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B3GNT4, Recombinant, Human (Beta-1,3-N-acetylglucosaminyltransferase 4)

Cat no: 167630


Supplier: United States Biological
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b1,3�Linked GlcNAc residues are present in the backbone of various biologically important glycans which are involved in many essential biological functions such as keratan sulfate synthesis in corneal tissue (1). The addition of such residues are catalyzed by a family of b1,3�N�acetylglucosaminyltransferases, that includes at least eight members (15). All of them are type II Golgi resident transmembrane proteins and have high homology to the b1,3�galactosyltransferase family. b1,3�N� acetylglucosaminyltransferase 4 or b3GNT4 is involved in polylactosamine synthesis and is mainly expressed in brain tissues such as whole brain, hippocampus, amygdala, cerebellum and caudate nucleus (6). The enzymatic activity of the recombinant protein was determined using a phosphatase coupled assay (7). Source: Recombinant corresponding to aa56-378 from human b-1,3-N-Acetylglucosaminyltransferase 4/B3GNT4, fused to 6-His tag at C-terminal, expressed in CHO cells (Q9C0J1). Molecular Weight: ~37kD Endotoxin: <1.0EU/1ug (LAL) Biological Activity: Measured by its ability to transfer N�acetylglucosamine from UDP�GlcNAc to B�lactose. Specific Activity: >10pmol/min/ug, as measured under the described conditions. Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Catalogue number: 167630
Reactivities: Human
Size: 20ug
Form: Supplied as a liquid in Tris, sodium chloride, Glycerol.
Purity: ~95% (SDS-PAGE)
References: 1. Seko, A. and Yamashita, K. (2005) Glycobiology 15:943. 2. Kataoka, K. and Huh, N.H. (2002) Biochem. Biophys. Res. Commun. 294:843. 3. Iwai,T. et al. (2002) J. Biol. Chem. 277:12802. 4. Togayachi, A. et al. (2001) J. Biol. Chem. 276:22032. 5. Sasaki, K. et al. (1997) Proc. Natl. Acad. Sci. USA 94:14294. 6. Shiraishi, N. et al. (2001) J. Biol. Chem. 276:3498. 7. Wu, Z.L. et al. (2011) Glycobiology 21:727.

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