCMA56; PRO0128; SDR41C1; D16S432E
• NCBI Protein Information: WW domain-containing oxidoreductase
• UniProt Protein Name: WW domain-containing oxidoreductase
• Protein Family: WW domain-containing oxidoreductase
• UniProt Gene Name: WWOX
• UniProt Synonym Gene Names: FOR; SDR41C1; WOX1

NCBI Description

This gene encodes a member of the short-chain dehydrogenases/reductases (SDR) protein family. This gene spans the FRA16D common chromosomal fragile site and appears to function as a tumor suppressor gene. Expression of the encoded protein is able to induce apoptosis, while defects in this gene are associated with multiple types of cancer. Disruption of this gene is also associated with autosomal recessive spinocerebellar ataxia 12. Disruption of a similar gene in mouse results in impaired steroidogenesis, additionally suggesting a metabolic function for the protein. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2014]

Uniprot Description

Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. Required for normal bone development (). May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm.