Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Stimulation of the T cell antigen receptor (TcR) results in protein tyrosine phosphorylation via non-receptor tyrosine kinases. The src-related p59[fyn] kinase is one such enzyme that associates with the TcR. Ligation of the TcR activates the protein kinase activity of p59[fyn] in various human T cells. Fyn interacts with the CD3-ζ chains through its N-terminal region. In turn, fyn binds other proteins through its SH2 and SH3 domains. These proteins (p82 and p116) may serve as substrates and/or mediators of fyn activity. A 72 kDa fyn-related protein binds to the TcR/CD3 complex in certain T cells. This protein, known as p72[fyn-R], is a variant of the fyn kinase and contains at least four novel Ser/Thr phosphorylation sites. These sites may make p72[fyn-R] less susceptible to the action of phosphatases than p59[fyn]. Like p59[fyn], p72[fyn-R] is constitutively associated with its receptor. The exact relationship between these two proteins is not yet clear. However, p72[fyn-R] immunoprecipitates with various antisera raised to either the N- or C-terminus of fyn. Similar to src and yes, fyn is highly expressed in brain. The localization of fyn in mouse brain and its interaction with myelin-associated glycoprotein (MAG) suggests that the fyn kinase has a role in the sensory network and in myelination during early stages of CNS formation.
Development References (4)
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Derkinderen P, Toutant M, Kadare G, Ledent C, Parmentier M, Girault JA. Dual role of Fyn in the regulation of FAK+6,7 by cannabinoids in hippocampus. J Biol Chem. 2001; 276(41):38289-38296. (Clone-specific: Immunoprecipitation, Western blot). View Reference
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Feuillet V, Semichon M, Restouin A. The distinct capacity of Fyn and Lck to phosphorylate Sam68 in T cells is essentially governed by SH3/SH2-catalytic domain linker interactions. Oncogene. 2002; 21(47):7205-7213. (Clone-specific: Immunofluorescence, Western blot). View Reference
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Kawakami T, Kawakami Y, Aaronson SA, Robbins KC. Acquisition of transforming properties by FYN, a normal SRC-related human gene. 1988; 85(11):3870-3874. (Biology). View Reference
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Zeng L, Si X, Yu WP, et al. PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. J Cell Biol. 2003; 160(1):137-146. (Clone-specific: Immunoprecipitation, Western blot). View Reference
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