Slap Antibody (C-7): sc-515453

Slap Antibody (C-7) is a mouse monoclonal IgG1 kappa light chain antibody that detects Slap protein of human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-Slap antibody (C-7) is available as a non-conjugated format, providing researchers with a versatile tool for studying this important protein. Slap protein, also known as Src-like adapter protein, plays a crucial role in cellular signaling pathways by acting as an adapter that links receptor tyrosine kinases to downstream signaling molecules. A unique structure, which includes a single Src homology 2 (SH2) domain and an SH3 domain, allows Slap to interact with various proteins involved in signal transduction, thereby influencing cellular responses to growth factors and other stimuli. The presence of the SH3 domain facilitates binding of proline-rich sequences in target proteins, which is essential for regulation of cellular processes such as proliferation and differentiation. Additionally, distinct N- and C-terminal regions of Slap contribute to specific interactions and regulatory functions, making Slap a vital component in the intricate network of cellular signaling. Slap monoclonal antibody (C-7) enables researchers to gain deeper insights into mechanisms of signal transduction and the role of Slap in various biological contexts.

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Slap Antibody (C-7) References:

1. Oligomerization of dopamine and serotonin receptors.  |  Lee, SP., et al. 2000. Neuropsychopharmacology. 23: S32-40. PMID: 11008065
2. Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.  |  Cicchetti, P., et al. 1992. Science. 257: 803-6. PMID: 1379745
3. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases.  |  Ellis, C., et al. 1990. Nature. 343: 377-81. PMID: 1689011
4. Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complex.  |  Morrison, DK., et al. 1990. Mol Cell Biol. 10: 2359-66. PMID: 1691440
5. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins.  |  Koch, CA., et al. 1991. Science. 252: 668-74. PMID: 1708916
6. Oncogenes and signal transduction.  |  Cantley, LC., et al. 1991. Cell. 64: 281-302. PMID: 1846320
7. Molecular characterization of dopamine receptors.  |  Bates, MD., et al. 1990. Am J Hypertens. 3: 29S-33S. PMID: 2143386
8. Signal transduction by receptors with tyrosine kinase activity.  |  Ullrich, A. and Schlessinger, J. 1990. Cell. 61: 203-12. PMID: 2158859
9. Novel, Selective, and Developable Dopamine D3 Antagonists with a Modified 'Amino' Region.  |  Micheli, F. 2017. ChemMedChem. 12: 1254-1260. PMID: 28426179
10. Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase.  |  Pandey, A., et al. 1995. J Biol Chem. 270: 19201-4. PMID: 7543898
11. Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation.  |  Ravichandran, KS., et al. 1993. Science. 262: 902-5. PMID: 8235613
12. Identification of a ten-amino acid proline-rich SH3 binding site.  |  Ren, R., et al. 1993. Science. 259: 1157-61. PMID: 8438166