eIF4A3 Recombinant Rabbit Monoclonal Antibody [JG35-33]
ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation.
Product Specifications
CAS Number
9000-83-3
Product Name Alternative
Abbreviation
eIF-4A-III, NMP 265, hNMP 265, EIF4A3, DDX48, KIAA0111
Swiss Prot
P38919 Human, Q91VC3 Mouse, Q3B8Q2 Rat
Cellular Locus
Cytoplasm, Nucleus, Spliceosome.
Host
Rabbit
Species Reactivity
Human,Mouse,Rat
Immunogen
Recombinant protein within N-terminal Human eIF4A3 .
Isotype
IgG
Conjugation
Non-conjugated
Type
Recombinant Rabbit monoclonal Antibody
Applications
WB, IHC-P, FC, IF-Cell, IF-Tissue, IP
Positive Control
Concentration
1 mg/mL
Dilution
WB: 1:500-1:1,000;IF-Cell: 1:50-1:200;IF-Tissue: 1:50-1:200;IHC-P: 1:50-1:200;FC: 1:50-1:100;IP: Use at an assay dependent concentration.
Purity
Protein A affinity purified.
Form
Liquid
Buffer
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Molecular Weight
Predicted band size: 47 kDa
Storage Conditions
Store at +4°C after thawing. Aliquot store at -20°C. Avoid repeated freeze/thaw cycles.
Recombinant Antibody
Yes
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