Search results for: Recombinant E. coli CA2 Proteins
#28394913 2017/04/10 Save this To Up
Cohnella amylopullulanases: Biochemical characterization of two recombinant thermophilic enzymes.Some industries require newer, more efficient recombinant enzymes to accelerate their ongoing biochemical reactions in harsh environments with less replenishment. Thus, the search for native enzymes from extremophiles that are suitable for use under industrial conditions is a permanent challenge for R & D departments. Here and toward such discoveries, two sequences homologous to amylopullulanases (EC 184.108.40.206, GH57) from an endogenous Cohnella sp., [Coh00831 (KP335161; 1998 bp) and Coh01133 (KP335160: 3678 bp)] were identified. The genes were heterologously expressed in E. coli to both determine their type and further characterize their properties. The isolated DNA was PCR amplified with gene specific primers and cloned in pET28a, and the recombinant proteins were expressed in E. coli BL21 (DE3). The temperatures and pH optima of purified recombinants Coh 01133 and Coh 00831 enzymes were 70°C and 8, and 60°C and 6, respectively. These enzymes are stable more than 90% in 60°C and 50°C for 90 min respectively. The major reactions released sugars which could be fractionated by HPLC analysis, from soluble starch were mainly maltose (G2), maltotriose (G3) and maltotetraose (G4). The enzymes hydrolyzed pullulan to maltotriose (G3) only. Enzyme activities for both proteins were improved in the availability of Mn2+, Ba2+, Ca2+, and Mg2+ and reduced in the presence of Fe2+, Li2+, Na2+, Triton X100 and urea. Moreover, Co2+, K+, and Cu2+ had a negative effect only on Coh 01133 enzyme.
1494 related Products with: Cohnella amylopullulanases: Biochemical characterization of two recombinant thermophilic enzymes.Human enzymes and protein Twort's Counterstain Kit Ras (dn N17) Recombinant HIV 1 tat recombinant ant HIV 1 gag p24 recombinant HIV 1 nef recombinant ant HIV 1 env gp41 recombinan HIV 2 env gp36 recombinan HCV core recombinant anti HCV core recombinant anti HCV core recombinant anti HCV core recombinant anti
#27997125 2016/12/20 Save this To Up
Secretagogin Is a Redox-Responsive Ca(2+) Sensor.Secretagogin (SCGN), a multifunctional, Ca(2+) binding, regulatory protein, known to regulate insulin release, has recently been implicated in the control of stress-related corticotropin-releasing hormone (CRH) secretion. Localization of SCGN to multiple intracellular (such as cytosol, nucleus, and endoplasmic reticulum) and extracellular sites appears to provide multifunctional capabilities; however, the structural elements conferring such a widespread cellular distribution to SCGN remain unidentified. We report that the spatial and functional attributes of SCGN plausibly originate from the interplay between Ca(2+) and its redox state. The mutation of selective Cys residues provides further insights into the origin and mode of redox responsiveness. In the reducing milieu, SCGN exhibits a higher affinity for Ca(2+), and more stability than in the oxidizing environment, suggesting it is a redox-responsive Ca(2+) sensor protein, which is further supported by its response to dithiothreitol (reducing stress) in MIN6 cells. Our data provide a biophysical and biochemical explanation for the diverse localization of SCGN in the cellular scenario and beyond the cell.
CA 19-9 antibody, Monoclo CA 19-9 antibody, Monoclo CA 50 antibody, Monoclona CA 15-3 antibody, Monoclo CA 15-3 antibody, Monoclo CA 19-9 antibody, Monoclo CA 19-9 antibody, Monoclo Rabbit Anti-Calretinin CA B-Phycoerythrin antibody 2-Amino Benzimidazole Su 2-Amino Benzimidazole Su EZH2 KMT6 antibody Isoty
#27907125 2016/12/01 Save this To Up
Identification of a Highly Conserved Hypothetical Protein TON_0340 as a Probable Manganese-Dependent Phosphatase.A hypothetical protein TON_0340 of a Thermococcus species is a protein conserved in a variety of organisms including human. Herein, we present four different crystal structures of TON_0340, leading to the identification of an active-site cavity harboring a metal-binding site composed of six invariant aspartate and glutamate residues that coordinate one to three metal ions. Biochemical and mutational analyses involving many phosphorous compounds show that TON_0340 is a Mn2+-dependent phosphatase. Mg2+ binds to TON_0340 less tightly and activates the phosphatase activity less efficiently than Mn2+. Whereas Ca2+ and Zn2+ are able to bind to the protein, they are unable to activate its enzymatic activity. Since the active-site cavity is small and largely composed of nearly invariant stretches of 11 or 13 amino acids, the physiological substrates of TON_0340 and its homologues are likely to be a small and the same molecule. The Mn2+-bound TON_0340 structure provides a canonical model for the ubiquitously present TON_0340 homologues and lays a strong foundation for the elucidation of their substrate and biological function.
2654 related Products with: Identification of a Highly Conserved Hypothetical Protein TON_0340 as a Probable Manganese-Dependent Phosphatase.Amplite™ Colorimetric A Amplite™ Fluorimetric A Amplite™ Fluorimetric A Amplite™ Fluorimetric A Amplite™ Luminometric A Recombinant Human ASF1A P Recombinant Human ASF1A P Recombinant Human ASF1A P hypothetical protein LOC2 hypothetical protein LOC5 hypothetical protein LOC1 hypothetical protein LOC2
#27813252 2016/11/04 Save this To Up
The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein.Apoptosis-linked gene 2 (ALG-2), which is a gene product of PDCD6, is a 22-kDa Ca(2+) -binding protein. Accumulating evidence points to a role for ALG-2 as a Ca(2+) -responsive adaptor protein. On binding to Ca(2+) , ALG-2 undergoes a conformational change that facilitates its interaction with various proteins. It also forms a homodimer and heterodimer with peflin, a paralog of ALG-2. However, the differences in cellular roles for the ALG-2 homodimer and ALG-2/peflin heterodimer are unclear. In the present study, we found that Trk-fused gene (TFG) protein interacted with the ALG-2 homodimer. Immunostaining analysis revealed that TFG and ALG-2 partially overlapped at endoplasmic reticulum exit sites (ERES), a platform for COPII-mediated protein transport from the endoplasmic reticulum. Time-lapse live-cell imaging demonstrated that both green fluorescent protein-fused TFG and mCherry-fused ALG-2 are recruited to ERES after thapsigargin treatment, which raises intracellular Ca(2+) levels. Furthermore, overexpression of ALG-2 induced the accumulation of TFG at ERES. TFG has an ALG-2-binding motif and deletion of the motif decreased TFG binding to ALG-2 and shortened its half-life at ERES, suggesting a critical role for ALG-2 in retaining TFG at ERES. We also demonstrated, by in vitro cross-linking assays, that ALG-2 promoted the polymerization of TFG in a Ca(2+) -dependent manner. Collectively, the results suggest that ALG-2 acts as a Ca(2+) -sensitive adaptor to concentrate and polymerize TFG at ERES, supporting a potential role for ALG-2 in COPII-dependent trafficking from the endoplasmic reticulum.
1228 related Products with: The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein.Anti PDX1 Polyclonal Anti MIC2 Gene Protein, CD99; Acyl CoA binding Protein T4 SSB (gene 32) protein T4 SSB (gene 32) protein T4 SSB (gene 32) protein T4 SSB (gene 32) protein E. coli SSB (Single Stran E. coli SSB (Single Stran E. coli SSB (Single Stran E. coli SSB (Single Stran Mouse Anti-Human Retinol
#27568390 2016/08/28 Save this To Up
Production of Ca(2+)-Independent and Acidstable Recombinant α-Amylase of Bacillus acidicola Extracellularly and its Applicability in Generating Maltooligosaccharides.The recombinant acidstable α-amylase (Ba-amy) of acidophilic bacterium Bacillus acidicola TSAS1 has been produced extracellularly using a combination of cloning (E. coli and P. pastoris) and physico-chemical treatment strategies. A total of 150,000 U/L of Ba-amy were attained under constitutive promoter in P. pastoris, which is 15-fold higher than that of the wild strain B. acidicola (10,000 U/L). The recombinant P. pastoris integrated two copies of Ba-amy under GAP promoter. The pure Ba-amy expressed in P. pastoris is a glycoprotein of 66 kDa, which is optimally active at pH 4.0 and 60 °C with a T 1/2 of 25 min at 70 °C. The K m, V max and K cat values of the recombinant Ba-amy are 1.66 mg/mL, 53.6 µmol/mg/min and 106.8/s, respectively. The enzyme generates maltose (30 %), maltotriose (20 %) and other higher maltooligosaccharides from starch, thus, useful in baking as an antistale. This is the first report on the optimization of extracellular production of recombinant acidic α-amylase of an acidophilic bacterium.
1489 related Products with: Production of Ca(2+)-Independent and Acidstable Recombinant α-Amylase of Bacillus acidicola Extracellularly and its Applicability in Generating Maltooligosaccharides.Recombinant Human Androge Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Macrophage Colony Stimula Macrophage Colony Stimula Androgen Receptor (Ab 650 Recombinant Influenza HA Recombinant Influenza HA Recombinant Influenza HA Recombinant HIV-1 pol Int
#27693650 2016/10/03 Save this To Up
MOMP from Campylobacter jejuni Is a Trimer of 18-Stranded β-Barrel Monomers with a Ca(2+) Ion Bound at the Constriction Zone.The Gram-negative organism Campylobacter jejuni is the major cause of food poisoning. Unlike Escherichia coli, which has two major porins, OmpC and OmpF, C. jejuni has one, termed major outer membrane protein (MOMP) through which nutrients and antibiotics transit. We report the 2.1-Å crystal structure of C. jejuni MOMP expressed in E. coli and a lower resolution but otherwise identical structure purified directly from C. jejuni. The 2.1-Å resolution structure of recombinant MOMP showed that although the protein has timeric arrangement similar to OmpC, it is an 18-stranded, not 16-stranded, β-barrel. The structure has identified a Ca(2+) bound at the constriction zone, which is functionally significant as suggested by molecular dynamics and single-channel experiments. The water-filled channel of MOMP has a narrow constriction zone, and single-molecule studies show a monomeric conductivity of 0.7±0.2 nS and a trimeric conductance of 2.2±0.2 nS. The ion neutralizes negative charges at the constriction zone, reducing the transverse electric field and reversing ion selectivity. Modeling of the transit of ciprofloxacin, an antibiotic of choice for treating Campylobacter infection, through the pore of MOMP reveals a trajectory that is dependent upon the presence metal ion.
2421 related Products with: MOMP from Campylobacter jejuni Is a Trimer of 18-Stranded β-Barrel Monomers with a Ca(2+) Ion Bound at the Constriction Zone.Campylobacter jejuni anti OMNICON® ZONE READER SYS CA 19-9 antibody, Monoclo CA 19-9 antibody, Monoclo Chlamydia trachomatis MOM Chlamydia trachomatis MOM CA 50 antibody, Monoclona CA 15-3 antibody, Monoclo CA 15-3 antibody, Monoclo CA 19-9 antibody, Monoclo CA 19-9 antibody, Monoclo V-ATPase 116 kDa isoform
#27297450 2016/09/19 Save this To Up
Expression and characterization of a lipase-related protein in the malpighian tubules of the Chinese oak silkworm, Antheraea pernyi.Lipases are ubiquitous enzymes in nature, which play a crucial role in fat metabolism by catalyzing the hydrolysis of triacylglycerol to free fatty acids and glycerol. However, reports concerning insect lipase are rare. In this study, we studied the expression and activity of a lipase-related protein from Antheraea pernyi (ApLRP). Recombinant ApLRP was expressed in Escherichia coli cells and used to raise rabbit anti-ApLRP polyclonal antibodies. ApLRP mRNA and protein expression were abundant in the midgut and malpighian tubules, respectively. After challenge with four different microorganisms (E. coli, Beauveria bassiana, Micrococcus luteus and nuclear polyhedrosis virus), the expression levels of ApLRP mRNA in midgut were inducted significantly compared with the control. The different pathogens induced different ApLRP gene expression patterns. The optimum temperature and pH for the enzyme's activity were 35°C and 7.0, respectively. ApLRP activity was stimulated in the presence of Mg2+, Na+, Ca2+ and b-mercaptoethanol; while Zn2+, Cu2+ and Fe3+ inhibited its activity. Detergents such as SDS, glycerol and Tween-20 increased the lipase activity by 20-30%. Our results indicated that ApLRP might play an important role in the innate immunity of insects.
1262 related Products with: Expression and characterization of a lipase-related protein in the malpighian tubules of the Chinese oak silkworm, Antheraea pernyi.Apoptosis Phospho-Specifi EGF Phospho-Specific Arra Thermal Shaker with cooli FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Multiple organ tumor tiss HIV 1 intergase antigen. DNA (cytosine 5) methyltr
#27174428 2016/07/15 Save this To Up
Mining of Ruminant Microbial Phytase (RPHY1) from Metagenomic Data of Mehsani Buffalo Breed: Identification, Gene Cloning, and Characterization.Phytases have been widely used as animal feed supplements to increase the availability of digestible phosphorus, especially in monogastric animals fed cereal grains. The present study describes the identification of a full-length phytase gene of Prevotella species present in Mehsani buffalo rumen. The gene, designated as RPHY1, consists of 1,251 bp and is expressed into protein with 417 amino acids. A homology search of the deduced amino acid sequence of the RPHY1 phytase gene in a nonredundant protein database showed that it shares 92% similarity with the histidine acid phosphatase domain. Subsequently, the RPHY1 gene was expressed using a pET32a expression vector in Escherichia coli BL21 and purified using a His60 Ni-NTA gravity column. The mass of the purified RPHY1 was estimated to be approximately 63 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal RPHY1 enzyme activity was observed at 55°C (pH 5) and exhibited good stability at 5°C and within the acidic pH range. Significant inhibition of RPHY1 activity was observed for Mg2+ and K+ metal ions, while Ca2+, Mn2+, and Na+ slightly inhibited enzyme activity. The RPHY1 phytase was susceptible to SDS, and it was highly stimulated in the presence of EDTA. Overall, the observed comparatively high enzyme activity levels and characteristics of the RPHY1 gene mined from rumen prove its promising candidature as a feed supplement enzyme in animal farming.
1501 related Products with: Mining of Ruminant Microbial Phytase (RPHY1) from Metagenomic Data of Mehsani Buffalo Breed: Identification, Gene Cloning, and Characterization.pYLEX1 - Expression Vect Ofloxacin CAS Number [824 MIC2 Gene Protein, CD99; MIC2 Gene Protein, CD99; MIC2 Gene Protein, CD99; T4 SSB (gene 32) protein T4 SSB (gene 32) protein T4 SSB (gene 32) protein T4 SSB (gene 32) protein DNA (cytosine 5) methyltr Human Epstein-Barr Virus Androgen Receptor (Phosph
#27055052 2016/04/08 Save this To Up
Characterization of Calflagin, a Flagellar Calcium-Binding Protein from Trypanosoma congolense.Identification of species-specific trypanosome molecules is important for laboratory- and field-based research into epidemiology and disease diagnosis. Although Trypanosoma congolense is the most important trypanosome pathogen of cattle in Africa, no species-specific molecules found in infective bloodstream forms (BSF) of the parasites have been identified, thus limiting development of diagnostic tests.
1161 related Products with: Characterization of Calflagin, a Flagellar Calcium-Binding Protein from Trypanosoma congolense.S100 alpha - Rabbit polyc Human S100 Calcium Bindin calcium binding protein P Chicken S100 calcium bind ELISA kit Calcyclin,Chick Acyl CoA binding Protein Mouse Anti-Human Retinol ribosome binding protein ribosome binding protein SH3 domain-binding protei Guanylate-binding protein amyloid beta precursor pr
#26896488 2016/06/25 Save this To Up
Expression and characterization of EF-hand I loop mutants of aequorin replaced with other loop sequences of Ca2+-binding proteins: an approach to studying the EF-hand motif of proteins.The binding properties of Ca(2+) to EF-hand I of aequorin (AQ) were characterized by replacing the loop sequence of EF-hand I (AQ[I]) with other known loop sequences of Ca(2+)-binding proteins, including photoproteins (aequorin, clytin-I, clytin-II and mitrocomin), Renilla luciferin-binding protein (RLBP) and calmodulin (CaM). For evaluation of the binding affinity of Ca(2+) to AQ[I] mutants, the half-decay time of the maximum intensity in the luminescence reaction triggered by Ca(2+) was used as an indicator and 22 kinds of AQ[I] mutants were expressed in Escherichia coli cells. AQ[I] mutants replaced with the EF-hand I and EF-hand III from photoproteins showed sufficient luminescence activity, but it was not shown by other EF-hands from RLBP and CaM. An AQ[I] mutant with a lysine or arginine residue at the second position of the non-conserved amino acid residue showed a slow-decay pattern of luminescence, indicating that the Ca(2+)-binding affinity to aequorin was reduced by a positive charge at the second position of the loop sequence. The specific loop sequence of the EF-hand I motif in aequorin caused the specific Ca(2+)-triggered luminescence pattern.
2212 related Products with: Expression and characterization of EF-hand I loop mutants of aequorin replaced with other loop sequences of Ca2+-binding proteins: an approach to studying the EF-hand motif of proteins.Rabbit Anti-Human Calpain Recombinant Human IFN-alp Recombinant Human IFN-alp Native Influenza HA (A To Native Influenza HA (A To Native Influenza HA (A To Anti Galectin(Gal 3) Huma Apoptosis Phospho-Specifi EGF Phospho-Specific Arra FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu
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