Anti-MYLK Antibody

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D162809 Anti-MYLK antibody Cat. No. D162809 Package 25 μl/100 μl/200 μl Storage -20°C, pH7.4 PBS, 0.05% NaN3, 40% Glycerol Product overview Description A n ti-MYLK rabbit polyclonal antibody Applications ELISA, IHC Immunogen Synthetic peptide of human MYLK Reactivity Human, Mouse Content 0 .5 mg/ml Host species Rabbit Ig class Immunogen-specific rabbit IgG Purification Antigen affinity purification Target information Symbol MYLK Full name myosin light chain kinase Synonyms KRP; AAT7; MLCK; MLCK1; MYLK1; smMLCK; MLCK108; MLCK210; MSTP083 Swissprot Q15746 Target Background This gene, a muscle member of the immunoglobulin gene superfamily, encodes myosin light chain kinase which is a calcium/calmodulin dependent enzyme. This kinase phosphorylates myosin regulatory light chains to facilitate myosin interaction with actin filaments to produce contractile activity. This gene encodes both smooth muscle and nonmuscle isoforms. In addition, using a separate promoter in an intron in the 3' region, it encodes telokin, a small protein identical in sequence to the C-terminus of myosin light chain kinase, that is independently expressed in smooth muscle and functions to stabilize unphosphorylated myosin filaments. A pseudogene is located on the p arm of chromosome 3. Four transcript variants that produce four isoforms of the calcium/calmodulin dependent enzyme have been identified as well as two transcripts that produce two isoforms of telokin. Additional variants have been identified but lack full length transcripts. Sangon Biotech Applications Immunohistochemistry Predicted cell location: Cytoplasm Predicted cell location: Cytoplasm Positive control: Human liver cancer Positive control: Human esophagus cancer Recommended dilution: 25-100 Recommended dilution: 25-100 The image on the left is immunohistochemistry of paraffin-embedded The image on the left is immunohistochemistry of paraffin-embedded Human liver cancer tissue using D162809(MYLK Antibody) at Human esophagus cancer tissue using D162809(MYLK Antibody) at dilution 1/25, on the right is treated with synthetic peptide. (Original dilution 1/25, on the right is treated with synthetic peptide. (Original magnification: ×200) magnification: ×200) ELISA Recommended dilution: 5000-10000 Sangon Biotech.

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Structural Insight Into the Environment of the Serine/Threonine Protein Kinase Domain of Titin
Structural insight into the environment of the serine/threonine protein kinase domain of titin Dissertation zur Erlangung des akademischen Grades des Doktors der Naturwissenschaften an der Universitat¨ Konstanz Mathematisch-Naturwissenschaftliche Sektion Fachbereich Biologie vorgelegt von Simone Muller¨ Tag der mundlichen¨ Prufung:¨ 30.03.2006 1. Referent: Prof. Dr. Wolfram Welte 2. Referent: PD Dr. Matthias Wilmanns 3. Referent: Prof. Dr. Helmut Plattner Contents Abbreviations ix Summary xi Zusammenfassung xiii 1 Introduction 1 1.1 Striated muscle and the structure of the sarcomere . 1 1.2 Titin . 3 1.3 Structure and function of titin . 5 1.3.1 Z-disc and anchoring of titin . 5 1.3.2 I-band and elasticity of the sarcomere . 5 1.3.3 A-band and the thick filament . 6 1.3.4 M-line and anchoring function . 7 1.4 Modules in titin: Ig and FnIII domains . 7 1.5 Titin kinase . 9 1.6 Titin kinase signalling pathway . 11 1.7 Disease association of a titin kinase mutation . 12 1.8 Muscle-specific RING finger protein MURF . 13 1.9 NBR1 . 15 1.10 The protein p62 . 16 1.11 Aim of the work . 17 2 The A-band immunoglobulin domains A168 and A169 19 2.1 Introduction . 19 2.1.1 Immunoglobulin domains . 19 2.1.2 Interaction of titin A168-A169 and MURF . 20 2.2 Materials and Methods . 21 2.2.1 Purification of A168-A169 . 21 2.2.2 Preparation of Selenomethionine incorporated A168-A169 22 2.2.3 Purification of titin A168-A169-A170 . 22 2.2.4 Crystallisation of A168-A169-A170 and diffraction tests .
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Kinase Related Protein / Telokin Inhibits Ca2+-Independent Contraction in Triton Skinned Guinea Pig Taenia Coli
Kinase related protein / telokin inhibits Ca2+-independent contraction in triton skinned guinea pig taenia coli Olga Shcherbakova, Daria Serebryanaya, Alexander Postnikov, Mechthild M Schroeter, Stefan Zittrich, Angelika A Noegel, Vladimir Shirinsky, Alexander Vorotnikov, Gabriele Pfitzer To cite this version: Olga Shcherbakova, Daria Serebryanaya, Alexander Postnikov, Mechthild M Schroeter, Stefan Zittrich, et al.. Kinase related protein / telokin inhibits Ca2+-independent contraction in triton skinned guinea pig taenia coli. Biochemical Journal, Portland Press, 2010, 429 (2), pp.291-302. 10.1042/BJ20090819. hal-00495489 HAL Id: hal-00495489 https://hal.archives-ouvertes.fr/hal-00495489 Submitted on 28 Jun 2010 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Biochemical Journal Immediate Publication. Published on 11 May 2010 as manuscript BJ20090819 Kinase Related Protein / telokin inhibits Ca2+-independent contraction in triton skinned guinea pig taenia coli Olga Shcherbakova*1, Daria Serebryanaya*†1, Alexander Postnikov†1, Mechthild M. Schroeter‡, Stefan Zittrich‡, Angelika A. Noegel$, Vladimir Shirinsky*, Alexander Vorotnikov*,§, and Gabriele Pfitzer‡¶ * Laboratory of Cell Motility, Institute of Experimental Cardiology at the Russian Cardiology and Production Research Centre, 3rd Cherepkovskaya Str. 15a, Moscow 121552, Russia † Department of Bioorganic Chemistry, Biological Faculty, Moscow State University, Vorobjovy Hills, Moscow 119899, Russia ‡ Institute of Vegetative Physiology, University of Cologne, Robert-Koch-Str.
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82606505.Pdf
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Monday, February 27, 2012 359a airway smooth muscle cells, which is a more physiological system, to deter- 1821-Pos Board B591 mine the mechanism whereby one MLCK phosphorylates many SMM mole- Increased Intrinsic Stiffness of Aortic Vascular Smooth Muscle Cells cules. Direct observations of single QD-labeled MLCK molecules show as a Mechanism for Increased Aortic Stiffness in Spontaneously clearly that MLCK co-localizes with and can move along the actin- and Hypertensive Rats myosin-containing stress fibers, under the conditions of high ionic strength, Nancy Sehgel1, Shumin Gao1, Yi Zhu1,2, Zhe Sun2, or physiological ionic strength with CaM-Ca2þ and ATP. The diffusion Jerome P. Trzeciakowski3, William C. Hunter1,4, Dorothy E. Vatner1, coefficient, calculated from mean-squared-displacement (MSD) data from Gerald A. Meininger2, Stephen F. Vatner1, Hongyu Qiu1. MLCK-QDs’ trajectories, indicates that the mechanism by which one MLCK 1Department of Cell Biology and Molecular Medicine, UMDNJ-New Jersey, phosphorylates multiple SMMs may involve MLCK movement along thick Newark, NJ, USA, 2Dalton Cardiovascular Res Center and Department of and/or thin filaments on a time scale measured in seconds. Medical Pharmacology and Physiology, Univ of Missouri, Columbia, MO, USA, 3Department of Systems Biology and Translational Medicine, Texas 1819-Pos Board B589 A&M, College Station, TX, USA, 4Department of Biomedical Engineering, The Effects of Telokin on the Mechanics of Thiophosphorylated Smooth New Jersey Institute of Technology, Newark, NJ, USA. Muscle Myosin An increase in vascular stiffness is a fundamental component of hypertension.
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MLCK Antibody (N-Term) Purified Rabbit Polyclonal Antibody (Pab) Catalog # Ap7966a
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 MLCK Antibody (N-term) Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP7966a Specification MLCK Antibody (N-term) - Product Information Application WB,E Primary Accession Q15746 Other Accession P29294 Reactivity Human, Mouse Predicted Rabbit Host Rabbit Clonality Polyclonal Isotype Rabbit Ig Antigen Region 923-953 MLCK Antibody (N-term) - Additional Information Gene ID 4638 Other Names Myosin light chain kinase, smooth muscle, Western blot analysis of anti-MLCK-long Pab MLCK, smMLCK, Kinase-related protein, (Cat. #AP7966a) in mouse brain tissue KRP, Telokin, Myosin light chain kinase, lysate. MLCK-long (Arrow) was detected using smooth muscle, deglutamylated form, purified Pab. Secondary HRP-anti-rabbit was MYLK, MLCK, MLCK1, MYLK1 used for signal visualization with chemiluminescence. Target/Specificity This MLCK antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 923-953 amino acids from the N-terminal region of human MLCK. Dilution WB~~1:1000 Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. Storage Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C Western blot analysis of lysate from mouse in small aliquots to prevent freeze-thaw bladder tissue lysate, using MLCKlong cycles. Antibody (M1)(Cat. #AP7966a). AP7966a was diluted at 1:1000. A goat anti-rabbit IgG Precautions H&L(HRP) at 1:10000 dilution was used as Page 1/4 10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 MLCK Antibody (N-term) is for research use the secondary antibody.
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Functional Role of the C-Terminal Domain of Smooth Muscle Myosin Light Chain Kinase on the Phosphorylation of Smooth Muscle Myosin
J. Biochem. 129. 437-444 (2001) Functional Role of the C-Terminal Domain of Smooth Muscle Myosin Light Chain Kinase on the Phosphorylation of Smooth Muscle Myosin Takuya Numata,' Tsuyoshi Katoh,•õ and Michio Yazawa*,1 * Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810; and •õPresent address: Department of Biochemistry, Asahikawa Medical College, Asahikawa 078-8510 Received September 26, 2000; accepted December 20, 2000 Smooth muscle myosin light chain kinase (MLCK) is known to bind to thin filaments and myosin filaments. Telokin, an independently expressed protein with an identical amino acid sequence to that of the C-terminal domain of MLCK, has been shown to bind to unphosphorylated smooth muscle myosin. Thus, the functional significance of the C- terminal domain and the molecular morphology of MLCK were examined in detail. The C-terminal domain was removed from MLCK by ƒ¿-chymotryptic digestion, and the activ ity of the digested MLCK was measured using myosin or the isolated 20-kDa light chain (LC20) as a substrate. The results showed that the digestion increased Km for myosin 3- fold whereas it did not change the value for LC20. In addition, telokin inhibited the phosphorylation of myosin by MLCK by increasing Km but only slightly increased Km for LC20. Electron microscopy indicated that MLCK was an elongated molecule but was flexible so as to form folded conformations. MLCK was crosslinked to unphosphorylated heavy meromyosin with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide in the absence of Ca2+/calmodulin (CaM), and electron microscopic observation of the products revealed that the MLCK molecule bound to the head-tail junction of heavy meromyosin.
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Role of the Short Isoform of Myosin Light Chain Kinase in the Contraction of Cultured Smooth Muscle Cells As Examined by Its Down-Regulation
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Assembly of Smooth Muscle Myosin by the 38K Protein, a Homologue Of
Assembly of Smooth Muscle Myosin by the 38k Protein, a Homologue of a Subunit of Pre-mRNA Splicing Factor-2 Tsuyoshi Okagaki,* Akio Nakamura,* Tomohiko Suzuki,‡ Kazuhiro Ohmi,§ and Kazuhiro Kohama* *Department of Pharmacology, Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan; ‡Department of Biology, Kochi University, Kochi 780-8072, Japan; and §National Children’s Hospital, Setagaya-ku, Tokyo 154-0004, Japan Abstract. Smooth muscle myosin in the dephosphory- bound to myosin with both COOH-terminal 20 and lated state does not form filaments in vitro. However, NH2-terminal 28 residues of the 38k protein being es- thick filaments, which are composed of myosin and my- sential for myosin binding. The amino acid sequence of osin-binding protein(s), persist in smooth muscle cells, the 38k protein was not homologous to telokin, but to even if myosin is subjected to the phosphorylation– human p32, which was originally found in nuclei as a Downloaded from dephosphorylation cycle. The characterization of subunit of pre-mRNA splicing factor-2. Western blot- telokin as a myosin-assembling protein successfully ex- ting showed that the protein was expressed in various plained the discrepancy. However, smooth muscle cells smooth muscles. Immunofluorescence microscopy with that are devoid of telokin have been observed. We ex- cultured smooth muscle cells revealed colocalization of pected to find another ubiquitous protein with a similar the 38k protein with myosin and with other cytoskeletal role, and attempted to purify it from chicken gizzard. elements. The absence of nuclear immunostaining was The 38k protein bound to both phosphorylated and de- discussed in relation to smooth muscle differentiation.
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Telokin) Is Phosphorylated by Smooth-Muscle Myosin Light-Chain Kinase and Modulates the Kinase Activity Apolinary SOBIESZEK1, Oleg Y
Biochem. J. (1997) 328, 425–430 (Printed in Great Britain) 425 Kinase-related protein (telokin) is phosphorylated by smooth-muscle myosin light-chain kinase and modulates the kinase activity Apolinary SOBIESZEK1, Oleg Y. ANDRUCHOV and Krzysztof NIEZNANSKI Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, A-5020 Salzburg, Austria Telokin is an abundant smooth-muscle protein with an amino chem. J. 322, 65–71], indicates that the telokin dimer was acting acid sequence identical with that of the C-terminal region of as the substrate with a single protomer being phosphorylated. smooth-muscle myosin light-chain kinase (MLCK), although it Our enzyme kinetic analysis of the phosphorylation reaction is expressed as a separate protein [Gallagher and Herring (1991) conﬁrms this interpretation. Because telokin phosphorylation J. Biol. Chem. 266, 23945–23952]. Here we demonstrate that also required micromolar concentrations of MLCK, which also telokin is also similar to smooth-muscle myosin regulatory light facilitates the formation of kinase oligomers, we concluded that chain (ReLC) not only in its gross physical properties but also as the oligomers are interacting with telokin. Thus it seems that an MLCK substrate. Telokin was slowly phosphorylated by telokin modulates the phosphorylation rate of myosin ﬁlaments # MLCK in the presence of Ca + and calmodulin and could be by a mechanism that includes the direct or indirect inhibition of readily dephosphorylated by myosin light-chain phosphatase. A the kinase active site by the telokin dimer, and that removal threonine residue was phosphorylated with up to 0.25 mol}mol of the inhibition is controlled by slow phosphorylation of the stoichiometry.
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MOLECULAR AND FUNCTIONAL CHARACTERIZATION OF THE ROLE OF HYDROGEN SULPHIDE IN SEXUAL MEDICINE ROESWITA LEONO LIAW B.Sc. (Hons), National University of Singapore A THESIS SUBMITTED FOR THE DEGREE OF MASTER OF SCIENCE DEPARTMENT OF OBSTETRICS & GYNAECOLOGY NATIONAL UNIVERSITY OF SINGAPORE 2011 i ii ACKNOWLEDGEMENTS First and foremost, I would like to express my heartfelt gratitude to my project supervisor, Professor Ganesan P Adaikan for the great opportunity to work on this interesting project and also for his invaluable advice, patient guidance and encouragement throughout the course of this project. I would also like to thank Dr Balasubramanian Srilatha, my co-supervisor, for her helpful input and constructive suggestions which were instrumental to the development of the project. My sincere thanks also go out to Dr Jun Meng for the friendship, advice, support, bantering of ideas along the way as well as for sharing his expertise and setting aside time for consultation on troubleshooting problems with regards to real time PCR and western blot. I would also like to thank Miss Maryam Jameelah, past member of this lab who has done a good job in maintaining an orderly lab environment and also for providing assistance. I would like to extend my appreciation to both the academic and non-academic staff of the Department of Obstetrics & Gynaecology, NUS for the kind help they rendered along the way. I would also like to express my gratitude to the National University of Singapore for granting me the graduate research scholarship and hence allowing me to pursue my interest in research. The project was made possible under the NMRC grant (R-174-000-104-213) awarded to my supervisors.
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A New Member of the I Set Mark Pfuhl and Annalisa Pastore
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: a new member of the I set Mark Pfuhl and Annalisa Pastore EMBL, Heidelberg, Meyerhofstrasse 1, 691 17 Heidelberg, Federal Republic of Germany Background: Titin is a gigantic protein located in the two P-sheets packed against each other. Each sheet thick filament of vertebrate muscles. The putative contains four strands. The structure of M5 belonau to the functions of titin range from interactions with myosin I (intermediate) set of the immunoglobulin superfamily and other muscle proteins to a role in muscle recoil. and is very similar to telokin, which is also found in mus- Analysis of its complete sequence has shown that titin cles. Although M5 and telokin have relatively little is a multi-domain protein containing several copies of sequence similarity, the two proteins clearly share the modules of 100 amino acids each. These are thought same hydrophobic core. The major difference between to belong to the fibronectin type-111 and immuno- telokin and the titin M5 module is the absence of the C' globulin superfamilies. So far, a complete structural strand in the latter. determination has not been carried out on any of the Conclusions: The titin domains and several of the titin modules. immunoglobulin-like domains from other modular Results: The three-dimensional structure of an immuno- muscle proteins are highly conserved at the positions globulin module, located in the M-line of the sarcomere corresponding to the hydrophobic core of M5.
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Regulation of 130Kda Smooth Muscle Myosin Light Chain Kinase Expression by an Intronic Carg Element
JBC Papers in Press. Published on October 22, 2013 as Manuscript M113.510362 The latest version is at http://www.jbc.org/cgi/doi/10.1074/jbc.M113.510362 Regulation of 130kDa smooth muscle myosin light chain kinase expression by an intronic CArG element Meng Chen, Wenwu Zhang, Xiao Lu, April M. Hoggatt, Susan J. Gunst, Ghassan S. Kassab, Johnathan D. Tune and B. Paul Herring* Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Indianapolis, IN 46202 Short title: smMLCK regulates intestinal contractility and proliferation * To whom correspondence should be addressed: Paul Herring, Department of Cellular and Integrative Physiology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis IN, 46202 Phone: (317) 278-1785 FAX: (317) 274-3318 Email: [email protected] Background: Mechanisms regulating Deletion of the CArG region from the transcription of MLCK are poorly defined. endogenous mylk1 gene, specifically in smooth Results: Deleting a CArG element from the muscle cells, decreased expression of the mylk1 gene specifically decreased expression of 130kDa smMLCK by 40% without affecting the 130kDa smMLCK isoform, resulting in expression of the 220kDa MLCK or telokin. decreased intestinal contractility and This reduction in 130kDa smMLCK proliferation. expression resulted in decreased Conclusion: The 130kDa smMLCK isoform has phosphorylation of myosin light chains, functions that cannot be compensated for by the attenuated smooth muscle contractility and a 220kDa MLCK. 24% decrease in small intestine length that Significance: Floxed mylk1 mice permit specific was associated with a significant reduction of functions of the 130kDa smMLCK to be Ki67-positive smooth muscle cells. Overall, determined.
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MYLK (Human) Recombinant Protein
MYLK (Human) Recombinant Purity: 97% by SDS-PAGE/CBB staining Protein Activity: The activity was determined by IMAP™ assay. The enzyme was incubated with fluorescein labeled Catalog Number: P5641 peptide and Ca/Calmodulin. The phosphorylation was detected by IMAP™ technology (fluorescence Regulation Status: For research use only (RUO) polarization). Product Description: Human MYLK (NP_444253.2, Substrate: GS peptide. 1428 a.a. - 1771 a.a.) partial recombinant protein with ATP: 100 uM. GST tag at N-terminal expressed in baculovirus infected Storage Buffer: In 50 mM Tris-HCl, 150 mM NaCl, pH Sf21 cells. 7.5 (0.05% CHAPS, 1 mM DTT, 10% glycerol). Sequence: Storage Instruction: Store at -80°C. MAPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEG Aliquot to avoid repeated freezing and thawing. DKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIAD KHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDF Entrez GeneID: 4638 ETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPD FMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDK Gene Symbol: MYLK YLKSSKYIAWPLQGWQATFGGGDHPPKSDLEVLFQG PLGAMGSPEEPKDEVEVSDDDEKEPEVDYRTVTINTE Gene Alias: DKFZp686I10125, FLJ12216, KRP, MLCK, QKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKF MLCK1, MLCK108, MLCK210, MSTP083, MYLK1, FKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKA smMLCK NIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEG VEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRL Gene Summary: This gene, a muscle member of the ENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVIC immunoglobulin gene superfamily, encodes myosin light YILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEIS chain kinase which is a calcium/calmodulin dependent DDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKN
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