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

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
Formation of the EditosomeAPOBEC1;A1CF
Gene ExpressionNR5A1;RRAGB;RNPS1;GTF3AA;ZCRB1;HNRNPA0;ZNF34;TNPO1;TRMT1
mRNA EditingADARB1;ADARB1A;APOBEC1;A1CF
mRNA Editing: C to U ConversionA1CF;APOBEC1

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 bindingRBM23;HNRPKL;THOC3;NOL9;RBMY1F;TNRC6B;RPS3A;RPUSD1;ZBP1
NOT double-stranded RNA binding
nucleotide bindingMRPL23;CRCP;THOC4;TGFBR1B;TOR2A;RBM25;AKT2L;CLCN3;ACVR1L
protein bindingGRB10;UBE2B;F5;CPS1;RFC4;MCM8;WEE1;PTPN4;BRD3
single-stranded RNA bindingAGO1;LONP1;DHX58;LUZP4;JMJD6;RBMX;A1CF;ANXA1;CNBP

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

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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