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EIF4EBP2 Protein, Human, Recombinant (His)

Catalog No. TMPJ-01109

Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 (EIF4EBP2) is a member of the Eukaryotic Translation Initiation Factor 4E Binding Protein Family. EIF4EBP2 regulates eIF4E activity by preventing its assembly into the eIF4F complex, mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. This regulation of is associated to cell proliferation, cell differentiation and viral infection. Phosphorylated EIF4EBP2 on serine and threonine residues in response to insulin, EGF and PDGF.

EIF4EBP2 Protein, Human, Recombinant (His)

EIF4EBP2 Protein, Human, Recombinant (His)

Catalog No. TMPJ-01109
Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 (EIF4EBP2) is a member of the Eukaryotic Translation Initiation Factor 4E Binding Protein Family. EIF4EBP2 regulates eIF4E activity by preventing its assembly into the eIF4F complex, mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. This regulation of is associated to cell proliferation, cell differentiation and viral infection. Phosphorylated EIF4EBP2 on serine and threonine residues in response to insulin, EGF and PDGF.
Pack SizePriceAvailabilityQuantity
10 μg$1847-10 days
50 μg$5457-10 days
500 μg$1,9007-10 days
1 mg$2,7307-10 days
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 (EIF4EBP2) is a member of the Eukaryotic Translation Initiation Factor 4E Binding Protein Family. EIF4EBP2 regulates eIF4E activity by preventing its assembly into the eIF4F complex, mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. This regulation of is associated to cell proliferation, cell differentiation and viral infection. Phosphorylated EIF4EBP2 on serine and threonine residues in response to insulin, EGF and PDGF.
Species
Human
Expression System
E. coli
TagN-6xHis
Accession NumberQ13542
Synonyms
Eukaryotic Translation Initiation Factor 4E-Binding Protein 2,EIF4EBP2,eIF4E-Binding Protein 2,4E-BP2
Amino Acid
Met1-Ile120
Construction
Met1-Ile120
Protein Purity
Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight17 KDa (reducing condition)
Endotoxin< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
FormulationLyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM Tris-HCl, 150 mM NaCl, pH 8.0 .
Reconstitution
Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research Background
Eukaryotic Translation Initiation Factor 4E-Binding Protein 2 (EIF4EBP2) is a member of the Eukaryotic Translation Initiation Factor 4E Binding Protein Family. EIF4EBP2 regulates eIF4E activity by preventing its assembly into the eIF4F complex, mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. This regulation of is associated to cell proliferation, cell differentiation and viral infection. Phosphorylated EIF4EBP2 on serine and threonine residues in response to insulin, EGF and PDGF.

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