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#9046 ARD1A Antibody

CSTコード 包装
希望納入価格 (円)
国内在庫 i
2020年2月21日15時25分 現在
ご登録代理店情報 i
#9046S100 μL58,000

ARD1A 製品一覧

感度分子量 (kDa)抗体の由来貯法
内在性28 Rabbit-20℃
種交差性 (社内試験済)
交差する可能性がある種 i


ヒト、サル -
9046 の推奨プロトコール i

最適な結果を得るために:Cell Signaling Technology (CST) 社は、各製品の推奨プロトコールを使用することを強くお薦めいたします。



ウェスタンブロッティング (1:1000)免疫沈降 (1:50)


内在性レベルのARD1A タンパク質を検出します。高い相同性をもつARD1B タンパク質とは交差しません。由来不明の60 kDa のタンパク質とも交差します。
ヒトのARD1A タンパク質のVal171 周辺領域 (合成ペプチド)

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※下記の社内データは、すべて9046 の推奨プロトコールで実験した結果です。

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using ARD1A Antibody.



Immunoprecipitation of ARD1A from HeLa cell extracts, using Normal Rabbit IgG #2729 (lane 2) or ARD1A Antibody (lane 3). Lane 1 is 10% input. Western blot analysis was performed using ARD1A Antibody.


Protein acetylation is a common modification that occurs both at lysine residues within proteins (ε-amino acetylation) and multiple amino acid residues at the amino terminus of proteins (α-amino acetylation). The N-α-acetyltransferase ARD1 homolog A protein (ARD1A, also known as NAA10) and the highly homologous N-α-acetyltransferase ARD1 homolog B protein (ARD1B, also known as ARD2 or NAA11) are mutually exclusive catalytic subunits of the amino-terminal acetyltransferase complex (NatA) (1-3). This complex, which consists of either ARD1A or ARD1B and the N-α-acetyltransferase 15 (NAA15) auxiliary protein, localizes to ribosomes where it functions to acetylate Ser-, Ala-, Gly-, Thr-, Cys-, Pro-, and Val- amino termini after initiator methionine cleavage during protein translation (1-5). Like ε-amino acetylation, amino-terminal α-amino acetylation functions to regulate protein stability, activity, cellular localization, and protein-protein interactions (4,5). Defects in ARD1A have been shown to cause amino-terminal acetyltransferase deficiency (NATD), which results in severe delays and defects in postnatal growth (6).

In addition to functioning as amino-terminal acetyltransferases in the NatA complex, free ARD1A and ARD1B proteins regulate cell growth and differentiation through ε-amino acetylation of lysine residues in multiple target proteins, including the HIF-1α, β-catenin, and AP-1 transcription factors (7-9). ARD1A-mediated acetylation of HIF-1α at Lys532 under normoxic conditions enhances binding of VHL, leading to increased ubiquitination and degradation of HIF-1α and down-regulation of HIF-1α target genes involved in angiogenesis, apoptosis, cellular proliferation, and glucose metabolism (7). Decreased expression of ARD1A under hypoxic conditions contributes to the stabilization of HIF-1α and upregulation of target genes (7). ARD1A also promotes cell proliferation and tumorigenesis by acetylating and activating β-catenin and AP-1 transcription factors, leading to the stimulation of cyclin D1 expression (8,9). Interestingly, the acetyltransferase activity of ARD1A is regulated by autoacetylation at Lys136, which is required for the ability of ARD1A to promote proliferation and tumorigenesis (9). Research studies have shown that ARD1 proteins are over-expressed in multiple cancers, including breast, prostate, lung, and colorectal cancers (10-13).

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ARD1A Antibody

Immune Cell Signaling Pathways