おすすめの製品
由来生物
mouse
品質水準
結合体
unconjugated
抗体製品の状態
purified immunoglobulin
抗体製品タイプ
primary antibodies
クローン
polyclonal
フォーム
buffered aqueous solution
分子量
antigen ~52.2 kDa
化学種の反応性
human
テクニック
indirect immunofluorescence: suitable
western blot: 1 μg/mL
NCBIアクセッション番号
UniProtアクセッション番号
輸送温度
dry ice
保管温度
−20°C
ターゲットの翻訳後修飾
unmodified
遺伝子情報
human ... G3BP1(10146)
詳細
Ras-GAP SH3-domain binding protein stress granule assembly factor 1 (G3BP1) is encoded by the gene mapped to human chromosome 5q33.1– 5q33.3. The encoded protein is composed of 466 amino acids and is a member of the G3BP family. G3BP1 contains an N-terminal nuclear transport factor 2 (NTF2)-like domain, a minimal putative Src homology 3 (SH3) domain binding sequence and an acid rich domain. In addition, it also contains two domains commonly found in RNA binding proteins, an RNA recognition motif (RRM) and an arginine/glycine rich (RGG) domain.
This gene encodes one of the DNA-unwinding enzymes which prefers partially unwound 3′-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. This enzyme is a member of the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. It binds specifically to the Ras-GTPase-activating protein by associating with its SH3 domain. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. (provided by RefSeq)
免疫原
G3BP1 (NP_005745.1, 1 a.a. ~ 466 a.a) full-length human protein.
Sequence
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ
Sequence
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ
生物化学的/生理学的作用
G3BP stress granule assembly factor 1 (G3BP1) plays a vital role in Ras signaling, nuclear factor κB (NFκB) signaling, the ubiquitin proteasome pathway and RNA processing. G3BP1 is also implicated in cancer formation or progression. The encoded protein is required for stress granule (SG) - processing body (PB) interactions and normal SG assembly. G3BP1 inhibits human immunodeficiency virus-1 (HIV-1) replication by binding and sequestering HIV-1 transcripts inside cytosolic organelles.
物理的形状
無色透明のPBS溶液、pH 7.4
免責事項
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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保管分類コード
10 - Combustible liquids
WGK
WGK 1
引火点(°F)
Not applicable
引火点(℃)
Not applicable
最新バージョンのいずれかを選択してください:
Novel Role of Ras-GTPase Activating Protein SH3 Domain-Binding Protein G3BP in Adhesion and Migration of 32D Myeloid Progenitor Cells.
The Open Hematology Journal, 6(1) (2012)
G3BP1 promotes stress-induced RNA granule interactions to preserve polyadenylated mRNA.
The Journal of Cell Biology, 209(1), 73-84 (2015)
The expression of Ras-GTPase activating protein SH3 domain-binding proteins, G3BPs, in human breast cancers.
The Histochemical Journal, 34(5), 223-231 (2002)
G3BP1 restricts HIV-1 replication in macrophages and T-cells by sequestering viral RNA
Virology, 486, 94-104 (2015)
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