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Recombinant Human mRNA (2′-O-methyladenosine-N (6)-)-methyltransferase (PCIF1)

ACP10652

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP10652 Target NamePCIF1
Target SynonymsbA465L10.1; C20orf67; Pcif1; PCIF1_HUMAN; PDX1 C terminal inhibiting factor 1; Phosphorylated CTD interacting factor 1; Phosphorylated CTD-interacting factor 1FormLyophilized powder
Expression SystemCustom Production. Please inquire and provide the desire expression system.Expression Range1-704
Protein LengthFull length proteinPurity>85% (SDS-PAGE)
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDQ9H4Z3
Background Information
  • Uniprot Id

    Q9H4Z3

  • Target Species

    Human

  • Target Name

    PCIF1

  • Target Full Name

    mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase

  • Target Function

    Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs. Recruited to the early elongation complex of RNA polymerase II (RNAPII) via interaction with POLR2A and mediates formation of m6A(m) co-transcriptionally.

  • Target Subcellular Location

    Nucleus.

  • Target Tissue Specificity

    Ubiquitous.

  • Target Synonyms

    bA465L10.1; C20orf67; Pcif1; PCIF1_HUMAN; PDX1 C terminal inhibiting factor 1; Phosphorylated CTD interacting factor 1; Phosphorylated CTD-interacting factor 1

  • Target Background

    Enables RNA polymerase II C-terminal domain phosphoserine binding activity; S-adenosyl-L-methionine binding activity; and mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity. Involved in mRNA methylation; negative regulation of translation; and positive regulation of translation. Located in intercellular bridge; microtubule cytoskeleton; and nucleoplasm.

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