Description

Background:

Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR plays also a role in T-cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade. Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Plays also a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen.

Product datasheet:

Overview

Product Description  
Species ReactivitiesHuman,Mouse,Rat,Monkey
ImmunogenSynthesized peptide derived from human Syk around the phosphorylation site of Y525.

Properties

FormLiquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions-20°C/1 year
ClonalityPolyclonal

References:

  1. Cloning of the cDNA for the deleted syk kinase homologous to ZAP-70 from human basophilic leukemia cell line (KU812).
    Yagi S., Suzuki K., Hasegawa A., Okumura K., Ra C.
    Biochem. Biophys. Res. Commun. 200:28-34(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex.
    Law C.-L., Sidorenko S.P., Chandran K.A., Draves K.E., Chan A.C., Weiss A., Edelhoff S., Disteche C.M., Clark E.A.
    J. Biol. Chem. 269:12310-12319(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AUTOPHOSPHORYLATION.
  3. DNA sequence and analysis of human chromosome 9.
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC]

    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

  4. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT). Tissue: Eye and Lymph.
  5. Molecular cloning of the human homologue to the pig protein-tyrosine kinase syk.
    Mueller B., Cooper L., Terhorst C.
    Immunogenetics 39:359-362(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-635. Tissue: Tonsil.
  6. Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases.
    Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R., Bolen J.B., Kieff E.
    Immunity 2:155-166(1995) [PubMed] [Europe PMC] Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
  7. Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product.
    Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.
    Immunity 5:591-604(1996) [PubMed] [Europe PMC] Cited for: INTERACTION WITH VAV1.
  8. Phospholipase C-gamma1 interacts with conserved phosphotyrosyl residues in the linker region of Syk and is a substrate for Syk.
    Law C.L., Chandran K.A., Sidorenko S.P., Clark E.A.
    Mol. Cell. Biol. 16:1305-1315(1996) [PubMed] [Europe PMC] Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG1, INTERACTION WITH PLCG1.
  9. Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases.
    Deckert M., Elly C., Altman A., Liu Y.C.
    J. Biol. Chem. 273:8867-8874(1998) [PubMed] [Europe PMC] Cited for: FUNCTION IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL.
  10. Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323.
    Lupher M.L. Jr., Rao N., Lill N.L., Andoniou C.E., Miyake S., Clark E.A., Druker B., Band H.
    J. Biol. Chem. 273:35273-35281(1998) [PubMed] [Europe PMC] Cited for: ENZYME REGULATION, INTERACTION WITH CBL.
external
sizechest(in.)waist(in.)hips(in.)
XS34-3627-2934.5-36.5
S36-3829-3136.5-38.5
M38-4031-3338.5-40.5
L40-4233-3640.5-43.5
XL42-4536-4043.5-47.5
XXL45-4840-4447.5-51.5

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