NFYA (NM_021705) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC205981L3V

Lenti ORF particles, NFYA (Myc-DDK tagged) - Human nuclear transcription factor Y, alpha (NFYA), transcript variant 2, 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: Myc-DDK
• Symbol: NFYA
• Synonyms: CBF-A; CBF-B; HAP2; NF-YA
• Mammalian Cell Selection: Puromycin
• Vector: pLenti-C-Myc-DDK-P2A-Puro
• ACCN: NM_021705
• ORF Size: 954 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC205981).
• 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_021705.2
• RefSeq Size: 6149 bp
• RefSeq ORF: 957 bp
• Locus ID: 4800
• UniProt ID: P23511
• Cytogenetics: 6p21.1
• Domains: CBF
• Protein Families: Transcription Factors
• Protein Pathways: Antigen processing and presentation
• MW: 33.9 kDa
• Gene Summary: The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms. [provided by RefSeq, Jul 2008]