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Merck

SAB1406936

Sigma-Aldrich

Anti-G3BP1 antibody produced in mouse

purified immunoglobulin, buffered aqueous solution

别名:

G3BP, HDH-VIII, MGC111040

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

mouse

共軛

unconjugated

抗體表格

purified immunoglobulin

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous solution

分子量

antigen ~52.2 kDa

物種活性

human

技術

indirect immunofluorescence: suitable
western blot: 1 μg/mL

NCBI登錄號

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... G3BP1(10146)

一般說明

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

生化/生理作用

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.

外觀

Solution in phosphate buffered saline, pH 7.4

免責聲明

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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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Novel Role of Ras-GTPase Activating Protein SH3 Domain-Binding Protein G3BP in Adhesion and Migration of 32D Myeloid Progenitor Cells.
Schwarz K, et al.
The Open Hematology Journal, 6(1) (2012)
Novel Role of Ras-GTPase Activating Protein SH3 Domain-Binding Protein G3BP in Adhesion and Migration of 32D Myeloid Progenitor Cells.
Schwarz K, et al.
The Open Hematology Journal, 6(1) (2012)
G3BP1 restricts HIV-1 replication in macrophages and T-cells by sequestering viral RNA
Jimenez VC, et al.
Virology, 486, 94-104 (2015)
G3BP1 promotes stress-induced RNA granule interactions to preserve polyadenylated mRNA.
Aulas A, et al.
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.
French J, et al.
The Histochemical Journal, 34(5), 223-231 (2002)

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