Recombinant Mouse Tyrosine-Protein Kinase Lyn (LYN) Protein (His&Myc)

Name: Recombinant Mouse Tyrosine-Protein Kinase Lyn (LYN) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-02851P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Tyrosine-Protein Kinase Lyn (LYN) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P25911
Target Symbol	LYN
Synonyms	Lyn; Tyrosine-protein kinase Lyn; EC 2.7.10.2; V-yes-1 Yamaguchi sarcoma viral related oncogene homolog; p53Lyn; p56Lyn
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	GCIKSKRKDNLNDDEVDSKTQPVRNTDRTIYVRDPTSNKQQRPVPEFHLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLSSKREGFIPSNYVAKVNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDYDPMHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQSDGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEFMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMSALSQGYRMPRMENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP
Expression Range	2-512aa
Protein Length	Full Length of Mature Protein
Mol. Weight	63.7 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-96'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages. Phosphorylates CLNK.
Subcellular Location	Cell membrane. Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Membrane; Lipid-anchor.
Protein Families	Protein kinase superfamily, Tyr protein kinase family, SRC subfamily
Database References	KEGG: mmu:17096 STRING: 10090.ENSMUSP00000038838 UniGene: PMID: 28368000 these findings demonstrated that Lyn overexpression ameliorated airway mucus hypersecretion by down-regulating STAT6 and its binding to the MUC5AC promoter. PMID: 28205598 A novel pancancer mechanism of Lyn-dependent control of epithelial-mesenchymal transition and role of this kinase in tumor progression. PMID: 28288135 these results reveal a role for Lyn as a specific suppressor of the TLR-MyD88-IRF5 pathway and illustrate the importance of fine-tuning IRF5 activity for the maintenance of immune homeostasis PMID: 27521268 These findings reveal that the function and regulation of Lyn during B1 cell B cell receptor signaling is distinct from other B cell subsets. PMID: 27889108 A mutation in LYN, an inhibitory protein tyrosine kinase that is implicated in systemic autoimmunity, combines with an Aire mutation to provoke organ-specific autoimmunity. PMID: 27571405 the Hck, Fgr and Lyn kinases are also necessary for amastigote uptake by macrophages. Src-mediated Arg activation is required for efficient uptake. PMID: 27358479 the Lyn mutation in NOD neutrophils is likely responsible for dysregulation of neutrophil adhesion and directed migration. PMID: 27591397 Our studies indicate not only a concept of mucus hypersecretion in asthma that involves Lyn kinase but also an important therapeutic candidate for asthma. PMID: 28024734 Together, the basal-state signaling checkpoint regulated by LynA expression and degradation and the signaling reorganization initiated by receptor clustering allow cells to discriminate optimally between pathogens and nonpathogens. PMID: 26517880 Oxidized LDL-bound CD36 recruits an Na/K-ATPase-Lyn complex in macrophages that promotes atherosclerosis. PMID: 26350901 Lyn kinase modulates inhibitory signaling to suppress endotoxin-induced lung inflammation. PMID: 26453518 A complex functional interplay between FcgammaRIIa, Lyn, and alphaIIbbeta3 in immune complex-induced platelet activation. PMID: 26291522 report that Lyn is required for bacterial infection-induced recruitment of autophagic components to pathogen-containing phagosomes PMID: 26735693 Data indicate interactions between Ets1 transcription factor and two of its important regulators: Lyn, which maintains Ets1 expression to limit the differentiation of autoreactive plasma cells (PCs), and Btk. PMID: 26209625 results indicate that Lyn plays a positive regulatory role in RIG-I-mediated interferon expression as a downstream component of IPS-1 PMID: 25585356 Fyn, but not Lyn, was required for complete Pyk2 phosphorylation by thrombin. PMID: 25967238 Data show that tyrosine protein kinase Lyn acts as a sensor of hydrogen peroxide (H2O2) levels to facilitate microglial migration toward alpha-Synuclein (alpha-syn). PMID: 25825709 Lyn is a key regulator of survival signaling in plasma cells, limiting plasma cell accumulation and autoimmune disease susceptibility. PMID: 25118329 Lyn is a key regulator of the mucosal immune system, governing pathophysiology in multiple models of intestinal disease. PMID: 25339668 The Src family kinases Hck, Fgr, and Lyn are critical for the generation of the in vivo inflammatory environment without a direct role in leukocyte recruitment. PMID: 25225462 Lyn activity protects mice from DSS colitis and regulates the production of IL-22 from innate lymphoid cells. PMID: 24045577 analyses revealed a SHP2- and Lyn-dependent pathway leading to phosphorylation of Vav1, Rac activation, and F-actin polymerization in SCF-treated BMMCs PMID: 24733849 Data (including data from mutant mice) suggest Lyn facilitates erythrocyte production/erythropoiesis by influencing different stages of erythroid progenitor expansion, differentiation, mature cell development, cell survival, and signal transduction. PMID: 24552351 Data suggest that the tyrosine phosphorylation profile of Lyn in B-lymphocytes is altered in mercury poisoning; Lyn appears to play role as pivotal mediator of mercury immunotoxicity; thus, Lyn is a potential biomarker for mercury exposure. PMID: 24440445 Lyn regulates inflammatory responses in Klebsiella pneumoniae infection via the p38/NF-kappaB pathway. PMID: 24338528 the TAG-1-mediated cell-to-cell interaction between the unpolarized multipolar cells and the pioneering axons regulates the polarization of multipolar cells partly through Lyn kinase and Rac1 PMID: 24559674 B cell-intrinsic Lyn-dependent signaling pathways regulate B cell homeostasis and activation, which in concert with B cell-specific MyD88 signaling pathways can drive the development of autoimmune disease. PMID: 24376269 regulates TGF-beta3 isoform and modulates the development of airway remodeling PMID: 24127553 in contrast to c-Src and Yes, which increase vascular permeability in response to stimuli, Lyn stabilizes endothelial junctions through phosphorylation of FAK. PMID: 24108461 Lyn gene dosage and activity are critical for normal erythropoiesis; constitutively active Lyn alters Epo signaling, which in turn produces erythroid defects. PMID: 23692855 Data show that the hyperresponsive phenotype of B cells lacking Lyn is predicated on significantly increased basal and inducible PI3K activity. PMID: 22777522 Chronic inflammation can induce thymic atrophy and perturb spleen homeostasis in LynDeltaN mice through the increased production of TNFalpha, LTss and TNFR1 signaling. PMID: 23071785 these results indicate that Lyn plays a positive role in TLR4-induced production of TNF-alpha in MCs controlling the activity of the TRAF-6/TAK-1 protein complex. PMID: 22302035 MLR-1023 increased the V(max) of Lyn with an EC(50) of 63 nM. PMID: 22473614 Lyn kinase activator MLR-1023-mediated blood glucose lowering was insulin-dependent. PMID: 22431203 Lyn deficiency disturbs the generation of mature germinal center (GC) B cells and leads to impaired development of mature GCs. PMID: 22942428 This study demonstrates that Lyn is a haploinsufficient gene in autoimmune disease PMID: 22798664 Lyn enhances endotoxin-induced dendritic cell (DC) maturation and modified DC cytokine expression profiles, leading to elevated natural killer (NK) cell IFN-gamma production. PMID: 22491248 Lyn but not Fyn kinase controls IgG-mediated systemic anaphylaxis. PMID: 22450804 The role of the Src family kinase Lyn in the immunomodulatory activities of cathelicidin peptide LL-37 on monocytic cells PMID: 22246800 Lyn-deficient T2 and follicular B cells expressed elevated levels of the pro-apoptotic factor Bim. PMID: 21928281 protein deficiency affects B-cell maturation as well as survival PMID: 22057631 A model in which PECAM-1/SHP-2 complexes, formed in a Lyn-dependent manner, suppress GPVI signaling. PMID: 21297004 Despite possessing enhanced killing, alveolar macrophage Lyn/Fgr/Hck-deficient (triple-knockout) mice do not demonstrate enhanced inflammatory responses to Pneumocystis murina. PMID: 21220696 The results of this study suggested a novel role for Lyn kinase in the regulation of DA release in the mesolimbic system, which leads to the control of alcohol reward. PMID: 21307254 Lyn- and PLC-beta3-dependent regulation of SHP-1 phosphorylation controls Stat5 activity and myelomonocytic leukemia-like disease PMID: 20858858 Although Lyn is involved in dampening the cytokine Toll-like receptor response, Lyn-deficient macrophages and mice still develop microbial tolerance. PMID: 20385881 Lyn B isozyme differs from Lyn A in its association with negative regulatory lipid phosphatase SHIP-1 and in the regulation of calcium responses. PMID: 20308635 Lyn stimulates platelet secretion by activating the phosphoinositide 3-kinase-Akt-nitric oxide (NO)-cyclic GMP pathway and also provide an explanation why Lyn can both stimulate and inhibit platelet activation PMID: 20189992

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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