Recombinant Human FYN-binding protein(FYB)

Code CSB-YP009099HU
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Source Yeast
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Code CSB-EP009099HU
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Source E.coli
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Code CSB-EP009099HU-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-BP009099HU
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Source Baculovirus
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Code CSB-MP009099HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names FYB1
Uniprot No. O15117
Alternative Names ADAP; Adhesion and degranulation promoting adaptor protein; FYB 120/130; Fyb; FYB-120/130; FYB_HUMAN; FYN binding protein; FYN T binding protein; FYN-binding protein; FYN-T-binding protein; p120/p130; PRO0823; SLAP 130; SLAP-130; SLAP130; SLP 76 associated phosphoprotein; SLP-76-associated phosphoprotein; SLP76 associated phosphoprotein
Species Homo sapiens (Human)
Expression Region 1-783
Target Protein Sequence MAKYNTGGNP TEDVSVNSRP FRVTGPNSSS GIQARKNLFN NQGNASPPAG PSNVPKFGSP KPPVAVKPSS EEKPDKEPKP PFLKPTGAGQ RFGTPASLTT RDPEAKVGFL KPVGPKPINL PKEDSKPTFP WPPGNKPSLH SVNQDHDLKP LGPKSGPTPP TSENEQKQAF PKLTGVKGKF MSASQDLEPK PLFPKPAFGQ KPPLSTENSH EDESPMKNVS SSKGSPAPLG VRSKSGPLKP AREDSENKDH AGEISSLPFP GVVLKPAASR GGPGLSKNGE EKKEDRKIDA AKNTFQSKIN QEELASGTPP ARFPKAPSKL TVGGPWGQSQ EKEKGDKNSA TPKQKPLPPL FTLGPPPPKP NRPPNVDLTK FHKTSSGNST SKGQTSYSTT SLPPPPPSHP ASQPPLPASH PSQPPVPSLP PRNIKPPFDL KSPVNEDNQD GVTHSDGAGN LDEEQDSEGE TYEDIEASKE REKKREKEEK KRLELEKKEQ KEKEKKEQEI KKKFKLTGPI QVIHLAKACC DVKGGKNELS FKQGEQIEII RITDNPEGKW LGRTARGSYG YIKTTAVEID YDSLKLKKDS LGAPSRPIED DQEVYDDVAE QDDISSHSQS GSGGIFPPPP DDDIYDGIEE EDADDGFPAP PKQLDMGDEV YDDVDTSDFP VSSAEMSQGT NVGKAKTEEK DLKKLKKQEK EEKDFRKKFK YDGEIRVLYS TKVTTSITSK KWGTRDLQVK PGESLEVIQT TDDTKVLCRN EEGKYGYVLR SYLADNDGEI YDDIADGCIY DND
Protein Length Full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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
Protein 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
Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton. Modulates the expression of IL2. Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.
Gene References into Functions
  1. results of this study indicate that a novel T cell adaptor protein, activation-dependent, raft-recruited ADAP-like phosphoprotein (ARAP), plays a unique role in T cells as a part of both the proximal activation signaling and inside-out signaling pathways that result in integrin activation and T cell adhesion PMID: 27335501
  2. Ubc9 is an essential regulator of ADAP where it is required for TCR-induced membrane recruitment of the small GTPase Rap1 and its effector protein RapL and for activation of the small GTPase Rac1 in T cell adhesion. PMID: 29127148
  3. Current knowledge of the functions of the adapter protein ADAP in T cell signaling with a focus on the role of individual phosphotyrosine (pY) motifs for SH2 domain mediated interactions is presented. PMID: 27258783
  4. A distinct set of proteins interaction partners required for chemokine-directed T cell migration is attracted by phosphotyrosine 571 of ADAP, including ZAP70. PMID: 26246585
  5. FYB nonsense mutations in humans causing small-platelet thrombocytopenia and a significant bleeding tendency. PMID: 25876182
  6. Data (including data from studies in knockout/transgenic mice) suggest that ADAP regulates positive feedback loop of TGFbeta1 production and TGFbeta1-induced CD103 expression in CD8+ T-lymphocytes and protects against influenza H5N1 virus infection. PMID: 25909459
  7. The aim of this study was to perform an association study between seven Fyn-binding protein gene (FYB)-tag single nucleotide polymorphisms (SNPs) and type I diabetes mellitus (T1DM), as well as with disease age of onset. PMID: 25729932
  8. The autosomal recessive bleeding phenotype seen in several members of this highly consanguineous family included petechial rash, mild epistaxis and thrombocytopenia with some decrease in platelet volume. These clinical findings, together with the results of exome sequencing pointed to only one strong candidate gene, the FYB gene. PMID: 25516138
  9. ADAP interacts with talin and kindlin-3 to promote platelet Integrin alphaIIbbeta3 activation and stable fibrinogen binding. PMID: 24523237
  10. ADAP and Nck adapter proteins cooperatively facilitate T cell adhesion to the LFA-1 ligand ICAM-1. PMID: 24769494
  11. These findings indicate that ADAP regulates two steps of HIV-1 infection cooperatively with two distinct receptors, and as such, serves as a new potential target in the blockade of HIV-1 infection. PMID: 24047317
  12. our findings indicate an association between polymorphisms located in FYB gene and SLE, suggesting their possible involvement in disease susceptibility and clinical manifestations. PMID: 23628395
  13. Multipoint binding of SLP-76 to ADAP facilitates the assembly of SLP-76 microclusters. PMID: 23979596
  14. TM4SF10, possibly through ADAP, may regulate Fyn activity PMID: 21881001
  15. a functional cooperation between Nck and ADAP in stabilizing the recruitment of WASp to SLP76 regulates actin rearrangement. PMID: 21536650
  16. the ADAP CARMA1 binding site is required for IKK gamma ubiquitination; both TAK1 and CARMA1 binding sites are required for IkappaB alpha phosphorylation and degradation and NF-kappaB nuclear translocation PMID: 20164171
  17. Mass spectrometric identification of ADAP associated with EVL, an actin-binding protein of the ENA/VASP family, DOCK2 and GEF-H1 suggests a direct link between ADAP and the cytoskeleton. PMID: 19798671
  18. ADAP lipid interaction defines the helically extended SH3 scaffold as a novel member of membrane interaction domains PMID: 15843031
  19. show in an ADAP-deficient Jurkat T cell line that the co-dependence of ADAP and SKAP55 extends beyond their functional and physical interactions and show that SKAP55 protein is unstable in the absence of ADAP PMID: 15849195
  20. Lipid binding of ADAP at the immunological synapse most likely contributes to the function of ADAP as a regulator of T cell migration and adhesion. PMID: 16831444
  21. An eight-membered ring formed upon oxidation of two neighboring cysteines leads to significant changes in the variable arginine-threonine (RT) loop of the hSH3N domain of this protein. PMID: 17511475
  22. ADAP-deficient T-cell-receptor transgenic T cells demonstrate that ADAP is a positive regulator of antigen-dependent, LFA-1 integrin-mediated T cell conjugate formation with antigen presenting cells. PMID: 17785790
  23. Naive transgenic ADAP-deficient T cells show impaired adhesion to ovalbumin fragment-bearing antigen-presenting cells that is restored following reconstitution with wild-type ADAP. PMID: 18802088

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Involvement in disease Thrombocytopenia 3 (THC3)
Subcellular Location Cytoplasm. Nucleus. Cell junction.
Tissue Specificity Expressed in hematopoietic tissues such as myeloid and T-cells, spleen and thymus. Not expressed in B-cells, nor in non-lymphoid tissues.
Database Links

HGNC: 4036

OMIM: 273900

KEGG: hsa:2533

UniGene: Hs.370503

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