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Human B3GALTL Gene ORF cDNA clone in cloning vector

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Human B3GALTL cDNA Clone Product Information
NCBI RefSeq:NM_194318.3
RefSeq ORF Size:1497bp
cDNA Description:Full length Clone DNA of Homo sapiens beta 1,3-galactosyltransferase-like.
Gene Synonym:B3GTL, Gal-T, B3GLCT, B3Glc-T, beta3Glc-T
Species:Human
Vector:pGEM-T Vector
Plasmid:pGEM-B3GALTL
Restriction Site:
Tag Sequence:
Sequence Description:Identical with the Gene Bank Ref. ID sequence except for the point mutations: 665 C/T, 1108 G/A resulting in the amino acid ala substitution by val, gln substitution by lys and 348 T/C not causing the amino acid variation.
Sequencing primers:SP6 and T7 or M13-47 and RV-M
Promoter:
Application:
Antibiotic in E.coli:Ampicilin
Antibiotic in mammalian cell:
Shipping_carrier:Each tube contains lyophilized plasmid.
Storage:The lyophilized plasmid can be stored at room temperature for three months.
pGEM-T Vector Information

The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.

pGEM-T Simple Usage Suggestion:

The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.

Vector Sequence Download
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Background

B3GALTL is a beta-1,3-glucosyltransferase that transfers glucose to O-linked fucosylglycans on thrombospondin type-1 repeats (TSRs) of several proteins. B3GALTL is a type II membrane protein. Defects in B3GALTL gene are a cause of Peters-plus syndrome (PPS). As an O-fucosyltransferase, B3GALTL transfers glucose toward fucose with a beta-1,3 linkage. It specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan.

References
  • Heinonen TY. et al., 2003, Biochem Biophys Res Commun. 309 (1): 166-74.
  • Sato T. et al., 2006, Glycobiology. 16 (12): 1194-206.
  • Kozma K. et al., 2006, J Biol Chem. 281 (48): 36742-51.
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