Only in Titles

Search results for: Lambda Protein Phosphatase Lambda Protein Phosphatase

paperclip

#33480088   2021/01/22 To Up

Establishment of age- and sex-specific reference intervals for serum liver function tests in pediatric population aged 1-<18 years: A prospective study.

The diagnosis, treatment, and prognosis of pediatric diseases rely on the accurate establishment of the reference interval (RI). This study aimed to establish pediatric RIs for liver function tests and evaluated the correlation of the analytes.
Xuetong Zhu, Kaijin Wang, Qi Zhou, Jiancheng Xu

2909 related Products with: Establishment of age- and sex-specific reference intervals for serum liver function tests in pediatric population aged 1-<18 years: A prospective study.

900 tests100 TESTS50ug96 tests4 Membranes/Box1 LITRE2 Pieces/Box4 Membranes/Box0.1 mg

Related Pathways

    No related Items
paperclip

#33166334   2020/11/09 To Up

Prediction of PIK3CA mutations from cancer gene expression data.

Breast cancers with PIK3CA mutations can be treated with PIK3CA inhibitors in hormone receptor-positive HER2 negative subtypes. We applied a supervised elastic net penalized logistic regression model to predict PIK3CA mutations from gene expression data. This regression approach was applied to predict modeling using the TCGA pan-cancer dataset. Approximately 10,000 cases were available for PIK3CA mutation and mRNA expression data. In 10-fold cross-validation, the model with λ = 0.01 and α = 1.0 (ridge regression) showed the best performance, in terms of area under the receiver operating characteristic (AUROC). The final model was developed with selected hyper-parameters using the entire training set. The training set AUROC was 0.93, and the test set AUROC was 0.84. The area under the precision-recall (AUPR) of the training set was 0.66, and the test set AUPR was 0.39. Cancer types were the most important predictors. Both insulin like growth factor 1 receptor (IGF1R) and the phosphatase and tensin homolog (PTEN) were the most significant genes in gene expression predictors. Our study suggests that predicting genomic alterations using gene expression data is possible, with good outcomes.
Jun Kang, Ahwon Lee, Youn Soo Lee

1130 related Products with: Prediction of PIK3CA mutations from cancer gene expression data.



Related Pathways

paperclip

#33135063   2020/11/02 To Up

Titin-Truncating Mutations Associated With Dilated Cardiomyopathy Alter Length-Dependent Activation And Its Modulation Via Phosphorylation.

Dilated cardiomyopathy (DCM) is associated with mutations in many genes encoding sarcomere proteins. Truncating mutations in the titin gene TTN are the most frequent. Proteomic and functional characterisations are required to elucidate the origin of the disease and the pathogenic mechanisms of TTN-truncating variants.
Petr G Vikhorev, Natalia N Vikhoreva, WaiChun Yeung, Amy Li, Sean Lal, Cristobal G Dos Remedios, Cheavar A Blair, Maya Guglin, Kenneth S Campbell, Magdi H Yacoub, Pieter de Tombe, Steven B Marston

1778 related Products with: Titin-Truncating Mutations Associated With Dilated Cardiomyopathy Alter Length-Dependent Activation And Its Modulation Via Phosphorylation.

100ug/vial100ug Lyophilized1 Set100ug2 Pieces/Box1 Set1 Set25 x 2 ml250ul1 Set1 Set1,000 tests

Related Pathways

paperclip

#32962211   2020/09/20 To Up

Tip60 Phosphorylation at Ser 99 Is Essential for Autophagy Induction in .

Tip60, a key histone acetyltransferase of the MYST family and member of the nuclear multimeric protein complex (NuA4), regulates the activity and stability of proteins involved in the cell cycle, DNA damage responses, autophagy, etc. However, the function and regulatory mechanism of Tip60 homolog in are not elucidated. In the present study, Tip60 (BmTip60) was functionally identified. Developmental profiles showed that the protein levels and nuclear localization of BmTip60 peaked in fat body during the larval-pupal metamorphosis when autophagy was intensive; simultaneously, the BmTip60 protein migrated to form an upper band as detected by Western blot. Interestingly, the upper band of BmTip60 was reduced by λ-phosphatase treatment, indicating that it was a phosphorylated form of BmTip60. Results showed that BmTip60 was promoted by starvation but not 20-hydroxyecdysone treatment. Transcription factor AMP-activated protein kinase (AMPK) affected by starvation was pivotal for BmTip60 protein migration. In addition, one mammalian phosphorylation site was identified in BmTip60 at Ser99, the constitutive-activation mutation of Ser99 to Asp99 but not its inactive mutation to Ala99 significantly upregulated autophagy, showing the critical role of phosphorylation at Ser99 for BmTip60-mediated autophagy. In conclusion, the starvation-AMPK axis promotes BmTip60 in , which was requisite for autophagy induction. These results reveal a regulatory mechanism of histone acetyltransferase Tip60 homologs by phosphorylation in insects, and sheds light on further related studies of acetylation regulation.
Wenmei Wu, Kang Li, Haigang Zhao, Xianying Xu, Jing Xu, Man Luo, Yang Xiao, Ling Tian

1904 related Products with: Tip60 Phosphorylation at Ser 99 Is Essential for Autophagy Induction in .

0.1ml0.1ml (1mg/ml)0.1ml50ul (1mg/ml)0.1ml0.1ml50 samples100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized

Related Pathways

paperclip

#32946790   2020/09/15 To Up

Yes-associated protein 1 translocation through actin cytoskeleton organization in trophectoderm cells.

A mammalian embryo experiences the first cell segregation at the blastocyst stage, in which cells giving form to the embryo are sorted into two lineages; trophectoderm (TE) and inner cell mass (ICM). This first cell segregation process is governed by cell position-dependent Hippo signaling, which is a phosphorylation cascade determining whether Yes-associated protein 1 (YAP1), one of the key components of the Hippo signaling pathway, localizes within the nucleus or cytoplasm. YAP1 localization determines the transcriptional on/off switch of a key gene, Cdx2, required for TE differentiation. However, the control mechanisms involved in YAP1 nucleocytoplasmic shuttling post blastocyst formation remain unknown. This study focused on the mechanisms involved in YAP1 release from TE nuclei after blastocoel contraction in bovine blastocysts. The blastocysts contracted by blastocoel fluid aspiration showed that the YAP1 translocation from nucleus to cytoplasm in the TE cells was concomitant with the protruded actin cytoskeleton. This YAP1 release from TE nuclei in the contracted blastocysts was prevented by actin disruption and stabilization. In contrast, Y27632, which is a potent inhibitor of Rho-associated coiled-coil containing protein kinase 1/2 (ROCK) activity, was found to promote YAP1 nuclear localization in the TE cells of contracted blastocysts. Meanwhile, lambda protein phosphatase (LPP) treatment inducing protein dephosphorylation could not prevent YAP1 release from TE nuclei in the contracted blastocysts, indicating that YAP1 release from TE nuclei does not depend on the Hippo signaling pathway. These results suggested that blastocyst contraction causes YAP1 release from TE nuclei through actin cytoskeleton remodeling in a Hippo signaling-independent manner. Thus, the present study raised the possibility that YAP1 subcellular localization is controlled by actin cytoskeletal organization after the blastocyst formation. Our results demonstrate diverse regulatory mechanisms for YAP1 nucleocytoplasmic shuttling in TE cells.
Shota Yamamura, Nanami Goda, Hiroki Akizawa, Nanami Kohri, Ahmed Z Balboula, Ken Kobayashi, Hanako Bai, Masashi Takahashi, Manabu Kawahara

1097 related Products with: Yes-associated protein 1 translocation through actin cytoskeleton organization in trophectoderm cells.

100ul100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized1x10e7 cells100ug Lyophilized100μg100ug Lyophilized100ug Lyophilized100ug Lyophilized

Related Pathways

paperclip

#32866611   2020/08/29 To Up

Expression, purification and crystallization of CLK1 kinase - A potential target for antiviral therapy.

Cdc-like kinase 1 (CLK1) is a dual-specificity kinase capable of autophosphorylation on tyrosine residues and Ser/Thr phosphorylation of its substrates. CLK1 belongs to the CLK kinase family that regulates alternative splicing through phosphorylation of serine-arginine rich (SR) proteins. Recent studies have demonstrated that CLK1 has an important role in the replication of influenza A and chikungunya viruses. Furthermore, CLK1 was found to be relevant for the replication of HIV-1 and the West Nile virus, making CLK1 an interesting cellular candidate for the development of a host-directed antiviral therapy that might be efficient for treatment of newly emerging viruses. We describe here our attempts and detailed procedures to obtain the recombinant kinase domain of CLK1 in suitable amounts for crystallization in complex with specific inhibitors. The key solution for the reproducibility of crystals resides in devising and refining expression and purification protocols leading to homogeneous protein. Co-expression of CLK1 with λ-phosphatase and careful purification has yielded crystals of CLK1 complexed with the KH-CB19 inhibitor that diffracted to 1.65 Å. These results paved the path to the screening of more structures of CLK1 complexed compounds, leading to further optimization of their inhibitory activity. Moreover, since kinases are desired targets in numerous pathologies, the approach we report here, the co-expression of kinases with λ-phosphatase, previously used in other kinases, can be adopted as a general protocol in numerous kinase targets for obtaining reproducible and homogenic non-phosphorylated (inactive) forms suitable for biochemical and structural studies thus facilitating the development of novel inhibitors.
Noa Dekel, Yael Eisenberg-Domovich, Alexander Karlas, Thomas F Meyer, Franz Bracher, Mario Lebendiker, Tsafi Danieli, Oded Livnah

1679 related Products with: Expression, purification and crystallization of CLK1 kinase - A potential target for antiviral therapy.

100 ml100 TESTS0.2 mg0.2 mg0.1 mg0.1ml (1mg/ml)1 ml25 µg0.1 ml250 ml0.25 mg1 LITRE

Related Pathways

paperclip

#32802966   2020/07/07 To Up

Phosphoregulation of tropomyosin-actin interaction revealed using a genetic code expansion strategy.

Tropomyosins are coiled-coil proteins that regulate the stability and / or function of actin cytoskeleton in muscle and non-muscle cells through direct binding of actin filaments. Recently, using the fission yeast, we discovered a new mechanism by which phosphorylation of serine 125 of tropomyosin (Cdc8), reduced its affinity for actin filaments thereby providing access for the actin severing protein Adf1/Cofilin to actin filaments causing instability of actin filaments. Here we use a genetic code expansion strategy to directly examine this conclusion. We produced in Cdc8-tropomyosin bearing a phosphate group on Serine-125 (Cdc8 ), using an orthogonal tRNA-tRNA synthetase pair that directly incorporates phosphoserine into proteins in response to a UAG codon in the corresponding mRNA. We show using total internal reflection (TIRF) microscopy that, whereas produced Cdc8 does not bind actin filaments, Cdc8 incubated with lambda phosphatase binds actin filaments. This work directly demonstrates that a phosphate moiety present on serine 125 leads to decreased affinity of Cdc8-tropomyosin for actin filaments. We also extend the work to demonstrate the usefulness of the genetic code expansion approach in imaging actin cytoskeletal components.
Saravanan Palani, Darius Koester, Mohan K Balasubramanian

1688 related Products with: Phosphoregulation of tropomyosin-actin interaction revealed using a genetic code expansion strategy.

1 Set1 Set1 Set1 Set100 1 Set1 Set1 Set1 Set10.00 nmol 6 ml Ready-to-use

Related Pathways

paperclip

#32747587   2020/08/03 To Up

Dephosphorylation of DNA Fragments with Alkaline Phosphatase.

The removal of 5' phosphates from nucleic acids is used to enhance subsequent labeling with [γ-P]-ATP, reduce the circularization of plasmid vectors in ligation reactions, and render DNA susceptible or resistant to other enzymes that act on nucleic acids (e.g., λ exonuclease). Essentially, any nucleotide phosphatase (e.g., bacterial alkaline phosphatase, calf intestinal alkaline phosphatase [CIP], placental alkaline phosphatase, shrimp alkaline phosphatase [SAP], or several acid phosphatases such as sweet potato and prostate acid phosphatase) will catalyze the removal of 5' phosphates from nucleic acid templates. In fact, these enzymes prefer small substrates such as -nitrophenyl phosphate (PNPP) and the exposed 5' phosphates of nucleic acids to bulky globular protein substrates.
Michael R Green, Joseph Sambrook

1238 related Products with: Dephosphorylation of DNA Fragments with Alkaline Phosphatase.

1 mg100ug1 ml96T/Kit100ug 15 ml 1 mg100ug1 mg400/kit100ug 125 ml

Related Pathways

paperclip

#32702241   2020/08/10 To Up

Design of Tunable Protein Interfaces Controlled by Post-Translational Modifications.

The design of protein interaction interfaces is a cornerstone of synthetic biology, where they can be used to promote the association of protein subunits into active molecular complexes or into protein nanostructures. In nature, protein interactions can be modulated by post-translational modifications (PTMs) that modify the protein interfaces with the addition and removal of various chemical groups. PTMs thus represent a means to gain control over protein interactions, yet they have seldom been considered in the design of synthetic proteins. Here, we explore the potential of a reversible PTM, serine phosphorylation, to modulate the interactions between peptides. We designed a series of interacting peptide pairs, including heterodimeric coiled coils, that contained one or more protein kinase A (PKA) recognition motifs. Our set of peptide pairs comprised interactions ranging from nanomolar to micromolar affinities. Mass spectrometry analyses showed that all peptides were excellent phosphorylation substrates of PKA, and subsequent phosphate removal could be catalyzed by lambda protein phosphatase. Binding kinetics measurements performed before and after treatment of the peptides with PKA revealed that phosphorylation of the target serines affected both the association and dissociation rates of the interacting peptides. We observed both the strengthening of interactions (up to an 11-fold decrease in ) and the weakening of interactions (up to a 180-fold increase in ). -designed PTM-modulated interfaces will be useful to control the association of proteins in biological systems using protein-modifying enzymes, expanding the paradigm of self-assembly to encompass controlled assembly of engineerable protein complexes.
Daniel L Winter, Hasti Iranmanesh, Douglas S Clark, Dominic J Glover

1995 related Products with: Design of Tunable Protein Interfaces Controlled by Post-Translational Modifications.

1000.2 mg5001 Set100024 reactions 10001 Set101 mg5001 Set

Related Pathways

paperclip

#32363836   // To Up

Naringenin Attenuates Toxicity and Oxidative Stress Induced by Lambda-cyhalothrin in Liver of Male Rats.

Extensive use of Lambda-cyhalothrin (LTC), a synthetic pyrethroid insecticide, has been associated with serious health problems to the non-target organisms including mammals. The present study investigated the protective effect of naringenin (NGN), an antioxidant flavonoid, against the toxicity induced LTC in the liver of male rats.
Ahmed Mokhtar Abu El-Saad, Wessam Mohamad Abdel-Wahab

1878 related Products with: Naringenin Attenuates Toxicity and Oxidative Stress Induced by Lambda-cyhalothrin in Liver of Male Rats.

1 mg96T50 ul900 tests

Related Pathways