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Safety Information

SAB1406936

Sigma-Aldrich

Anti-G3BP1 antibody produced in mouse

purified immunoglobulin, buffered aqueous solution

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Synonym(s):
G3BP, HDH-VIII, MGC111040
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~52.2 kDa

species reactivity

human

technique(s)

indirect immunofluorescence: suitable
western blot: 1 μg/mL

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... G3BP1(10146)

General description

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)

Immunogen

G3BP1 (NP_005745.1, 1 a.a. ~ 466 a.a) full-length human protein.

Sequence
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ

Biochem/physiol Actions

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.

Physical form

Solution in phosphate buffered saline, pH 7.4

Disclaimer

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.

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

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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)
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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