GALNT7 (NM_017423) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC208199L2V

Lenti ORF particles, GALNT7 (mGFP-tagged) - Human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7) (GALNT7), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Symbol: GALNT7
• Synonyms: GALNAC-T7; GalNAcT7
• Vector: pLenti-C-mGFP
• ACCN: NM_017423
• ORF Size: 1971 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC208199).
• 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.

Reference Data

• RefSeq: NM_017423.1, NP_059119.1
• RefSeq Size: 4339
• RefSeq ORF: 1974
• Locus ID: 51809
• Domains: RICIN, Glycos_transf_2
• Protein Families: Transmembrane
• Protein Pathways: Metabolic pathways, O-Glycan biosynthesis
• MW: 75.4 kDa
• Gene 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]