SMG-1 Antibody [L4N6]

Catalog No.: F7448

Application: Reactivity: Human, Monkey

Lane 1: U2OS, Lane 2: 293, Lane 3: MCF7

当該製品は品切れ状态で、ごメールアドレスを教えていただければ、在庫があると、メールで顧客様に伝えます。

代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

Dilution
WB1:1000 IP1:50

Application
WB, IP

Source
Rabbit Monoclonal Antibody

Reactivity
Human, Monkey

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
410 kDa

Datasheet & SDS

生物学的記述

Specificity
SMG-1 Antibody [L4N6] detects endogenous levels of total SMG-1 protein.

Clone
L4N6

Synonym(s)
Serine/threonine-protein kinase SMG1; SMG-1; hSMG-1; Lambda/iota protein kinase C-interacting protein; Lambda-interacting protein; Nonsense mediated mRNA decay-associated PI3K-related kinase SMG1; SMG1; ATX; KIAA0421; LIP

Background
SMG‑1 is a large serine/threonine kinase and a member of the phosphoinositide 3‑kinase‑related kinase (PIKK) family, which includes ATM, ATR, mTOR, DNA‑PKcs, and TRRAP, and it is widely expressed in mammalian cells where it functions as a core regulator of mRNA quality control and stress‑responsive signaling. SMG‑1 forms a stable complex with SMG‑8 and SMG‑9, and this assembly targets the RNA‑binding protein UPF1 (hUpf1) for phosphorylation following recognition of premature termination codons on spliced mRNAs, thereby triggering nonsense‑mediated mRNA decay (NMD) and preventing the accumulation of truncated, nonfunctional or aberrant proteins. SMG‑1 phosphorylates p53 and other substrates in response to DNA damage and genotoxic stress, and it contributes to cell‑cycle control by modulating the G1/S checkpoint through both p53‑dependent and p53‑independent mechanisms, including regulation of Cdc25A and suppression of CDK2 activity. SMG‑1 activity intersects with DNA‑damage and survival pathways, and exhibits the potential to protect cells from extrinsically induced apoptosis by influencing cell‑death‑receptor signaling and by stabilizing anti‑apoptotic regulators such as c‑FLIP, which dampens caspase‑8 activation in response to TNFα and Smac‑mimetic compounds. Loss or inhibition of SMG‑1 increases sensitivity to DNA‑damaging agents and to extrinsic apoptotic stimuli, and reduced SMG‑1 expression or function has been associated with impaired NMD, altered cell‑cycle progression, and either tumor‑suppressive or context‑dependent oncogenic phenotypes in different cancers.

Background

SMG‑1 is a large serine/threonine kinase and a member of the phosphoinositide 3‑kinase‑related kinase (PIKK) family, which includes ATM, ATR, mTOR, DNA‑PKcs, and TRRAP, and it is widely expressed in mammalian cells where it functions as a core regulator of mRNA quality control and stress‑responsive signaling. SMG‑1 forms a stable complex with SMG‑8 and SMG‑9, and this assembly targets the RNA‑binding protein UPF1 (hUpf1) for phosphorylation following recognition of premature termination codons on spliced mRNAs, thereby triggering nonsense‑mediated mRNA decay (NMD) and preventing the accumulation of truncated, nonfunctional or aberrant proteins. SMG‑1 phosphorylates p53 and other substrates in response to DNA damage and genotoxic stress, and it contributes to cell‑cycle control by modulating the G1/S checkpoint through both p53‑dependent and p53‑independent mechanisms, including regulation of Cdc25A and suppression of CDK2 activity. SMG‑1 activity intersects with DNA‑damage and survival pathways, and exhibits the potential to protect cells from extrinsically induced apoptosis by influencing cell‑death‑receptor signaling and by stabilizing anti‑apoptotic regulators such as c‑FLIP, which dampens caspase‑8 activation in response to TNFα and Smac‑mimetic compounds. Loss or inhibition of SMG‑1 increases sensitivity to DNA‑damaging agents and to extrinsic apoptotic stimuli, and reduced SMG‑1 expression or function has been associated with impaired NMD, altered cell‑cycle progression, and either tumor‑suppressive or context‑dependent oncogenic phenotypes in different cancers.

References
[1] Yamashita A, et al. Biochim Biophys Acta. 2005 Dec 30;1754(1-2):305-15. [2] Gubanova E, et al. Cell Cycle. 2013 Dec 15;12(24):3770-80.

PVDFメンブレン孔径参考表

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

技術サポート

ストックの作り方、阻害剤の保管方法、細胞実験や動物実験の際に注意すべき点など、製品を取扱う時に問い合わせが多かった質問に対しては取扱説明書でお答えしています。

Handling Instructions

他に質問がある場合は、お気軽にお問い合わせください。

* 必須

* 大学・企業名 大学・企業名を記入してください

* 名前 名前を記入してください

* 電子メール 電子メール・アドレスを記入してください 有効なメールアドレスを入力してください

電話番号

* 内容 お問い合わせ内容をご入力ください

Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%