A1CF

  • Official Full Name

    APOBEC1 complementation factor
  • Overview

    Mammalian apolipoprotein B mRNA undergoes site-specific C to U deamination, which is mediated by a multi-component enzyme complex containing a minimal core composed of APOBEC-1 and a complementation factor encoded by this gene. The gene product has three non-identical RNA recognition motifs and belongs to the hnRNP R family of RNA-binding proteins. It has been proposed that this complementation factor functions as an RNA-binding subunit and docks APOBEC-1 to deaminate the upstream cytidine. Studies suggest that the protein may also be involved in other RNA editing or RNA processing events. Alternative splicing occurs at this locus and three full-length transcript variants, encoding three distinct isoforms, have been described. Additional splicing has been observed but the full-length nature of these variants has not been determined.
  • Synonyms

    A1CF;APOBEC1 complementation factor;ACF;ACF64;ACF65;APOBEC1CF;ASP;apo-B RNA editing protein;APOBEC-1 stimulating protein;apobec-1 complementation factor (ACF) (ASP);RP11-564C4.2;MGC163391

Recombinant Proteins

  • Human
  • Mouse
  • Rat
  • E.coli
  • Mammalian Cell
  • HEK293
  • HEK293T
  • His
  • Non
  • Myc&DDK
  • His&Fc&Avi
Cat.# Product name Source (Host) Species Tag Protein Length Price
A1CF-641H Recombinant Human A1CF Protein, His-tagged E.coli Human His Gly389~Arg587
A1cf-01M Recombinant Mouse A1cf Protein, His-tagged E.coli Mouse His Gly389-Arg588
A1CF-0376H Recombinant Human A1CF Protein (Gly389-Arg587), N-His-tagged E.coli Human His Gly389-Arg587
A1CF-3507H Recombinant Human A1CF protein, His-tagged E.coli Human His 1-122 aa
A1CF-376R Recombinant Rat A1CF Protein Mammalian Cell Rat His
A1CF-9165HCL Recombinant Human A1CF 293 Cell Lysate HEK293 Human Non
A1CF-1197H Recombinant Human A1CF Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Human Myc&DDK
A1cf-1446M Recombinant Mouse A1cf Protein, Myc/DDK-tagged HEK293T Mouse Myc&DDK
A1CF-31R Recombinant Rat A1CF Protein, His (Fc)-Avi-tagged HEK293 Rat His&Fc&Avi
A1CF-31R-B Recombinant Rat A1CF Protein Pre-coupled Magnetic Beads HEK293 Rat

    Involved Pathway

    A1CF involved in several pathways and played different roles in them. We selected most pathways A1CF participated on our site, such as Formation of the Editosome,Gene Expression,mRNA Editing, which may be useful for your reference. Also, other proteins which involved in the same pathway with A1CF were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    mRNA Editing ADARB1A,ADARB1,APOBEC1
    Formation of the Editosome APOBEC1
    Gene Expression ZFP36L1,PAPOLA,PRMT5,C14orf166,SAP130,CDKAL1,ARHGEF38,NR2C2AP,LSM6,MTF2
    mRNA Editing: C to U Conversion APOBEC1

    Protein Function

    A1CF has several biochemical functions, for example, RNA binding,NOT double-stranded RNA binding,nucleotide binding. Some of the functions are cooperated with other proteins, some of the functions could acted by A1CF itself. We selected most functions A1CF had, and list some proteins which have the same functions with A1CF. You can find most of the proteins on our site.

    Function Related Protein
    RNA binding EIF1AXB,RPS3,RPL29,PAPOLA,RBM46,RNASEH1,FARSB,NOL3,RPLP1,PTBP1
    nucleotide binding BOLL,NAIP1,RBM3,SEPT9A,ARL3L1,STK30,ACVR1L,MOV10B.1,NT5C2,RBM20
    protein binding RPP25,RUSC2,SSTR2,OSTB,RAD9A,UBQLN4,COLQ,ULK2,MEIOB,ACVRL1
    single-stranded RNA binding NXF1,EIF2C3,STRBP,POLR2GL,LONP1,AGO3,HNRNPA1,POLR2G,ANXA1,ZFP36

    Interacting Protein

    A1CF has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with A1CF here. Most of them are supplied by our site. Hope this information will be useful for your research of A1CF.

    REL;TRAF1;FHL3;uvrB;ssrna_au

    Resources

    References

    • Nonaka, T; Doi, T; et al. Carboxy-terminal domain of AID required for its mRNA complex formation in vivo. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 106:2747-2751(2009).
    • Conticello, SG; et al. The AID/APOBEC family of nucleic acid mutators. GENOME BIOLOGY 9:-(2008).

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