GTP cyclohydrolase 1 (GCH1) (NM_000161) Human Tagged ORF Clone Lentiviral Particle

SKU RC202893L3V

Lenti ORF particles, GCH1 (Myc-DDK tagged) - Human GTP cyclohydrolase 1 (GCH1), transcript variant 1, 200ul, >10^7 TU/mL

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: Myc-DDK
• Target Symbol: GTP cyclohydrolase 1
• Synonyms: DYT5; DYT5a; DYT14; GCH; GTP-CH-1; GTPCH1; HPABH4B
• 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(RC202893).
• ACCN: NM_000161
• ORF Size: 750 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_000161.2
• RefSeq Size: 2941 bp
• RefSeq ORF: 753 bp
• Locus ID: 2643
• UniProt ID: P30793
• Cytogenetics: 14q22.2
• Domains: GTP_cyclohydroI
• Protein Families: Druggable Genome
• Protein Pathways: Folate biosynthesis, Metabolic pathways
• MW: 27.9 kDa
• Summary: This gene encodes a member of the GTP cyclohydrolase family. The encoded protein is the first and rate-limiting enzyme in tetrahydrobiopterin (BH4) biosynthesis, catalyzing the conversion of GTP into 7,8-dihydroneopterin triphosphate. BH4 is an essential cofactor required by aromatic amino acid hydroxylases as well as nitric oxide synthases. Mutations in this gene are associated with malignant hyperphenylalaninemia and dopa-responsive dystonia. Several alternatively spliced transcript variants encoding different isoforms have been described; however, not all variants give rise to a functional enzyme. [provided by RefSeq, Jul 2008]