G3BP2 Antibody #31799
Filter:
- WB
- IP
- IF
Supporting Data
REACTIVITY | H M R Mk |
SENSITIVITY | Endogenous |
MW (kDa) | 60, 70 |
SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunoprecipitation | 1:50 |
Immunofluorescence (Immunocytochemistry) | 1:100 - 1:400 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
G3BP2 Antibody recognizes endogenous levels of total G3BP2 protein. This antibody does not cross-react with G3BP1 protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human G3BP2 protein. Antibodies are purified by peptide affinity chromatography.
Background
Stress granules (SGs) are cytoplasmic mRNA-protein condensates formed in response to cellular stressors, such as oxidative stress, ultraviolet radiation, and viral infection (1). The Ras GTPase-activating protein-binding proteins (G3BPs), consisting of G3BP1 and G3BP2, are key nucleating factors essential for SG formation (2). As their name suggests, G3BPs were originally identified as proteins that interact with the SH3 domain of Ras GTPase-activating protein (RasGAP) (3). However, a recent study argues that G3BP1 may not be a genuine RasGAP-binding partner, suggesting that further studies are necessary to validate this function (4). Rather, G3BPs are well known to be involved in mRNA decay and inhibition of translation initiation (5,6). The SARS-CoV-2 virus has also been reported to target G3BPs via interaction between the viral N protein and the N-terminal domain of G3BP. This binding prevents G3BPs from interacting with other SG-associated proteins, therefore suppressing SG assembly and promoting viral replication (7). G3BP2, in particular, has also been reported to play a role in the initiation of breast tumor formation and affect the expression of PD-L1 in breast and glioblastoma cells under stress conditions (8,9).
- Riggs, C.L. et al. (2020) J Cell Sci 133, jcs242487. doi: 10.1242/jcs.242487.
- Wang, F. et al. (2020) Pharmacol Res 161, 105143.
- Parker, F. et al. (1996) Mol Cell Biol 16, 2561-9.
- Annibaldi, A. et al. (2011) PLoS One 6, e29024.
- Fischer-Kešo, R. et al. (2014) Mol Cell Biol 34, 4244-56.
- Fischer, J.W. et al. (2020) Mol Cell 78, 70-84.e6.
- Luo, L. et al. (2021) Sci Bull (Beijing) 66, 1194-1204.
- Gupta, N. et al. (2017) Proc Natl Acad Sci USA 114, 1033-1038.
- Zhang, Y. et al. (2021) Mol Oncol, doi: 10.1002/1878-0261.12915.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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