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Validated All-in-One™ qPCR Primer for LCK(NM_005356.4) Search again
Product ID:
HQP056250
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
IMD22, LSK, YT16, p56lck, pp58lck
Gene Description:
LCK proto-oncogene, Src family tyrosine kinase
Target Gene Accession:
NM_005356.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules. Multiple alternatively spliced variants, encoding the same protein, have been described. [provided by RefSeq].
Gene References into function
- The association of Lck with c-Cbl in vivo required a functional SH3 domain. These results suggest a model whereby the SH3 domain negatively regulates basal localization of Lck to lipid rafts via association with c-Cbl.
- p56(Lck) targets CD4 to specialized lipid microdomains preferentially localized on microvilli
- Negative regulation of Lck by Cbl ubiquitin ligase
- Lck is required for stromal cell-derived factor 1 alpha (CXCL12)-induced lymphoid cell chemotaxis.
- The activation of Lck in T cells activates apoptotic pathways which are counteracted by Vav and suggests a novel role for costimulation in protecting T cells from CD4-mediated cell death.
- Anti-CD45RO suppressed Src family protein tyrosine kinase p56lck expression in PMNs.
- the distinct potential of Fyn and Lck to phosphorylate Sam68 is likely controlled by the interaction of the kinase SH3 domain with the linker and Sam68, possibly on a competitive binding basis.
- no association between polymorphisms and protein level in type 1 diabetes
- role in signaling through P2X7 receptor in human T cells
- We conclude that the Lck deficiency influences early steps during radiation-induced mitochondrial alterations
- evaluated the role of Lck tyrosine kinase, an early effector of T cell activation, in regulation of the membrane-cytoskeleton linker protein ezrin; results identify ezrin as the first cytoskeletal substrate for Lck
- The exon 7-spliced Lck isoform in T lymphocytes: a potential regulator of p56lck signaling pathways.
- interaction of linker of activated T cells with open-active form of Lck in lipid rafts reveals a new mechanism for the regulation of Lck in T cells
- lck phosphorylation has a role in costimulation with the T-cell receptor during lymphocyte activation
- The costimulatory effects of HCV E2 on T cells depend on CD81 cross-linking that activates Lck through raft aggregation and thus leads to enhanced TCR signaling.
- Analysis of the three-dimensional structure of Lck protein domains.
- protein tyrosine kinase Lck phosphorylates TCRzeta
- lck serine phosphorylation is inhibited by T cell receptor-stimulated generation of hydrogen peroxide
- examined the folding and solution structures of ternary CD4-Lck-Zn2+ and CD8alpha-Lck-Zn2+ complexes;coreceptor tails and the Lck N-terminus are unstructured in isolation but assemble in the presence of zinc to form compactly folded heterodimeric domains
- CD38 initiates and propagates several activating signaling pathways including those with Lck and CD3-zeta
- p56lck in the presence of hypoxia/reoxygenation regulates NFkappaB activation, uPA secretion, and cell motility through tyrosine phosphorylation of IkappaBalpha
- By turning off Lck, Yersinia pestis phosphatase YopH blocks T cell antigen receptor signaling at its very first step, effectively preventing the development of a protective immune response against this lethal bacterium.
- the SD10 region in Lck, which is a novel site involved in substrate recognition, binds to CD45-D2
- Not only is Lck dispensable for T cell activation by bacterial superantigens, but it actively inhibits this signaling pathway.
- p56(lck) in presence of H/R regulates MEK-1-dependent ERK1/2 phosphorylation and uPA secretion through tyrosine phosphorylation of EGF receptor
- Lck and ZAP-70 have roles in the interaction of human MUC1 and beta-catenin in activated Jurkat T cells
- apoptotic effect of Herpesvirus saimiri Tip protein in T cells is mediated by Fas and requires the presence of active Lck in the cell
- direct binding of the hepatitis C virus core to gC1qR on T cells leads to impaired Lck/Akt activation and T-cell function
- following TCR stimulation, activated Lck in human T cells is degraded in the presence of an Hsp90 inhibitor; active Lck levels are influenced by two opposing processes, targeting for degradation by ubiquitination and rescue by Hsp90 monitoring.
- In human, the cytoplasmic domain of ADAM15v2 strongly interacts with Lck and Hck and regulates leukocyte function.
- major role for the common LCK polymorphisms in type 1 diabetes is unlikely.
- Loss of expression of lymphocyte-specific protein tyrosine kinase lck is associated with tumor-infiltrating lymphocytes in renal cancer
- Data suggest that, in addition to their established roles in the initiation of T cell receptor (TCR) signaling, CD45 and Lck may also influence the type of TCR signal generated.
- calculation of the equilibrium binding constant of the phosphotyrosine peptide pYEEI to the Src homology 2 domain of human Lck
- lck degradation plays an important role in the development of activation-induced nonresponsiveness in human cytotoxic T lymphocytes
- intracellular M. leprae activates Erk1/2 directly by p56Lck by means of a PKCepsilon-dependent and MEK-independent signaling pathway
- Lck enhanced Bcl-3-mediated activation of a p52/Bcl-3-responsive promoter in reporter gene assays independent of its tyrosine kinase activity, but requiring the Lck SH3 protein interaction domain
- data suggest that flexibility between SH2 and SH3 domains contributes to the adaptation of Src-family kinases to specific environments and distinct functions
- The difference in the spatio-temporal localization of LCK and ZAP70 proteins following stimulation may eliminate signal crosstalk, and could explain the differentiation of the specific downstream responses of these pathways
- The data show that Shc is connected to the activated TCR via direct interaction with Lck.
- Analysis of the ligand binding specificity of the lymphocyte specific kinase (Lck) SH3 domain.
- Phosphorylation of Tyr315 and Zap70 association with CrkII were both dependent upon the Lck protein tyrosine kinase
- the Lck binding region of SLP-76 is essential for T cell antigen receptor signaling and normal T cell development and function
- Our results suggest the potential involvement of STAT5b in Lck-mediated cellular transformation.
- the cross-talk between Syk and Lck regulates hypoxia/reoxygenation-induced breast cancer progression
- Lck is required for the acute response to hypoxia of human T lymphocytes, as it is necessary to confer oxygen (O2) sensitivity on Kv1.3 channels.
- All lymph node metastases examined showed FAK overexpression, with significant correlation with the expression in matched primary tumor.
- Detection in lymphoma tissue biopsies may be of clinical relevance in predicting response to treatment.
- alternative pathway operates in the absence of Lck-dependent tyrosine-phosphorylation events and was initiated by the T cell receptor-dependent activation of raft-enriched heterotrimeric Galpha11 proteins
- Glucocorticoids causes dissociation of T-cell receptor associated protein complex containing LCK and FYN.
- data demonstrate that growth transformation by herpesvirus saimiri depends on a complex interaction of Tip (tyrosine kinase interacting protein) with the T-cell tyrosine kinase Lck
- Tip LBD1 binding did not cause gross structural changes in Lck SH3 but globally stabilized the domain and reduced the rate of partial unfolding by a factor of five
- Chromium activates epithelial cell Lck to signal for prolonged STAT3 activation and transactivation of interleukin-6, an important immunomodulator of lung disease progression
- These results suggest that competition between Lck-SH3 homodimerization and binding of regulatory proline-rich sequence motifs possibly represents a novel mechanism by which kinase activity is modulated.
- study reveals increased ligand binding affinity of the mutant with the proline to glycine mutation in the Lck SH3 which correlates with a slightly increased flexibility of the RT-loop and an enhanced sampling of ligand binding-competent conformations
- Lck is regulated by a weak tail bite to allow for its activation and service in TCR signaling, perhaps through a competitive SH2 engagement mechanism.
- Microdomain-localized CD45 inactivates Lck and inhibits TCR signaling at the early immune synapse
- the X-ray structure of the lck/imatinib complex confirms that the conformation adopted by lck is distinct from other structurally-characterized src-family kinases and instead resembles kinases abl1 and kit in complex with imatinib.
- sensitivity to apoptosis is regulated through quantitative changes in the stoichiometry of DISC components triggered by p56(Lck) activation and localization.
- activated Ras, Golgi apparatus-localized Lck is needed for the full activation of Raf-1
- Ephrin-B1 is likely to play an important role in the regulation of malignant T lymphocytes through the control of lipid-raft-associated signaling, adhesion, and invasive activity
- Lck-dependent tyrosine phosphorylation of diacylglycerol kinase alpha regulates its membrane association in T cells.(
- lymphocyte-specific protein tyrosine kinase binds to T cell-specific adapter protein (TSAd) prolines and phosphorylates and interacts with the three C-terminal TSAd tyrosines
- HIV-1 Gag directly interacted with the Lck unique domain, targeting HIV-1 Gag to the plasma membrane in T cells
- findings show that low levels of Lck caused a dramatic reduction in c-Cbl phosphorylation and a general reduction in protein ubiquitination after TCR stimulation
- a role of Galphaq in the fine-tuning of proximal TCR signals at the level of Lck and a negative regulatory role of Galphaq in transcriptional activation of cytokine responses.
- Functional integrity of CD28 receptor p56lck transgene and plasma membrane lipid rafts are all prerequisites for up-regulation and long-term expression of Foxp3 mRNA transcripts in CD4positive25(high)Foxp3positive regulatory T cell precursors.
- during T cell activation, Lck is accessible to very subtle regulatory mechanisms