Recombinant Human Fyn protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, WB.
>90% Densitometry
Baculovirus infected Sf9 cells
Tag free
SDS-PAGE, WB
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance (PubMed:11536198, PubMed:15489916, PubMed:15557120, PubMed:16387660, PubMed:20100835, PubMed:7568038, PubMed:7822789). Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain (PubMed:15489916). Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions (PubMed:15489916). Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin) (PubMed:17194753). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT (PubMed:14707117, PubMed:15536091). Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage (PubMed:16841086). Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6 (PubMed:14761972, PubMed:18258597, PubMed:19179337). Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein (PubMed:11162638, PubMed:12788081, PubMed:19652227). Involved in reelin signaling by mediating phosphorylation of DAB1 following reelin (RELN)-binding to its receptor (By similarity). Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation (PubMed:22080863). Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation (PubMed:20028775). Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts (PubMed:18056706). CSK maintains LCK and FYN in an inactive form (By similarity). Promotes CD28-induced phosphorylation of VAV1 (PubMed:11005864). In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity). Can also promote CD244-mediated NK cell activation (PubMed:15713798).
Tyrosine-protein kinase Fyn, Proto-oncogene Syn, Proto-oncogene c-Fyn, Src-like kinase, p59-Fyn, SLK, FYN
Recombinant Human Fyn protein is a Human Full Length protein, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, WB.
>90% Densitometry
Baculovirus infected Sf9 cells
Tag free
SDS-PAGE, WB
No
No
Human
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.79% Tris HCl, 0.29% Sodium chloride, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00292% EDTA, 0.00174% PMSF
Liquid
Affinity purified.
Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance (PubMed:11536198, PubMed:15489916, PubMed:15557120, PubMed:16387660, PubMed:20100835, PubMed:7568038, PubMed:7822789). Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain (PubMed:15489916). Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions (PubMed:15489916). Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin) (PubMed:17194753). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT (PubMed:14707117, PubMed:15536091). Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage (PubMed:16841086). Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6 (PubMed:14761972, PubMed:18258597, PubMed:19179337). Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein (PubMed:11162638, PubMed:12788081, PubMed:19652227). Involved in reelin signaling by mediating phosphorylation of DAB1 following reelin (RELN)-binding to its receptor (By similarity). Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation (PubMed:22080863). Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation (PubMed:20028775). Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts (PubMed:18056706). CSK maintains LCK and FYN in an inactive form (By similarity). Promotes CD28-induced phosphorylation of VAV1 (PubMed:11005864). In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity). Can also promote CD244-mediated NK cell activation (PubMed:15713798).
Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.
Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state (PubMed:1699196). PTPRC/CD45 dephosphorylates Tyr-531 leading to activation (PubMed:1533589). Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus (PubMed:15537652). Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (PubMed:22080863). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity).
Nucleus
Dry Ice
-80°C
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
Fyn is a Src family tyrosine kinase with a molecular weight of approximately 59 kDa. It is often referred to as Fyn kinase and plays a significant role in signal transduction processes. This protein is observed in various tissues with high expression in the brain T cells and platelets. Fyn kinase is known for its function in cell communication and regulates different cellular processes in these tissues.
Fyn kinase influences cell growth differentiation and survival. It is a part of larger signaling complexes including those accountable for the development and function of the central nervous system. The protein's activity is important for neural plasticity and supports synaptic communication particularly within the brain. Fyn can interact with other proteins in these complexes to help direct cellular responses to external signals.
Fyn kinase is central to several intracellular signaling pathways such as the T cell receptor (TCR) signaling pathway and the integrin signaling pathway. The TCR signaling pathway involves the regulation of immune responses while the integrin signaling pathway contributes to cell adhesion and migration. Other proteins like Lck and Yes interact with Fyn within these pathways adding another layer of regulation and response in various cell types.
Fyn kinase has associations with Alzheimer's disease and certain types of cancer. In Alzheimer's dysregulation of Fyn activity contributes to synaptic dysfunction and neuronal damage. In cancer aberrant Fyn signaling can affect cellular proliferation and metastasis. Proteins such as Tau in Alzheimer's disease and Src in cancer relate to Fyn through their respective pathological processes.
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SDS-PAGE showing ab85650 at approximately 80kDa.
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