Choline Kinase Alpha Antibody Cat

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Choline kinase alpha Antibody Cat. No.: 63-448 Choline kinase alpha Antibody Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human This Choline kinase alpha (CHK) antibody is generated from rabbits immunized with a KLH IMMUNOGEN: conjugated synthetic peptide between 427-457 amino acids from the C-terminal region of human Choline kinase alpha (CHK). TESTED APPLICATIONS: WB APPLICATIONS: For WB starting dilution is: 1:1000 PREDICTED MOLECULAR 52 kDa WEIGHT: Properties This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by PURIFICATION: dialysis CLONALITY: Polyclonal ISOTYPE: Rabbit Ig CONJUGATE: Unconjugated September 27, 2021 1 https://www.prosci-inc.com/choline-kinase-alpha-antibody-63-448.html PHYSICAL STATE: Liquid BUFFER: Supplied in PBS with 0.09% (W/V) sodium azide. CONCENTRATION: batch dependent Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies STORAGE CONDITIONS: care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Additional Info OFFICIAL SYMBOL: CHKA ALTERNATE NAMES: Choline kinase alpha, CK, CHETK-alpha, Ethanolamine kinase, EK, CHKA, CHK, CKI ACCESSION NO.: P35790 PROTEIN GI NO.: 226694197 GENE ID: 1119 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References The major pathway for the biosynthesis of phosphatidylcholine occurs via the CDP-choline pathway. Choline kinase alpha is the initial enzyme in the sequence and may play a BACKGROUND: regulatory role. This protein also catalyzes the phosphorylation of ethanolamine. The antibody for this protein recognizes both isoforms. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 27, 2021 2 https://www.prosci-inc.com/choline-kinase-alpha-antibody-63-448.html.

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Identification and Validation of Novel and More Effective Choline Kinase
www.nature.com/scientificreports OPEN Identifcation and validation of novel and more efective choline kinase inhibitors against Streptococcus pneumoniae Tahl Zimmerman1*, Valerie Chasten1, Juan Carlos Lacal2 & Salam A. Ibrahim1 Streptococcus pneumoniae choline kinase (sChoK) has previously been proposed as a drug target, yet the efectiveness of the frst and only known inhibitor of sChoK, HC-3, is in the millimolar range. The aim of this study was thus to further validate sChoK as a potential therapeutic target by discovering more powerful sChoK inhibitors. LDH/PK and colorimetric enzymatic assays revealed two promising sChoK inhibitor leads RSM-932A and MN58b that were discovered with IC50 of 0.5 and 150 μM, respectively, and were shown to be 2–4 magnitudes more potent than the previously discovered inhibitor HC-3. Culture assays showed that the minimum inhibitory concentration (MIC) of RSM- 932A and MN58b for S. pneumoniae was 0.4 μM and 10 μM, respectively, and the minimum lethal concentration (MLC) was 1.6 μM and 20 μM, respectively. Western blot monitoring of teichoic acid production revealed diferential patterns in response to each inhibitor. In addition, both inhibitors possessed a bacteriostatic mechanism of action, and neither interfered with the autolytic efects of vancomycin. Cells treated with MN58b but not RSM-932A were more sensitive to a phosphate induced autolysis with respect to the untreated cells. SEM studies revealed that MN58b distorted the cell wall, a result consistent with the apparent teichoic acid changes. Two novel and more highly potent putative inhibitors of sChoK, MN58b and RSM-932A, were characterized in this study.
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Table S1. List of Oligonucleotide Primers Used
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DATASHEET USA: [email protected]
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MOLECULAR MEDICINE REPORTS 11: 611-618, 2015 Expression profiling of choline and ethanolamine kinases in MCF7, HCT116 and HepG2 cells, and the transcriptional regulation by epigenetic modification CHUA SIANG LING1, KHOO BOON YIN2, SEE TOO WEI CUN1 and FEW LING LING1 1School of Health Sciences, Universiti Sains Malaysia, Kubang Kerian, Kelantan 16150; 2Institute for Research in Molecular Medicine, Universiti Sains Malaysia, Penang 11800, Malaysia Received December 10, 2013; Accepted September 4, 2014 DOI: 10.3892/mmr.2014.2707 Abstract. The function of choline kinase (CK) and etha- cell lines were varied. The effects of TSA treatment on the nolamine kinase (EK) is to catalyse the phosphorylation mRNA expression levels of ck and ek imply that ck and ek of choline and ethanolamine, respectively, in order to yield mRNA expression may be regulated by epigenetic modifica- phosphocholine (PCho) and phosphoethanolamine (PEtn). A tion. high expression level of PCho, due to elevated CK activity, has previously been associated with malignant transformation. In Introduction the present study, a quantitative polymerase chain reaction was performed to determine the mRNA expression profiles of ck Choline kinase (CK) and ethanolamine kinase (EK) are enzymes and ek mRNA variants in MCF7 breast, HCT116 colon and that initiate the first step in the Kennedy pathway, resulting in HepG2 liver cancer cells. The ck and ek mRNA expression the biosynthesis of phosphatidylcholine and phosphatidyletha- profiles showed that total ckα was expressed most abundantly nolamine (1). In the presence of Mg2+, CK and EK catalyse the in the HepG2 cells. The HCT116 cells exhibited the highest ATP-dependent phosphorylation of choline and ethanolamine ckβ and ek1 mRNA expression levels, whereas the highest into phosphocholine (PCho) and phoshoethanolamine (PEtn), ek2α mRNA expression levels were detected in the MCF7 respectively.
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