Translational Control
Phospho-eIF2α (Ser51) Blocking Peptide
|
イイネ!(0)
|
|
| CSTコード |
包装 |
希望納入価格 (円) |
国内在庫  |
ご登録代理店情報  カスタマー情報にご登録いただいた代理店を表示しています。
ご登録代理店の変更は こちら。 |
| #1221S | 100 μg | 16,000 | |
|
eIF2A抗体製品一覧
| 使用目的 | |
| Phospho-eIF2α (Ser51) (119A11) Rabbit mAb (#3597) とPhospho-eIF2α (Ser51) (D9G8) XP® Rabbit mAb (#3398) の反応をブロックし、抗体の反応特異性を確認するために使用 |
IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human lung carcinoma, using Phospho-eIF2alpha (Ser51) (119A11) Rabbit mAb (#3597) in the presence of control peptide (left) or Phospho-eIF2alpha (Ser51) Blocking Peptide (right).
Phosphorylation of the eukaryotic initiation factor 2 (eIF2) α subunit is a well-documented mechanism to downregulate protein synthesis under a variety of stress conditions. eIF2 binds GTP and Met-tRNAi and transfers Met-tRNA to the 40S subunit to form the 43S preinitiation complex (1,2). eIF2 promotes a new round of translation initiation by exchanging GDP for GTP, a reaction catalyzed by eIF2B (1,2). Kinases that are activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), or heme deficiency (HRI) can phosphorylate the α subunit of eIF2 (3,4). This phosphorylation stabilizes the eIF2-GDP-eIF2B complex and inhibits the turnover of eIF2B. Induction of PKR by IFN-γ and TNF-α induces potent phosphorylation of eIF2α at Ser51 (5,6).
-
Kimball, S.R. (1999) Int. J. Biochem. Cell Biol. 31, 25-29.
-
De Haro, C. et al. (1996) FASEB J. 10, 1378-1387.
-
Kaufman, R.J. (1999) Genes Dev. 13, 1211-1233.
-
Sheikh, M.S. and Fornace Jr., A.J. (1999) Oncogene 18, 6121-6128.
-
Cheshire, J.L. et al. (1999) J. Biol. Chem. 274, 4801-4806.
-
Zamanian-Daryoush, M. et al. (2000) Mol. Cell. Biol. 20, 1278-1290.