GALNT7 (NM_017423) Human Tagged ORF Clone Lentiviral Particle

SKU
RC208199L3V
Lenti ORF particles, GALNT7 (Myc-DDK tagged) - Human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7) (GALNT7), 200ul, >10^7 TU/mL
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$1,162.00
5 Weeks*
Specifications
Product Data
Type Human Tagged ORF Clone Lentiviral Particle
Tag Myc-DDK
Target Symbol GALNT7
Synonyms GALNAC-T7; GalNAcT7
Vector pLenti-C-Myc-DDK-P2A-Puro
Mammalian Cell Selection Puromycin
Sequence Data
ORF Nucleotide Sequence
The ORF insert of this clone is exactly the same as(RC208199).
ACCN NM_017423
ORF Size 1971 bp
OTI Disclaimer The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info
OTI Annotation This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene.
Shipping Dry Ice
Reference Data
RefSeq NM_017423.1
RefSeq Size 4339 bp
RefSeq ORF 1974 bp
Locus ID 51809
UniProt ID Q86SF2
Cytogenetics 4q34.1
Domains Glycos_transf_2, RICIN
Protein Families Transmembrane
Protein Pathways Metabolic pathways, O-Glycan biosynthesis
MW 75.4 kDa
Summary This gene encodes GalNAc transferase 7, a member of the GalNAc-transferase family. The enzyme encoded by this gene controls the initiation step of mucin-type O-linked protein glycosylation and transfer of N-acetylgalactosamine to serine and threonine amino acid residues. This enzyme is a type II transmembrane protein and shares common sequence motifs with other family members. Unlike other family members, this enzyme shows exclusive specificity for partially GalNAc-glycosylated acceptor substrates and shows no activity with non-glycosylated peptides. This protein may function as a follow-up enzyme in the initiation step of O-glycosylation. [provided by RefSeq, Jul 2008]
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