Ras GAP Antibody (D-6): sc-271436

Ras GAP Antibody (D-6) is a mouse monoclonal IgG2a antibody raised against human Ras GAP (GTPase-activating protein), a crucial regulator of Ras signaling pathways. Anti-Ras GAP antibody (D-6) recognizes an epitope within the Ras GAP immunogen sequence and demonstrates broad species cross-reactivity, detecting Ras GAP in mouse, rat, and human samples through Western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA) applications. Ras GAP functions through a sophisticated molecular mechanism: by promoting GTP hydrolysis to GDP, Ras GAP acts as a molecular brake on p21Ras activity, converting this important signaling protein from its active to inactive state. This regulatory function proves essential for preventing uncontrolled cell proliferation that could lead to cancer development. The complexity of Ras GAP regulation extends through its interactions with other proteins, particularly neurofibromatosis type 1 (NF1), another protein exhibiting GTPase-activating activity. These interconnected regulatory networks highlight how precisely cells control their growth and differentiation signals. When Ras GAP function becomes disrupted through mutations or dysregulation, the resulting loss of control over Ras signaling can contribute to various cancers. Through these diverse cellular functions, Ras GAP (D-6) antibody provides researchers with a valuable tool for investigating both normal signaling mechanisms and cancer biology pathways.

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Ras GAP Antibody (D-6) References:

1. Ras-GAP binding and phosphorylation by herpes simplex virus type 2 RR1 PK (ICP10) and activation of the Ras/MEK/MAPK mitogenic pathway are required for timely onset of virus growth.  |  Smith, CC., et al. 2000. J Virol. 74: 10417-29. PMID: 11044086
2. Signaling of G(alpha)(12) family of G proteins through a tyrosine kinase and a Ras-GAP.  |  Cvejic, S., et al. 2000. Trends Cardiovasc Med. 10: 160-5. PMID: 11239796
3. QM/MM modeling the Ras-GAP catalyzed hydrolysis of guanosine triphosphate.  |  Grigorenko, BL., et al. 2005. Proteins. 60: 495-503. PMID: 15906320
4. Real-time in vitro measurement of intrinsic and Ras GAP-mediated GTP hydrolysis.  |  Shutes, A. and Der, CJ. 2006. Methods Enzymol. 407: 9-22. PMID: 16757310
5. eEF2 and Ras-GAP SH3 domain-binding protein (G3BP1) modulate stress granule assembly during HIV-1 infection.  |  Valiente-Echeverría, F., et al. 2014. Nat Commun. 5: 4819. PMID: 25229650
6. Ras GAP-related and C-terminal domain-dependent localization and tumorigenic activities of IQGAP1 in melanoma cells.  |  Reimer, M., et al. 2017. PLoS One. 12: e0189589. PMID: 29240845
7. Characterization of full-length neurofibromin: tubulin inhibits Ras GAP activity.  |  Bollag, G., et al. 1993. EMBO J. 12: 1923-7. PMID: 8491185
8. Catalytic domain of the p120 Ras GAP binds to RAb5 and stimulates its GTPase activity.  |  Liu, K. and Li, G. 1998. J Biol Chem. 273: 10087-90. PMID: 9553053
9. Sam68 is a Ras-GAP-associated protein in mitosis.  |  Guitard, E., et al. 1998. Biochem Biophys Res Commun. 245: 562-6. PMID: 9571195
10. Ras-GAP controls Rho-mediated cytoskeletal reorganization through its SH3 domain.  |  Leblanc, V., et al. 1998. Mol Cell Biol. 18: 5567-78. PMID: 9710640

The preferred Ras GAP antibody is Ras GAP Antibody (B4F8): sc-63.