Recombinant Rat Tyrosine-protein kinase Fyn (Fyn)

Code CSB-YP723478RA
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Source Yeast
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Code CSB-EP723478RA
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Source E.coli
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Code CSB-EP723478RA-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP723478RA
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Source Baculovirus
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Code CSB-MP723478RA
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Fyn
Uniprot No.
Alternative Names
FynTyrosine-protein kinase Fyn; EC 2.7.10.2; Proto-oncogene c-Fyn; p59-Fyn
Species
Rattus norvegicus (Rat)
Expression Region
2-537
Target Protein Sequence
GCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
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. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. 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. 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. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. 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. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling.
Gene References into Functions
  1. Fyn binds to mGluR1a at a consensus binding motif located in the intracellular C-terminus (CT) of mGluR1a in vitro. Active Fyn phosphorylates mGluR1a at a conserved tyrosine residue in the CT region. In cerebellar neurons and transfected HEK293T cells, Fyn-mediated tyrosine phosphorylation of mGluR1a is constitutively active and facilitates surface expression of mGluR1a and potentiates mGluR1a postreceptor signaling. PMID: 28948209
  2. the BDNF-Fyn-GluN2B signaling cascade in the spinal dorsal horn may constitute a key mechanism underlying central sensitization and neuropathic pain development after peripheral nerve injury PMID: 28497343
  3. results indicate that D2Rs inhibit SFK (mainly Fyn) phosphorylation in the striatum PMID: 26777117
  4. Results identified Fyn kinase as a molecular mediator of BDNF signaling that activates Erk1/2 and promotes oligodendrocyte myelination PMID: 26449489
  5. Study demonstrated that D1Rs regulate Fyn and downstream NMDA receptors in striatal neurons in vivo, acetylcholine through activating M4Rs inhibited Fyn and NMDA receptors in their sensitivity to D1R signaling PMID: 26277342
  6. These results suggest the critical physiological role of TRL4-Fyn interaction in the modulation of PAI-1-tPA axis in astrocytes during neuroinflammatory responses such as ischemia/reperfusion injuries. PMID: 25106729
  7. The Fyn-mediated NR2B tyrosine phosphorylation, can enhance NMDA receptor function. PMID: 25565773
  8. total levels of ApoER2 and surface levels of ApoER2 are increased by active Fyn PMID: 25340851
  9. Cellular PHLPP2 levels may aggravate oxidative toxicity by suppressing Nrf2/ARE transcriptional regulation via Akt(Se473)/GSK3beta/Fyn kinase axis. PMID: 24675471
  10. Type II PtdIns 4-kinases act downstream of Fyn kinase in Fc-epsilon-RI signaling cascades and are regulated by Fyn kinase. PMID: 24173619
  11. Data indicate a mechanism by which CaMKIIdelta2 and Fyn may coordinately regulate vascular smooth muscle cell motility. PMID: 24003228
  12. tau interacts in a phosphorylation-dependent manner with the PSD95-Fyn-NMDA receptor complex at the postsynaptic site PMID: 22833681
  13. data strongly indicate that Shp2 is essential for the activation of RBL cells in response to FcepsilonRIota aggregation; Shp2 regulates this process through Fyn and Ras with no involvement of PAG PMID: 22802969
  14. our results demonstrate that Fyn kinase downregulates nonmuscle myosin II activity, thus promoting oligodendrocyte morphological differentiation. PMID: 22437915
  15. Slit2 regulates the dispersal of oligodendrocyte precursor cells through Fyn and RhoA signaling. PMID: 22433866
  16. hyperosmotic cholestasis is triggered by a NADPH oxidase-driven reactive oxygen species formation that mediates Fyn-dependent retrieval of the Mrp2 and Bsep from the canalicular membrane, which may involve an increased cortactin phosphorylation. PMID: 22057277
  17. Data show that neither Fyn nor Src knockdown significantly affects basal NR2B expression, but D1 stimulation enhances NR2B insertion into plasma membrane in cultured prefrontal cortex neurons, a process obstructed by Fyn, but not Src, knockdown. PMID: 20569495
  18. in the thymus, Fyn acts as a tyrosine kinase that transduces the leptin signal independently of JAK2 activation, and mediates some of the immunomodulatory effects of leptin in this tissue PMID: 19888448
  19. Increasing the negative surface charge of the cell membrane reduces the amount of Fyn-SH3 domain binding to membrane-associated MBP. PMID: 19178193
  20. These results give support to our hypothesis that Fyn kinase plays a key role in the differentiation process of OLGcs promoted by aTf. PMID: 19115405
  21. Fyn kinase is involved in ethanol-induced phosphorylation of Cbl in rat cerebellum. PMID: 12231245
  22. Association between Fyn and Grin2A increases immediately after induction of transient brain ischemia followed by reperfusion and is maintained for at least 24 h. PMID: 12419528
  23. activation of adenylate cyclase by PACAP(1-38) results in the release of RACK1 from the NMDA receptor and Fyn PMID: 12524444
  24. The brain region-specific compartmentalization of Fyn kinase determines NMDA receptor sensitivity to ethanol PMID: 12736333
  25. An early induction of fyn mRNA in neurons is linked to neuronal activity and the delayed induction of fyn mRNA in reactive astrocytes near the damaged cells may play novel signaling roles during glial response PMID: 14697322
  26. Prion proteins are isolated from neuronal cells, along with Marcks and fyn. PMID: 14741357
  27. findings provide the first description of a mechanism for activation phospholipase D2 in a physiological setting and of a role for Fyn and Fgr in Fc epsilon RI-mediated signaling. PMID: 15282299
  28. Fyn phosphorylates the cytoplasmic domain of nephrin on tyrosine, leading to enhanced association with podocin and downstream signaling of nephrin. PMID: 15579503
  29. These results indicate that Fyn is activated by G-protein-coupled receptor stimulation and is responsible for transactivation of TrkA receptors on intracellular membranes. PMID: 16860569
  30. Fyn, due in part to its effects on Dab1, regulates the phosphorylation, trafficking, and processing of APP and apoEr2. PMID: 18089558
  31. Hypoxia enhanced phosphorylation of three srcFK proteins at Tyr-416 (60, 59, and 54 kDa, corresponding to src, fyn, and yes, respectively) and enhanced srcFK-dependent tyrosine phosphorylation of multiple target proteins. PMID: 18682436
  32. Platelet-derived growth factor PDGF regulates oligodendrocyte precursor cell migration through a signaling cascade coupling Fyn kinase to Cdk5 phosphorylation of WAVE2. PMID: 18701695
  33. tyrosine phosphorylation of Neph1 mediated by Fyn results in significantly increased Neph1 and ZO-1 binding, suggesting a critical role for Neph1 tyrosine phosphorylation in reorganizing the Neph1-ZO-1 complex. PMID: 18922801
  34. Data show that the increase in Fyn expression is converged on ERK1/2 (extracellular signal regulated kinase 1/2) activation on traumatic rats. PMID: 19109931
  35. These results show that oleic acid activates the PKC-Fyn signaling pathway, leading to the disassembly of the adherens junction. PMID: 19166962
  36. Report that full-length and truncated transcripts of Fyn tyrosine protein kinase are expressed during testicular development. PMID: 19441121
  37. We conclude, therefore, that a novel integrin/contactin complex coordinates signals from extracellular matrix and the axonal surface to regulate both oligodendrocyte survival and myelination by controlling Fyn activity PMID: 19625508
  38. Fyn-dependent phosphorylation of CRMP2 at Tyr(32) is involved in Sema3A signaling. PMID: 19652227

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Subcellular Location
Cell membrane.
Protein Families
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
Tissue Specificity
Detected in spinal cord oligodendrocytes (at protein level).
Database Links
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