Recombinant Human Tyrosine-protein kinase Lck (LCK)

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Code CSB-EP012806HU
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
IMD22; LCK; Lck p56; LCK proto-oncogene; Src family tyrosine kinase; LCK_HUMAN; Leukocyte C-terminal Src kinase; LSK; Lymphocyte cell specific protein tyrosine kinase; Lymphocyte cell-specific protein-tyrosine kinase; Lymphocyte specific protein tyrosine kinase; Membrane associated protein tyrosine kinase; Oncogene lck; P56 LCK; p56(LSTRA) protein tyrosine kinase; p56-LCK; p56lck; pp58 lck; pp58lck; Protein YT16; Proto oncogene tyrosine protein kinase LCK; Proto-oncogene Lck; Protooncogene tyrosine protein kinase LCK; T cell specific protein tyrosine kinase; T cell-specific protein-tyrosine kinase; T lymphocyte specific protein tyrosine kinase p56lck; Tyrosine-protein kinase Lck; YT 16; YT16
Homo sapiens (Human)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
Protein Length
Full Length of Isoform 3
Tag Info
N-terminal 6xHis-tagged
Liquid or 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.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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°C/-80°C. 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
3-7 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Interacts with FYB2.
Gene References into Functions
  1. The ionic CD3-epsilon -Lck interaction controls the phosphorylation level of the T-cell receptor. PMID: 28659468
  2. a previously unappreciated role for PLC-gamma1 in the positive regulation of Zap-70 and T-cell receptor tyrosine phosphorylation. Conversely, PLC-gamma1 negatively regulated the phosphorylation of SLP-76-associated proteins, including previously established Lck substrate phosphorylation sites within this complex. PMID: 28644030
  3. autophosphorylation of the LCK active-site loop is indispensable for its catalytic activity and LCK can stimulate its own activation by adopting a more open conformation, which can be modulated by point mutations, and CD4 and CD8, T-cell coreceptors, can enhance LCK activity PMID: 29083415
  4. the central biological role of the novel IL-2-R/Lck/PLCgamma/PKCtheta;/alphaPIX/Rac1/PYGM signalling pathway is directly related to the control of fundamental cellular processes such as T cell migration and proliferation. PMID: 27519475
  5. Possible models of regulation of Lck by Aurora-A during T cell activation are described in the review. PMID: 27910998
  6. Mutation of the basic clusters in the CD28 cytoplasmic domain reduced the recruitment to the CD28-Lck complex of protein kinase Ctheta; (PKCtheta;), which serves as a key effector kinase in the CD28 signaling pathway. PMID: 27460989
  7. Data suggest that T cell activation through the TCR complex is accompanied by the de novo activation of T-lymphocyte specific protein tyrosine kinase p56lck (Lck) and that phosphorylation of Tyr(394) plays a role in Lck function that goes beyond inducing an open conformation of the kinase. PMID: 28096507
  8. WASH has a pivotal role for regulation of NK cell cytotoxicity through Lck-mediated Y141 tyrosine phosphorylation. PMID: 27441653
  9. A phosphosite within the SH2 Domain of Lck regulates its activation by CD45. A negative feedback loop that responds to signaling events tunes active Lck amounts and TCR sensitivity. PMID: 28735895
  10. The results have revealed a novel splicing homozygous mutation of LCK that may be responsible for the clinical phenotype of HPV infection from latency to invasive carcinoma. PMID: 27087313
  11. this study show that Lck as a major signaling hub of CD147 in T cells PMID: 28148733
  12. data indicate that HSP65 suppresses cholesterol efflux and increases cellular cholesterol content through an Lck-mediated pathway in T cells PMID: 27742830
  13. LSKlow cells, which are derived from LSK cells in p18(-/-) mice, possess lymphoid differentiation ability and short-term repopulation capability. PMID: 27287689
  14. These results suggest that PM lipids, including phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate, modulate interaction of Lck with its binding partners in the TCR signaling complex and its TCR signaling activities in a spatiotemporally specific manner via its SH2 domain. PMID: 27334919
  15. this study shows that p56(lck), which is essential for activation of T cells through the T-cell receptor, is also critical for signal transduction through Toll-like receptors in T cells PMID: 26888964
  16. Aurora A inhibition causes delocalized clustering of Lck at the immunological synapses and decreases its phosphorylation levels thus indicating Aurora A is required for maintaining Lck active during T-cell activation. PMID: 27091106
  17. Results demonstrate that Lck represses oxidative phosphorylation through competitive binding with mitochondrial CRIF1 in a kinase-independent manner. PMID: 26210498
  18. introducing bulky side-chains into this patch (GGxxG to GVxxL) impairs the Lck-independent role of CD4 in T cell activation upon TCR engagement of agonist and weak agonist stimulation. PMID: 26147390
  19. our results support a novel function of nuclear Lck in promoting human leukemic T cell survival through interaction with a tumor suppressor, CRIF1 PMID: 25997448
  20. TSAD binds to and co-localizes with Nck. Expression of TSAD increases both Nck-Lck and Nck-SLP-76 interaction in T cells. PMID: 26163016
  21. These findings demonstrate highly dynamic Lck palmitoylation kinetics that are essential for signaling downstream of the Fas receptor. PMID: 26351666
  22. Cells from PAX5 translocated patients show LCK up-regulation and over-activation, as well as STAT5 hyper-phosphorylation, compared to PAX5 wt and PAX5 deleted cases. PMID: 25595912
  23. T cell receptor (TCR)-CD3 complex and the Lck kinase were required for Ca(2+) mobilization but not for apoptosis induction in Jurkat cells. PMID: 25947381
  24. In T-cells, cholesterol-dependent domains function in the regulation of the Src family kinase Lck (p56lck) by sequestering Lck from its activator CD45. (Review) PMID: 25658353
  25. Phosphatase CD45 both positively and negatively regulates T cell receptor phosphorylation in reconstituted membrane protein clusters, depending on LCK activity. PMID: 25128530
  26. Lck is retained in the cytosol of CD222-deficient cells, which obstructs the recruitment of Lck to CD45 at the cell surface, resulting in an abundant inhibitory phosphorylation signature on Lck at the steady state. PMID: 25127865
  27. Lck mediates signal transmission from CD59 to the TCR/CD3 pathway in Jurkat T cells. PMID: 24454946
  28. NUP214-ABL1-mediated cell proliferation in T-cell acute lymphoblastic leukemia is dependent on the LCK kinase and various interacting proteins. PMID: 23872305
  29. LCK phosphorylated Tyr-342 of FOXP3 by immunoprecipitation and in vitro kinase assay, and the replacement of Tyr-342 with phenylalanine (Y342F) abolished the ability to suppress MMP9 expression. PMID: 24155921
  30. our data reveal how SAP nucleates a previously unknown signaling complex involving NTB-A and LCK to potentiate restimulation-induced cell death of activated human T cells. PMID: 24688028
  31. Data show a major role for LCK in proximal and distal BCR-mediated signaling in CLL cells and suggest that LCK expression is important in the pathogenesis of CLL. PMID: 23505068
  32. Nef thus interferes with a specialized membrane microdomain-associated pathway for plasma membrane delivery of newly synthesized Lck whose specificity is determined by the affinity of cargo for these sorting platforms. PMID: 23601552
  33. In the absence of FAK, the inhibitory phosphorylation of Lck is impaired. PMID: 24227778
  34. spatial regulation of Lck by CD45 and GM1 ganglioside determines the outcome of apoptotic response to Gal-1 and this local regulation may occur only upon intimate effector (Gal-1 expressing) cell-T-cell attachment. PMID: 24231767
  35. VP11/12 SFK-binding motifs recruit Lck and the activated Src family kinase then leads (directly or indirectly) to phosphorylation of additional motifs involved in recruiting p85, Grb2, and Shc. PMID: 23946459
  36. LCK (lymphocyte-specific protein tyrosine kinase) plays a crucial role in T-cell response by transducing early activation signals triggered by TCR (T-cell receptor) engagement. [REVIEW] PMID: 23931554
  37. conformational states regulate clustering in early T cell signaling PMID: 23202272
  38. T-cell receptor-induced stimulation of T cells led to simultaneous phosphorylation of p56(lck) residues. PMID: 22674786
  39. LCK-positive tumour infiltrate is associated with a significantly longer overall survival and time to relapse in patients with radically resected stage I NSCLC. PMID: 22457183
  40. Data show that cytoskeletal modulation of lipid interactions regulates Lck kinase activity. PMID: 22613726
  41. increases in Ca(2+) lead to CaMKII activation and subsequent Lck-dependent p66Shc phosphorylation on Serine 36. This event causes both mitochondrial dysfunction and impaired Ca(2+) homeostasis, which synergize in promoting Jurkat T-cell apoptosis. PMID: 21983898
  42. The Kv1.3/Dlg1/Lck complex is part of the membrane pathway utilized by cyclic AMP to regulate T-cell function. PMID: 22378744
  43. DHHC2 localizes primarily to the endoplasmic reticulum and Golgi apparatus suggesting that it is involved in S-acylation of newly-synthesized or recycling Lck involved in T cell signalling. PMID: 22034844
  44. the segment comprising residues 112-126 of human LAT is required for its interaction with Lck. PMID: 22034845
  45. Feedback circuits monitor and adjust basal Lck-dependent events in T cell receptor signaling. PMID: 21917715
  46. These results showed that MG132-induced apoptosis was caused by ER stress and subsequent activation of mitochondria-dependent caspase cascade; the presence of p56(lck) enhances MG132-induced apoptosis by augmenting ER stress-mediated apoptotic events. PMID: 21819973
  47. Data show that MAL regulates membrane order and the distribution of microtubule and transport vesicle docking machinery at the IS and, by doing so, ensures correct protein sorting of Lck and LAT to the cSMAC. PMID: 21508261
  48. Deregulations of Lck-ZAP-70-Cbl-b cross-talk and miR181a in T cells were found to be associated with cholesterol-dependent-dismantling of HLA-DR rafts in macrophages in leprosy progression. PMID: 21453975
  49. Preactivated Lck is both necessary and sufficient for T cell activation but remains uncoupled from the T cell receptor in the absence of antigen. PMID: 21266711
  50. Suppressor of cytokine signaling 1 interacts with oncogenic lymphocyte-specific protein tyrosine kinase. PMID: 21234523

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Involvement in disease
Immunodeficiency 22 (IMD22)
Subcellular Location
Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytosol.
Protein Families
Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
Tissue Specificity
Expressed specifically in lymphoid cells.
Database Links

HGNC: 6524

OMIM: 153390

KEGG: hsa:3932

STRING: 9606.ENSP00000337825

UniGene: Hs.470627

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