EI2BG, Monoclonal Antibody

Translation initiation factor eIF-2B subunit gamma; eIF-2B GDP-GTP exchange factor subunit gamma; EIF2B3

For Research Use Only. Not for use in diagnostic procedures.

Monoclonal

IgG1,k

1778CT889.66.6.54

Mouse

This EI2BG antibody is generated from a mouse immunized with a KLH conjugated synthetic peptide between 110-452 amino acids from human EI2BG.

Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS.

Maintain refrigerated at 2-8 degree C for up to 2 weeks. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Small volumes of anti-EI2BG antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.

Crown Antibodies; New Antibodies

Western Blot (WB), ELISA (EIA)

WB: 1:2000

All lanes : Anti-EI2BG Antibody at 1:2000 dilution
Lane 1: HL-60 whole cell lysate
Lane 2: MCF-7 whole cell lysate
Lane 3: U-2OS whole cell lysate
Lane 4: K562 whole cell lysate

Lysates/proteins at 20 ug per lane.

Secondary
Goat Anti-mouse IgG, (H+L), Peroxidase conjugated at 1/10000 dilution.

Predicted band size : 50 kDa

Blocking/Dilution buffer: 5% NFDM/TBST.

50240 Da

eukaryotic translation initiation factor 2B subunit gamma

translation initiation factor eIF-2B subunit gamma

Translation initiation factor eIF-2B subunit gamma

The protein encoded by this gene is one of the subunits of initiation factor eIF2B, which catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. It has also been found to function as a cofactor of hepatitis C virus internal ribosome entry site-mediated translation. Mutations in this gene have been associated with leukodystrophy with vanishing white matter. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2009]

eIF2B-gamma: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. Defects in EIF2B3 are a cause of leukodystrophy with vanishing white matter (VWM). VWM is a leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or *****hood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy. Belongs to the eIF-2B gamma/epsilon subunits family. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Translation; Translation initiation

Chromosomal Location of Human Ortholog: 1p34.1

Cellular Component: cytoplasm; cytosol; eukaryotic translation initiation factor 2B complex

Molecular Function: guanyl-nucleotide exchange factor activity; protein binding; translation factor activity, nucleic acid binding; translation initiation factor activity

Biological Process: cellular response to stimulus; negative regulation of translation initiation in response to stress; oligodendrocyte development; response to glucose stimulus; response to heat; response to peptide hormone stimulus; translational initiation

Disease: Leukoencephalopathy With Vanishing White Matter

Krueger M.,et al.Proc. Natl. Acad. Sci. U.S.A. 97:8566-8571 (2000). Ota T.,et al.Nat. Genet. 36:40-45 (2004). Bechtel S.,et al.BMC Genomics 8:399-399 (2007). Gregory S.G.,et al.Nature 441:315-321 (2006). Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

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