4E-BP1 (Phospho-Thr70) Antibody

Description

Product Name 4E-BP1 (Phospho-Thr70) Antibody
Host Species Rabbit
Clonality Polyclonal
Purification Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Applications IHC
Species Reactivity Hu
Specificity The antibody detects endogenous levels of 4E-BP1 only when phosphorylated at threonine 70.
Immunogen Type Peptide-KLH
Immunogen Description Peptide sequence around phosphorylation site of threonine70 (T-K-T(p)-P-P) derived from Human 4E-BP1.
Target Name 4E-BP1
Modification Phospho-Thr70
Alternative Names 4EBP1; P/OKCL.6; P/OKCL.6; PHAS-I;
Accession No. Swiss-Prot#: Q13541;
NCBI Gene#: 1978;
NCBI Protein#: NP_004086.1.
SDS-PAGE MW 12kd
Concentration 1.0mg/ml
Formulation Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Storage Store at -20˚C/1 year

Application Details

Immunohistochemistry: 1:50~1:100

Images

Immunohistochemical analysis of paraffin-embedded human colon carcinoma tissue using 4E-BP1 (Phospho-Thr70) antibody #AB11781 (left)or the same antibody preincubated with blocking peptide (right).

Background

4E-BP1 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.

Pause A., Nature 371:762-767(1994).
Gevaert K., Nat. Biotechnol. 21:566-569(2003).
Haghighat A., EMBO J. 14:5701-5709(1995).

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