A rice tubulin tyrosine ligase-like 12 protein affects the dynamic and orientation of microtubules
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A rice tubulin tyrosine ligase-like 12 protein affects the dynamic and orientation of microtubules
The deryosination / retyrosing cycle is the most common post-translational modification of α-tubulin. Interestingly, for plants, the only qualified candidates of potential counterparts TTL are the 12 tubulin proteins Tyrosine ligase, such as 12 proteins. To better understand the biological functions of these potential TTL counterparts, we cloned the rice TTL protein (OSTTLL12) and overexpression of the OSTTLL12-RFP lines generated in rice and tobacco cells on 2.
We have seen unexpectedly that The overexpression of this Osttlel12-RFP has increased the relative abundance of α-tubulin eturbid in the coleoptile and seminal root, correlated with more stable microtubules. This was independent of the respective orientation of the cortical microtubule and followed by a corresponding growth of coleoptases and seminal roots. A disturbed organization of phragmasplast microtubules and disoriented cell walls constituted other characteristics of this phenotype. Thus, the high tubulin decyrosinization as a result of OSTTLL12 overexpression affects the structural and dynamic characteristics of microtubules, followed by changes in the axiality of cellular plate deposition and, therefore, plant growth. This article is protected by copyright. All rights reserved.
Evaluation of procalcitonin and reactive protein C in the differential early diagnosis of neonatal jaundice
Background: The objective of this study was to study the clinical value of the Procalcionine (PCT) and the C-Reactive Protein (CRP) in the differential diagnosis of neonatal jaundice.
Methods: Eighty-five cases of neonatal jaundice in our hospital from January 2016 to March 2019 have been selected as research topics, including 30 cases of physiological jaundice, 23 cases of infectious jaundice and 32 cases of molement jaundice. Five milliliters of non-anticoagulated venous peripheral blood and 3 ml of anticoagulated EDTA-K + peripheral blood were sampled from each newborn when the symptoms of jaundice took place. Non-anticoagulated blood samples were then centrifuged at 3,500 rpm for 7 minutes and serum was used for PCT and bilirubin exams, and anticoagulated blood samples were prepared for the CRP exam. The analysis of the receiver operating characteristics curve (ROC) was performed for the evaluation of the differential diagnosis of neonatal jaundice by PCT, CRP and the levels of bilirubin.
Results: Variance analyzes have shown that the postnatal age of jaundice occurring in the physiological group of jaundice was older than those of infectious jaundice and hemolytic jaundice (p <0.001), as well as PCT levels and CRP in the infectious jaundice group were higher than those in hemolytic jaundice and physiological jaundice groups (p <0.001). Pearson correlation analysis indicated that PCT and CRP levels were negatively correlated with postnatal age in the physiological jaundice group (p <0.05). The analysis of the ROC curve has demonstrated that the PCT and the CRP had the effectiveness of the strictest differential diagnosis of the neonatal pathological and neonatal physiological jaundice with PCT and CRP at 0.70 μg / L and 8.50 mg / L, as well as the effectiveness of the most differential diagnosis of neonatal infectious jaundice and neonatal hemolytic jaundice with PCT and CRP at 1.84 μg / L and 13.50 mg / L, respectively.
Conclusions: This study suggested that PCT and CRP had significant clinical values ​​in the differential diagnosis of neonatal jaundice and the PCT was greater than the differential diagnosis of neonatal infectious jaundice.
A rice tubulin tyrosine ligase-like 12 protein affects the dynamic and orientation of microtubules
Proteomic analysis reveals that Gene DiC1 autistic associated regulates the proteins associated with an organization and mitochondrial function
Dix-Domain containing 1 (DOMDC1) is an important neural development regulator, including cortical neural, neuronal migration and synaptic connectivity, and sequence variants in the gene have been linked to autism spectrum disorders (ASDS. ) Previous studies indicate that Didc1 controls neurorogenesis by WNT signaling, while its regulation of dendrite and synapse development requires signaling WNT and cytoskeleton. However, the prediction of these signaling pathways is mainly based on the structure of diddc1. Given the role of DOMDC1 in the development of neural and brain disorders, we hypothesized that Didsc1 can set additional signaling pathways in the brain. We conducted transcriptomic and proteomic analyzes of Cortis DiC1 KO Mouse to reveal such modifications. We found that transcriptomic approaches do not provide any new conclusion on Didc1’s downstream impacts.
In comparison, our proteomic approach reveals that several important mitochondrial proteins are significantly regulated in the absence of DIDC1, suggesting a new function of Didc1. AMIBEBIC (AK) keratitis is an infection in the sight, characterized by serious inflammation of the cornea, caused by the free protozoan of the genus Acanthamoeba. The identification of amoeba proteins involved in the AK pathogenesis can help elucidate molecular infection mechanisms and help indicate diagnostic and therapeutic targets.
Microtubule Associated Protein Tau / Tau Protein (MAPT) Antibody
Description: The microtubial-associated protein TAU (MAPT), more commonly known as TAU, is is normally a highly soluble protein found predominantly in neurons (1), but accumulations of highly phosphorylated tau protein aggregates are observed in several neurodegenerative diseases including Alzheimer’s disease, progressive supranuclear palsy, corticobasal degeneration, and frontotemporal lobar dementia. It was thought that these pathological tau aggregates were the toxic form of tau, but recent studies indicate that soluble and highly phosphorylated tau species are more closely associated with synaptic dysfunction and cell loss (2,3). Mutations in the TAU gene have also been associated with several of these neurodegenerative diseases (4).
Description: The microtubial-associated protein TAU (MAPT), more commonly known as TAU, is is normally a highly soluble protein found predominantly in neurons (1), but accumulations of highly phosphorylated tau protein aggregates are observed in several neurodegenerative diseases including Alzheimer’s disease, progressive supranuclear palsy, corticobasal degeneration, and frontotemporal lobar dementia. It was thought that these pathological tau aggregates were the toxic form of tau, but recent studies indicate that soluble and highly phosphorylated tau species are more closely associated with synaptic dysfunction and cell loss (2,3). Mutations in the TAU gene have also been associated with several of these neurodegenerative diseases (4).
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T231
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T231
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T231
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, IHC-P, IF, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T212
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, IHC-P, IF, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T212
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, IHC-P, IF, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T212
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of S214
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of S214
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of S214
Description: A polyclonal antibody for detection of Tau from Human. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T181
Description: A polyclonal antibody for detection of Tau from Human. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T181
Description: A polyclonal antibody for detection of Tau from Human. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of T181
Description: A polyclonal antibody for detection of Tau from Human, Mouse, Rat, Monkey. This Tau antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human Tau around the non-phosphorylation site of S235
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In this study, we evaluated the changes in the expression profile of proteins acanthamoeba triggered by the invasive process, using an approach involving two-dimensional polyacrylamide gel electrophoresis, followed by An identification of mass spectrometry (ESI-IT-TOF LC-MSN). AK has been induced by intrastromal inoculation in Wistar rats, using trophozoites from a T4 genotype, a strain of a. Castellanii derived in a prolonged axenic culture.
