Technical Data
035015
EIF4EBP1, ID (EIF4EBP1, Eukaryotic translation initiation factor 4E-binding protein 1, Phosphorylated heat- and acid-stable protein regulated by insulin 1)
Description:
This gene encodes one member of a family of translation repressor proteins. The protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation. [provided by RefSeq].

Applications:
Suitable for use in Western Blot, Immunohistochemistry, Flow Cytometry, ELISA

Recommended Dilution:
ELISA: 1:1,000
Western Blot: 1:50-100
Immunohistochemistry: 1:10-50
Flow Cytometry: 1:10-50

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabIgGPurified
SizeStorageShippingSourceHost
200ul-20CBlue IceHumanRabbit
Concentration:
As reported
Immunogen:
EIF4EBP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 38-69 amino acids from the Central region of human EIF4EBP1.
Purity:
Purified by saturated ammonium sulfate precipitation followed by dialysis against PBS.
Form
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide.
Specificity:
Human
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
She, Q.B., et al. Cancer Cell 18(1):39-51(2010)
Aoyagi, M., et al. Proc. Natl. Acad. Sci. U.S.A. 107(6):2640-2645(2010)
Naukkarinen, J., et al. PLoS Genet. 6 (6), E1000976 (2010) :
Kumar, A., et al. PLoS ONE 5 (1), E8730 (2010) :
Villalonga, P., et al. J. Biol. Chem. 284(51):35287-35296(2009)