MTHFD1 (NM_005956) Human Tagged ORF Clone Lentiviral Particle

SKU RC200297L3V

Lenti ORF particles, MTHFD1 (Myc-DDK tagged) - Human methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase (MTHFD1), 200ul, >10^7 TU/mL

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: Myc-DDK
• Target Symbol: MTHFD1
• Synonyms: CIMAH; MTHFC; MTHFD
• 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(RC200297).
• ACCN: NM_005956
• ORF Size: 2805 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_005956.2, NP_005947.2
• RefSeq Size: 3466 bp
• RefSeq ORF: 2808 bp
• Locus ID: 4522
• UniProt ID: P11586
• Cytogenetics: 14q23.3
• Domains: FTHFS, THF_DHG_CYH
• Protein Families: Druggable Genome, Stem cell - Pluripotency
• Protein Pathways: Glyoxylate and dicarboxylate metabolism, Metabolic pathways, One carbon pool by folate
• MW: 101.5 kDa
• Summary: This gene encodes a protein that possesses three distinct enzymatic activities, 5,10-methylenetetrahydrofolate dehydrogenase, 5,10-methenyltetrahydrofolate cyclohydrolase and 10-formyltetrahydrofolate synthetase. Each of these activities catalyzes one of three sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses. The trifunctional enzymatic activities are conferred by two major domains, an aminoterminal portion containing the dehydrogenase and cyclohydrolase activities and a larger synthetase domain. [provided by RefSeq, Jul 2008]