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Search results for: 43kDa


#33045298   2020/10/09 To Up

Molecular characterization, expression and functional analysis of TGFβ1-b in crucian carp (Carassius carassius).

Transforming growth factor β1 (TGFβ1) is a polyfunctional cytokine with important roles in growth, differentiation and immune function in various animals. In this study, PCR, bioinformatics, real-time quantitative PCR, prokaryotic expression, protein purification and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-TOF-MS) were applied to investigate the structural features and function of TGFβ1-b in crucian carp. The complete coding sequence (CDS) of TGFβ1-b was 1134 bp in length and was submitted to GenBank (ID: MH473141). TGFβ1-b encoded a putative protein of 377 amino acids and included a signal peptide consisting of 22 amino acids. TGFβ1-b was relatively conservative in fish and distant from mammals in terms of evolutionary relationship. TGFβ1-b was found to be expressed in various tissues, with the highest expression in the kidney. The expressions of TGFβ1-b in muscle, heart and liver were increased with the addition of Rhodopseudomonas palustris, Bacillus subtilis and Enterococcus faecium at 30 days (p < 0.01). While, the expressions of SMAD2, SMAD3 and SMAD7 were also up-regulated with the addition of R. palustris at 20 days (p < 0.01). The expression of TGFβ1-b could be affected by time and group factors (p < 0.05). Moreover, the expression vector TGFβ1-b-pDE2 was successfully constructed. Prokaryotic expression indicated that a 43 kDa target protein was obtained after induction with 1.5 mM isopropyl-beta-D-thiogalactopyranoside (IPTG) for 3.5 h at 37 °C for 200 r/h. The activities of alkaline phosphatase and lysozyme in injection TGFβ1-b protein group (ITg) and feeding broken bacterial liquid group (BTg) were significantly increased at 24 h (p < 0.01). And the activities of superoxide dismutase in ITg were significantly increased at 36 h (p < 0.01). Besides, the expressions of heat shock protein 30 and heat shock protein 47 in ITg and BTg were significantly increased (p < 0.01). Whereas, the expression of interleukin-11 was significantly reduced (p < 0.01). These results indicated that TGFβ1-b protein might play a role in immunity of crucian carp.
Chenyang Li, Li Wang

1697 related Products with: Molecular characterization, expression and functional analysis of TGFβ1-b in crucian carp (Carassius carassius).

900 tests100ug50 ml100 mg100ug Lyophilized1 Set

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#32958236   2020/09/01 To Up

The prion-like nature of amyotrophic lateral sclerosis.

The misfolding, aggregation, and deposition of specific proteins is the key hallmark of most progressive neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS). ALS is characterized by the rapid and progressive degenerations of motor neurons in the spinal cord and motor cortex, resulting in paralysis of those who suffer from it. Pathologically, there are three major aggregating proteins associated with ALS, including TAR DNA-binding protein of 43kDa (TDP-43), superoxide dismutase-1 (SOD1), and fused in sarcoma (FUS). While there are ALS-associated mutations found in each of these proteins, the most prevalent aggregation pathology is that of wild-type TDP-43 (97% of cases), with the remaining split between mutant forms of SOD1 (~2%) and FUS (~1%). Considering the progressive nature of ALS and its association with the aggregation of specific proteins, a growing notion is that the spread of pathology and symptoms can be explained by a prion-like mechanism. Prion diseases are a group of highly infectious neurodegenerative disorders caused by the misfolding, aggregation, and spread of a transmissible conformer of prion protein (PrP). Pathogenic PrP is capable of converting healthy PrP into a toxic form through template-directed misfolding. Application of this finding to other neurodegenerative disorders, and in particular ALS, has revolutionized our understanding of cause and progression of these disorders. In this chapter, we first provide a background on ALS pathology and genetic origin. We then detail and discuss the evidence supporting a prion-like propagation of protein misfolding and aggregation in ALS with a particular focus on SOD1 and TDP-43 as these are the most well-established models in the field.
L McAlary, J J Yerbury, N R Cashman

2915 related Products with: The prion-like nature of amyotrophic lateral sclerosis.

21 kit150 IU100.00 ul 5 G500 Units1 ml1 100ul

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#32735084   2020/07/31 To Up

Hippocampal sclerosis, TDP-43, and the duration of the symptoms of dementia of AD patients.

To examine the relationship between duration of the cognitive symptoms, from the earliest reported symptom to death, and hippocampal sclerosis (HS) and TAR-DNA binding protein of 43kDA (TDP-43) in Alzheimer's disease (AD) patients.
Oscar L Lopez, Julia Kofler, YueFang Chang, Sarah B Berman, James T Becker, Robert A Sweet, Neelesh Nadkarni, Riddhi Patira, M Ilyas Kamboh, Ann D Cohen, Beth E Snitz, Lewis H Kuller, William E Klunk

1700 related Products with: Hippocampal sclerosis, TDP-43, and the duration of the symptoms of dementia of AD patients.

5 Gmin 2 cartons100.00 ul 100 G1200 units1500 Units1

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#32507755   // To Up

[Frontotemporal Lobar Degeneration: A Historical Overview of the Concept].

Arnold Pick described a focal cortical syndrome caused by focal temporal and/or frontal cortical atrophy, later reffered to as Pick's disease (PiD), a prototype of frontotemporal lobar degeneration (FTLD). In contrast to the current concept of PiD, the presence of Pick bodies (tau-positive inclusions) was not thought to be necessary for the diagnosis of PiD. Four out of the seven patients in his original paper had predominant left temporal atrophy and language related symptoms corresponding to semantic dementia. It is now known that most patients with semantic dementia have transactive response DNA-binding protein 43kDa (TDP-43) pathology rather than tau pathology. The original concept of PiD was substantially similar to the current concept of FTLD, which has heterogeneous molecular pathology including tau, TDP-43 and fused in sarcoma (FUS).
Shinobu Kawakatsu, Ryota Kobayashi, Kazutaka Sakamoto, Koich Otani

1946 related Products with: [Frontotemporal Lobar Degeneration: A Historical Overview of the Concept].

100.00 ul1 ml 100ul100.00 ul100 1 ml

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#32473189   2020/05/27 To Up

Characterization of an efficient extracellular cyanophycinase and its encoding cphE gene from Streptomyces pratensis strain YSM.

Until now, no enzymes were described that hydrolyze cyanophycin granular protein (CGP) from a species of the genus Streptomyces. An isolate able to hydrolyze CGP was identified as Streptomyces pratensis strain YSM. The CGPase from S. pratensis strain YSM had an optimum activity at 42 °C and pH 8.5, and was able to degrade CGP at a rate of 12 ± 0.3 μg/mL min. Additionally, this CGPase hydrolyzes water-soluble CGP significantly faster than water-insoluble CGP. The molecular mass of CGPase subunits from S. pratensis strain YSM as determined by SDS-PAGE was about 43 kDa, and the enzyme was entirely inhibited by serine-protease inhibitors. The CGPase coding gene (cphE) was amplified from genomic DNA using primers designed form consensus sequence of putative CGPase sequences. The cphE was 1427 bp encoding a CGPase of 420 amino acids that showed about 44% and 22% similarities to CGPase from Pseudomonas anguilliseptica BI and Synechocystis sp. PCC 6803, respectively. The catalytic triad and serine-protease residues (GXSXG) were identified in the CphE sequence. Dipeptides and tetrapeptides were identified as hydrolysis products. Biotechnological exploitation of S. pratensis strain YSM for CGPase production might have an advantage due to the reduction of separation costs and its ability to degrade CGP in phosphate buffer saline using actively growing or resting cells.
Yasser Elbahloul, Alexander Steinbüchel

1555 related Products with: Characterization of an efficient extracellular cyanophycinase and its encoding cphE gene from Streptomyces pratensis strain YSM.

50μl100ug Lyophilized50 mg25 mg100ug1 mL96T100ug Lyophilized100ug50μl1 ml10 mg

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#31773773   2019/12/10 To Up

Amyotrophic Lateral Sclerosis with Pallidonigroluysian Degeneration: A Clinicopathological Study.

The pallidonigroluysian (PNL) system, the primary component of corticosubcortical circuits, is generally spared in amyotrophic lateral sclerosis (ALS). We evaluated the clinicopathological features of an unusual form of ALS with PNL degeneration (PNLD) and assessed whether ALS with PNLD represents a distinct ALS subtype.
Junko Ito, Hiroshi Shimizu, Kentaro Ohta, Jiro Idezuka, Hajime Tanaka, Hiroshi Kondo, Takashi Nakajima, Hitoshi Takahashi, Kohei Akazawa, Osamu Onodera, Akiyoshi Kakita

2303 related Products with: Amyotrophic Lateral Sclerosis with Pallidonigroluysian Degeneration: A Clinicopathological Study.

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#31722315   // To Up

[Immunotherapy Against Misfolded Proteins in ALS].

Protein misfolding crucially underlies the pathogenesis of amyotrophic lateral sclerosis (ALS). Mutant superoxide dismutase 1 (SOD1) and TAR DNA-binding protein 43kDa (TDP-43) are major causal proteins for familial and sporadic ALS, respectively, provoking diverse pathogenic pathways in both intracellular and extracellular environments. Of note, cell-to-cell spreading behavior is implicated in the progression of neurodegeneration, suggesting application in immunotherapies including vaccination, and antibody application as a molecular targeting therapy, due to strict antigen-specificity. Although immunotherapy of intravenous application of full-length immunoglobulin is aimed at targeting the extracellular proteins because of low access to the cytosol, it is therefore necessary to generate expression vectors for variable single chain fragments (scFv) that target intracellular proteins. Despite the advantages of scFv, such as low molecular size and the ability to apply molecular modifications adding proteolytic signals, safety and efficacy should be cautiously estimated in preclinical studies, using appropriate animal models. In ALS, we firstly succeeded in the vaccination of mutant SOD1 transgenic mice, which was followed by accumulating evidence showing the efficacy of immunization against misfolded SOD1. In TDP-43 proteinopathy, we are developing immunotherapy using intrabodies with proteolytic properties against mislocalized or aggregated forms of TDP-43 inside cells.
Makoto Urushitani, Yoshitaka Tamaki, Ryota Hikiami, Sumio Minamiyama

1585 related Products with: [Immunotherapy Against Misfolded Proteins in ALS].

10050 50501001050 100010210 1 mg

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#31670129   2019/10/19 To Up

Purification, characterization, and functional properties of a novel glycoprotein from tartary buckwheat (Fagopyrum tartaricum) seed.

A pure glycoprotein (BGP4-I) was obtained from tartary buckwheat seeds by aqueous extraction followed by DEAE-Sepharose Fast Flow ion exchange chromatography and Sephadex G-100 gel filtration chromatography. The average molecular weight of BGP4-I, as determined by high performance gel permeation chromatography, was 123.43 kDa. The structure of BGP4-I was characterized based on Fourier transform infrared spectroscopy, circular dichroism spectroscopy, and nuclear magnetic resonance spectroscopy, etc. Based on the nano-liquid chromatography-coupled electrospray ionization mass spectrometry analysis of the amino acid sequence of BGP4-I, belongs unequivocally to the glycosyl hydrolase family 1 in the Carbohydrate Active Enzymes database by alignment studies. The specific activity of BGP4-I was 18.44 μmol/min/mg on the substrate p-nitrophenyl-β-d-glucopyranoside. Furthermore, BGP4-I is unique in its specificity for some substrates. These results suggest that the BGP4-I from tartary buckwheat seeds is a novel specific β-glucosidase setting the foundation for potential applications in the food industry.
Yuhui Zhou, Yanli Ma, Lirong Li, Xilian Yang

2893 related Products with: Purification, characterization, and functional properties of a novel glycoprotein from tartary buckwheat (Fagopyrum tartaricum) seed.

1 ml100ug Lyophilized5ml1 mL1 kit(96 Wells)25 mg100ug1 kit(96 Wells)1000 tests100ml100ug Lyophilized100ul

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#31568752   2019/09/27 To Up

Molecular mechanism of the inhibition of TDP-43 amyloidogenesis by QBP1.

Transactive Response DNA-Binding Protein of 43 kDa (TDP-43) is an essential human protein implicated in Amyotrophic Lateral Sclerosis (ALS) and common dementias. Its C-terminal disordered region, composed of residues 264-414 includes a hydrophobic segment (residues 320-340), which drives physiological liquid/liquid phase separation and a Q/N-rich segment (residues 341-357), which is essential for pathological amyloid formation. Due to TDP-43's relevance for pathology, identifying inhibitors and characterizing their mechanism of action are important pharmacological goals. The Polyglutamine Binding Peptide 1 (QBP1), whose minimal active core is the octapeptide WGWWPGIF, strongly inhibits the aggregation of polyQ-containing amyloidogenic proteins such as Huntingtin. Rather promiscuous, this inhibitor also blocks the aggregation of other glutamine containing amyloidogenic proteins, but not Aβ, and its mechanism of action remains unknown. Using a series of spectroscopic assays and biochemical tests, we establish that QBP1 binds and inhibits amyloid formation by TDP-43's Q/N-rich region. NMR spectroscopic data evince that the aromatic rings of QBP1 accept hydrogen bonds from the HN groups of the Asn and Gln to block amyloidogenesis. This mechanism of blockage may be general to polyphenol amyloid inhibitors.
Miguel Mompeán, Daniel Ramírez de Mingo, Rubén Hervás, María Del Carmen Fernández-Ramírez, Mariano Carrión-Vázquez, Douglas V Laurents

1884 related Products with: Molecular mechanism of the inhibition of TDP-43 amyloidogenesis by QBP1.

10mg 5 G 1 G5mg10mg96 assays 6 ml Ready-to-use 10 mg1mg500 Units20mg20 ug

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