GTP cyclohydrolase 1 (GCH1) (NM_001024024) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC224968L3V

  • LentiORF®

Lenti ORF particles, GCH1 (Myc-DDK-tagged)-Human GTP cyclohydrolase 1 (GCH1), transcript variant 2, 200ul, >10^7 TU/mL

ORF Plasmid: DDK tGFP

Lentiviral Particles: DDK w/ Puro mGFP w/ Puro

AAV Particle: DDK


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USD 850.00

7 Weeks*

Size
    • 200 ul

Product Images

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Specifications

Product Data
Type Human Tagged ORF Clone Lentiviral Particle
Tag Myc-DDK
Symbol GTP cyclohydrolase 1
Synonyms DYT5; DYT5a; DYT14; GCH; GTP-CH-1; GTPCH1; HPABH4B
Mammalian Cell Selection Puromycin
Vector pLenti-C-Myc-DDK-P2A-Puro
ACCN NM_001024024
ORF Size 750 bp
Sequence Data
The ORF insert of this clone is exactly the same as(RC224968).
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_001024024.1, NP_001019195.1
RefSeq Size 1995 bp
RefSeq ORF 753 bp
Locus ID 2643
UniProt ID P30793
Cytogenetics 14q22.2
Protein Families Druggable Genome
Protein Pathways Folate biosynthesis, Metabolic pathways
MW 27.9 kDa
Gene 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]

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