"AGO2" Related Products

Recombinant Human EIF2C2, His-tagged

Cat.No.: EIF2C2-2180H
Product Overview: Recombinant Human AGO2(Met 1-Ala 859), fussed with His tag at N-terminal, was expressed in Baculovirus-Insect Cells.
Description: Argonaute 2 (AGO2), also known as Eukaryotic translation initiation factor 2C2 (EIF2C2), belongs to the Argonaute family, AGO subfamily, which is a component of the RNA-induced silencing complex (RISC) and mediates small interfering RNA (siRNA)-directed mRNA cleavage and microRNA translational suppression. AGO2 protein is the catalytic engine of mammalian RNAi. It contains a PIWI domain that is structurally related to RNases H and possibly shares with them a two-metal-ion catalysis mechanism. Human AGO2 was unable to cleave preformed RNA duplexes and exhibited weaker binding affinity for RNA duplexes compared with the single strand RNA. The enzyme exhibited greater RNase H activity in the presence of Mn2+ compared with Mg2+. Human AGO2 exhibited weaker binding affinities and reduced cleavage activities for antisense RNAs with either a 5'-terminal hydroxyl or abasic nucleotide. In mouse hematopoiesis, AGO2 controls early development of lymphoid and erythroid cells. AGO2 is a highly specialized member of the Argonaute family with an essential nonredundant Slicer-independent function within the mammalian miRNA pathway. AGO2 regulates dFMR1 expression, and the relationship between dFMR1 and AGO2 was defined by their physical interaction and co-regulation of downstream targets. AGO2 and dFMR1 are also connected through a regulatory relationship. AGO2 is a regulator of dFMR1 expression and have clarified an important developmental role for AGO2 in the nervous system and germ line that requires dFMR1 function. In addition, AGO2 is regulated at both the transcriptional and posttranslational level, and also implicate AGO2 and enhanced micro-RNA activity in the tumorigenic progression of breast cancer cell lines.
Source: Baculovirus-Insect Cells
Species: Human
Tag: His
Predicted N Terminal: Met
Form: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH7.4,10% glycerol,2mM DTT1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.2. Please contact us for any concerns or special requirements.
Bio-activity: Human AGO2 can bind Let-7a RNA and cleave target RNA (21nt).
Molecular Mass: The recombinant human AGO2 consists of 877 amino acids and predicts a molecular mass of 99 kDa as estimated by SDS-PAGE under reducing conditions.
Protein length: Met 1-Ala 859
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Purity: > 85 % as determined by SDS-PAGE.
Stability: Samples are stable for up to twelve months from date of receipt at -70 centigrade.
Storage: Store it under sterile conditions at -20 centigrade to -80 centigrade. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution. Centrifuge the vial at 4ºC before opening to recover the entire contents.
Gene Name: AGO2 argonaute RISC catalytic component 2 [ Homo sapiens ]
Official Symbol: AGO2
Synonyms: Q10; EIF2C2; protein argonaute-2; CTA-204B4.6; PAZ Piwi domain protein; PPD; argonaute 2; argonaute2; eIF-2C 2; eIF2C 2; eukaryotic translation initiation factor 2C, 2; hAgo2; protein slicer
Gene ID: 27161
mRNA Refseq: NM_012154
Protein Refseq: NP_036286
MIM: 606229
UniProt ID: Q9UKV8
Chromosome Location: 8q24
Pathway: Adaptive Immune System, organism-specific biosystem; Ca2+ pathway, organism-specific biosystem; Downstream signal transduction, organism-specific biosystem
Function: RNA 7-methylguanosine cap binding; RNA polymerase II core binding; core promoter binding

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Optional requirements on this protein    +Expand
C-fusion    N-fusion   Non-tagged
His    GST   Fc   Others
<1.0 eu/μg    <0.1 eu/μg   <0.01 eu/μg   Not required
Monomer Isolation    Dimer Isolation    Not required
>80% by SDS-PAGE    >90% by SDS-PAGE   >95% by SDS-PAGE   Others

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