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MABS1865

Sigma-Aldrich

Anti-4EBP2 Antibody, clone 16D9.1

clone 16D9.1, from mouse

Synonym(e):

Eukaryotic translation initiation factor 4E-binding protein 2, eIF4E-binding protein 2

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About This Item

UNSPSC-Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Biologische Quelle

mouse

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

16D9.1, monoclonal

Speziesreaktivität

human

Speziesreaktivität (Voraussage durch Homologie)

rat (based on 100% sequence homology), bovine (based on 100% sequence homology)

Verpackung

antibody small pack of 25 μg

Methode(n)

immunohistochemistry: suitable (paraffin)
western blot: suitable

Isotyp

IgG1κ

NCBI-Hinterlegungsnummer

Verwandte Kategorien

Allgemeine Beschreibung

Eukaryotic translation initiation factor 4E-binding protein 2 (UniProt: Q13542; also known as 4E-BP2, eIF4E-binding protein 2) is encoded by the EIF4EBP2 gene (Gene ID; 1979) in human. 4E-BP2 acts as a repressor of translation initiation involved in synaptic plasticity, learning and memory formation. However, insulin and other growth factors can release this inhibition via a phosphorylation-dependent disruption of their binding to eIF4E. 4E-BP2 regulates EIF4E activity by preventing its assembly into the eIF4F complex. 4E-BP2 undergoes phosphorylation at Threonine 37, 46, and 70 and Serine 65 and 83 by mTOR. 4E-BP2 contains a TOR signaling (TOS) motif (aa 116-120) that mediates interaction with RPTOR, leading to promote phosphorylation by mTORC1 complex. Its hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repression of translation. On the other hand, hyperphosphorylated form of 4E-BP2 dissociates from EIF4E, which allows interaction between EIF4G1/EIF4G3 and EIF4E and leads to initiation of translation. 4E-BP2 is first phosphorylated at Threonine 37 and 46 by mTOR that induces folding of region from Proline 18 to Arginine 62 into a four-stranded beta-domain, which sequesters the helical YXXXXLPhi motif into a partly buried beta-strand that blocks accessibility to EIF4E. Protein phosphorylated at Threonine 37 and 46 is, however, unstable. Hence, subsequent phosphorylation at Serine 65 and 83 and Threonine 70 is required to stabilize the fold, which significantly reduces affinity for EIF4E. 4E-BP2 is enriched in brain where it acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation.

Spezifität

Clone 16D9.1 specifically detects eIF4E-binding protein 2 in human cells. It targets an epitope within 16 amino acids from the C-terminal region.

Immunogen

KLH-conjugated linear peptide corresponding to 16 amino acids from the C-terminal region of human eIF4E-binding protein 2.

Anwendung

Research Category
Zelluläre Signaltransduktion
Anti-4EBP2, clone 16D9.1, Cat. No. MABS1865, is a mouse monoclonal antobody that detects eIF4E-binding protein 2 and has been tested for use in Immunohistochemistry (Paraffin) and Western Blotting.
Immunohistochemistry Analysis: A 1:1,000 dilution from a representative lot detected 4EBP2 in human pancreas and human liver tissue sections.

Qualität

Evaluated by Western Blotting in SHSY-5Y cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected 4EBP2 in SHSY-5Y cell lysate.

Zielbeschreibung

~13 kDa observed; 12.94 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Physikalische Form

Protein G purified
Format: Purified
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Lagerung und Haltbarkeit

Stable for 1 year at 2-8°C from date of receipt.

Sonstige Hinweise

Concentration: Please refer to lot specific datasheet.

Haftungsausschluss

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Tobias Hochstoeger et al.
Science advances, 10(7), eadi7830-eadi7830 (2024-02-16)
A central mechanism of mTOR complex 1 (mTORC1) signaling is the coordinated translation of ribosomal protein and translation factor mRNAs mediated by the 5'-terminal oligopyrimidine motif (5'TOP). Recently, La-related protein 1 (LARP1) was proposed to be the specific regulator of

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