GALNT1 (NM_020474) Human Tagged ORF Clone Lentiviral Particle

SKU RC214166L4V

Lenti ORF particles, GALNT1 (mGFP-tagged) - Human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) (GALNT1), 200ul, >10^7 TU/mL

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Target Symbol: GALNT1
• Synonyms: GALNAC-T1
• Vector: pLenti-C-mGFP-P2A-Puro
• Mammalian Cell Selection: Puromycin
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC214166).
• ACCN: NM_020474
• ORF Size: 1677 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_020474.2
• RefSeq Size: 3778 bp
• RefSeq ORF: 1680 bp
• Locus ID: 2589
• UniProt ID: Q10472
• Cytogenetics: 18q12.2
• Domains: Glycos_transf_2, RICIN
• Protein Families: Secreted Protein, Transmembrane
• Protein Pathways: Metabolic pathways, O-Glycan biosynthesis
• MW: 64 kDa
• Summary: This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. Transcript variants derived from this gene that utilize alternative polyA signals have been described in the literature. [provided by RefSeq, Jul 2008]