Wilms' tumor 1-associating protein (WTAP) was previously identified as a protein associated with Wilms' tumor-1 (WT-1) protein that is essential for the development of the genitourinary system. WT1 was originally identified as a tumor suppressor for Wilms' tumor, but it is also overexpressed in a variety of cancer cells. The WTAP-WT1 axis in vascular cells suggest that WTAP is a vital and multifaceted regulator of vascular remodeling. WTAP has been suggested to function in alternative splicing, stabilization of mRNA, and cell growth. Knocking down endogenous WTAP increased Smooth muscle cells (SMCs) proliferation, because of increased DNA synthesis and G(1)/S phase transition, together with reduced apoptosis. These effects could be the result of WTAP suppressing the transcriptional activity of WT1 in SMCs. WTAP may thus also play a role in messenger RNA processing in mammalian cells, either dependent on or independent of its interaction with WT1.
Product Name:
Human HEXA Recombinant Protein (RPES4054)
Product Code:
RPES4054
Size:
20µg
Species:
Human
Expressed Host:
Baculovirus-Insect Cells
Synonyms:
TSD
Accession:
AAD13932.1
Sequence:
Met 1-Thr 529
Fusion tag:
C-His
Activity:
Measured by its ability to hydrolyze 4-methylumbelliferyl-N-acetyl-?-D-glucosaminide (4-MU-Glc-NAc).The specific activity is >1,250 pmoles/min/µg.
Endotoxin:
<1.0 EU per µg of the protein as determined by the LAL method.
Protein Construction:
A DNA sequence encoding the human HEXA (AAD13932.1) (Met 1-Thr 529) was fused with a polyhistidine tag at the C-terminus.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
59.7 kDa
AP Mol Mass:
64 kDa
Formulation:
Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
