Log In Sign up
The largest database of trusted experimental protocols
> Chemicals & Drugs > Amino Acid > Synapsin I

Synapsin I

Synapsins are a family of phosphoproteins that associate with the cytoplasmic surface of synaptic vesicles and play a key role in the regulation of neurotransmitter release.
Synapsin I, the most extensively studied member of the family, is involved in the tethering of synaptic vesicles to the actin cytoskeleeton, and in the modulation of neurotransmitter release.
It is essentail for the proper functioining of the central nervous system and is implicated in various neurological disorders.
Researchers can leverage the PubCompare.ai platform to streamline their Synapsin I optimization process, locating the best protocols from literature, preprints, and patents, and leveraging AI-powered comparisons to enhance reproducibility and accuracy.

Most cited protocols related to «Synapsin I»

1
Measuring DNA Repair by Transient Transfection
To measure the repair by transient transfection, 2.5×104 cells/cm2 were plated and transfected the next day with 0.8 µg/ml of pCBASce mixed with 3.6 µl/ml of Lipofectamine 2000 (Invitrogen) along with a variety of other vectors. The KU and RAD52 expression vectors were added at 0.8 µg/ml, the ERCC1 vector was added at 0.4 µg/ml, the RAD51-K133R vector was added at 0.1 µg/ml, and the BRC3 vector was added at 0.2 µg/ml. For each experiment, an equivalent amount of empty vector (pCAGGS-BSKX) was included in the parallel transfections. Each of these expression vectors have been previously described [18] (link). GFP positive cells were quantified by flow cytometric analysis (FACS) 3d after transfection on a Cyan ADP (Dako). Amplification of PCR products from sorted GFP+ cells, associated restriction digests, and quantification of bands were performed using the primers KNDRF and KNDRR as previously described for analysis of DR-GFP [50] (link).
To measure repair using the inducible I-SceI protein (TST) in combination with siRNA-mediated inhibition of CtIP, HEK293 cell lines with each of the reporters and stable expression of TST were first plated on 24 well plates at 105 cells/well. The following day, the wells were transfected with 70nM siRNA duplex mixed with 4ul/ml of Lipofectamine 2000 in Optimem (Invitrogen). After 4.5h, transfection complexes were diluted two-fold with media without antibiotics, and 48h after the initiation of transfection, 4OHT was added at 3 µM for 24h. Three days after 4OHT was added, the percentage of GFP+ cells was analyzed by FACS as described above. Knockdown of CtIP levels using the various siRNAs was confirmed by RT-PCR from RNA samples isolated from parallel transfections at the time of 4OHT addition (data not shown). Amplification product was quantified at the threshold cycle by including SYBR green in the PCR reaction and using an iQ5 cycler for real-time analysis at the end of each cycle (BioRad). Products were normalized relative to a primer set directed against actin. Sequences of the siRNAs siCtIP-p (Santa Cruz Biotechnology), and siCtIP-1 [25] (link), and primers for RT-PCR are shown in Figure S1D.
Repair frequencies are the mean of at least three transfections or four 4OHT treatments, and error bars represent the standard deviation from the mean. For some experiments, repair frequencies are shown relative to samples co-transfected with I-SceI and an empty vector (EV). For this calculation, the percentage of GFP+ cells from each sample was divided by the mean value of the EV samples treated in the parallel experiment. Similarly, to calculate the fold-difference in repair between siRNA-treated and control-siRNA treated cells, the percentage of GFP+ cells from each sample was divided by the mean value of control-siRNA samples from the parallel experiment. Statistical analysis was performed using the unpaired t-test.
Bennardo N., Cheng A., Huang N, & Stark J.M. (2008). Alternative-NHEJ Is a Mechanistically Distinct Pathway of Mammalian Chromosome Break Repair. PLoS Genetics, 4(6), e1000110.
Full text: Click here
Publication 2008
Actins Antibiotics Cloning Vectors Flow Cytometry HEK293 Cells lipofectamine 2000 Oligonucleotide Primers Psychological Inhibition RAD52 protein, human RBBP8 protein, human Reverse Transcriptase Polymerase Chain Reaction RNA, Small Interfering SYBR Green I Synapsin I Transfection Transients
2
Soybean Tissue Harvesting for Transcriptome Analysis
The seeds were derived from introgressing G. soja (PI468916) into G. max (A81-356022). Specifically, the BC5F5 plant P-C609-45-2-2 was heterozygous for the LG I protein QTL introgression from G. soja. These seeds were planted directly into pots containing Bradyrhizobium japonicum-inoculated soil and supplemented with full nutrient fertilizer (Osmocote 14-14-14) in growth chambers at the University of Minnesota. Chambers were set initially to a photoperiod of 14/10 and thermocycle of 22°C/10°C and monitored to mimic Illinois field growing conditions. Relative humidity settings were 50-60%, and light intensity was measured at 550-740 μE m-2 sec-1. All harvests occurred at 1400 hours and consisted of samples pooled from a minimum of three plants [52 (link)]. Samples were harvested from plants in parallel and flash frozen in liquid nitrogen before storage at -80°C. Open flowers and young leaf tissue samples were collected simultaneously. Pods and seeds were harvested by seed weight and pod lengths that correspond to approximated Days After Flowering (DAF) as specified. The one-cm pod was processed intact (approximately 7-DAF), while the four and five cm pods (approximately 10-13 DAF and 14-17 DAF) were divided into seed and pod-shell components. Seed 21-DAF, Seed 25-DAF, Seed 28-DAF and Seed 35-DAF had seed weights between 10 and 25 milligrams, 25 and 50 milligrams, 50 and 100 milligrams, 100 and 200 milligrams, and greater than 200 milligrams, respectively.
Root and nodule tissues were harvested from plants grown in growth chambers set to 16-hr photoperiods with light intensities ranging from 310-380 μE m-2 sec-1. Seeds were imbibed for three days, planted in quartz sand and fertilized with a full nutrient solution. Root tissue was harvested after 12 days. Nodules were harvested at 20-25 days after inoculation; for these samples, plants were fertilized for the first seven days with nutrient solution containing 3.5 mM NO3 and subsequently fertilized every other day with a full nutrient solution lacking nitrogen.
Soybean tissue samples were ground with liquid nitrogen by mortar and pestle. Total RNA was isolated by a modified TRIzol® (Invitrogen) protocol [53 (link)]. DNA was removed by digest with on-column RNase-free DNase (Qiagen), and RNA was purified and concentrated by RNeasy column (Qiagen). RNA quality was evaluated by gel electrophoresis, spectrophotometer and Agilent 2100 bioanalyzer.
Severin A.J., Woody J.L., Bolon Y.T., Joseph B., Diers B.W., Farmer A.D., Muehlbauer G.J., Nelson R.T., Grant D., Specht J.E., Graham M.A., Cannon S.B., May G.D., Vance C.P, & Shoemaker R.C. (2010). RNA-Seq Atlas of Glycine max: A guide to the soybean transcriptome. BMC Plant Biology, 10, 160.
Full text: Click here
Publication 2010
Bradyrhizobium japonicum Deoxyribonucleases Electrophoresis Freezing Heterozygote Humidity Light Marijuana Abuse Nitrogen Nutrients Plant Embryos Plant Leaves Plant Roots Plants Quartz Ribonucleases Soybeans Synapsin I Tissues trizol Vaccination
3
Comprehensive Drug-Target Interaction Dataset
Dataset for drugs and targets with known pharmacological interactions were extracted from DrugBank database (http://drugbank.ca/, accessed on June 1st 2011), which so far contains 6707 drug entries including 1436 FDA-approved small molecule drugs, 134 FDA-approved biotech (protein/peptide) drugs, 83 nutraceuticals and 5086 experimental drugs. Additionally, 4228 non-redundant protein (i.e. drug target/enzyme/transporter/carrier) sequences are also potentially linked to these entries. To confirm the quality of this data set, we have carefully compared this database with other databases such as STITCH, SuperTarget and KEGG database, as well as the literature [22] (link), [23] (link). In the process of building dataset, some drugs and targets (such as nitric oxide and ribosomal protein Thx) were omitted since their chemical descriptors cannot be calculated (details are provided in Supporting Information S1). As a result, a dataset including 6511 drugs and 3987 targets was applied in this work as the benchmark dataset (detailed information of these drugs and targets was given in Supporting Information S2 and S3).
Yu H., Chen J., Xu X., Li Y., Zhao H., Fang Y., Li X., Zhou W., Wang W, & Wang Y. (2012). A Systematic Prediction of Multiple Drug-Target Interactions from Chemical, Genomic, and Pharmacological Data. PLoS ONE, 7(5), e37608.
Full text: Click here
Publication 2012
Drug Delivery Systems Enzymes Investigational New Drugs Membrane Transport Proteins Nutraceuticals Oxide, Nitric Peptides Pharmaceutical Preparations Proteins Ribosomal Proteins Synapsin I
4
Generation and Characterization of iPSCs

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2010
Biopsy Cloning Vectors DNA, Complementary Embryo Ethics Committees, Research Females Fibroblasts Gentamicin Homo sapiens Human Embryonic Stem Cells Hyperostosis, Diffuse Idiopathic Skeletal IGF1 protein, human Induced Pluripotent Stem Cells Infection KLF4 protein, human Lentivirus matrigel MECP2 protein, human Mice, Laboratory Neurons Oncogenes, myc POU5F1 protein, human Retroviridae Short Hairpin RNA SOX2 protein, human Stem Cells Synapsin I Vertebral Column
5
Cloning and Expression of GCaMP Variants
The original GCaMP2 expression construct was obtained from M. Kotlikoff 34 (link), TN-XXL from O. Griesbeck 6 , and D3cpV from A. Palmer 13 (link). GCaMPs were sub-cloned into pRSETa for expression and purification in E. coli. GCaMPs were sub-cloned into pCMV for HEK293 cell assays and cultured brain slice experiments. GCaMP variants, TN-XXL and D3cpV were sub-cloned into the pCAGGS vector with a CAG promoter (CMV-enhancer, β-actin promoter, and regulatory element from the woodchuck hepatitis virus35 (link) (WPRE)) for in utero electroporation 36 (link). pCAG-mCherry 37 (link) was co-transfected with GCaMPs for cultured hippocampal slices and in utero electroporation for better control of expression level. To make transgenic worms and flies, GCaMPs were sub-cloned into pSM under control of the str-2 promoter (from C.I. Bargmann) and pMUH (a gift from Barret Pfeiffer, Janelia Farm Research Campus), respectively. pMUH-GCaMPs were incorporated into an attP40 integrase site on the second Drosophila chromosome 38 (link) (Genetic Services, Inc.). For in vivo calcium imaging in mice, GCaMP2 and GCaMP3 were expressed using an adeno-associated virus 2/1 (AAV2/1) driving the sensor under control of the pan-neuronal human synapsin-1 promoter 39 (link). GCaMP2 and GCaMP3 were sub-cloned into the rAAV-hSYN expression vector, and live virus was produced (University of Pennsylvania Vector Core Services). All constructs were verified by sequencing.
Tian L., Hires S.A., Mao T., Huber D., Chiappe M.E., Chalasani S.H., Petreanu L., Akerboom J., McKinney S.A., Schreiter E.R., Bargmann C.I., Jayaraman V., Svoboda K, & Looger L.L. (2009). Imaging neural activity in worms, flies and mice with improved GCaMP calcium indicators. Nature methods, 6(12), 875-881.
Publication 2009
Actins Adeno-associated virus-2 Animals, Transgenic Biological Assay Brain Calcium Chromosomes Cloning Vectors Diptera Drosophila Electroporation Escherichia coli GCaMP2 HEK293 Cells Helminths Hepatitis A Homo sapiens Integrase Marmota Mice, Laboratory Neurons Regulatory Sequences, Nucleic Acid Service, Genetic Synapsin I Uterus Virus

Most recents protocols related to «Synapsin I»

1
Candidate Gene Screening for Tobacco Mutants
Not available on PMC !

Example 5

Three tobacco lines, FC401 wild type (Wt); FC40-M207 mutant line fourth generation (M4) and FC401-M544 mutant line fourth generation (M4) were used for candidate gene screening. Low anatabine traits were confirmed for the two tobacco mutant lines (M207 and M544) in root and leaf before screening (see FIG. 3).

RNA was extracted from root tissues of wild type (Wt) FC401, M207 and M544 with RNeasy Plus Mini kit from Quiagen Inc. following the manufacturer's protocol. cDNA libraries were prepared from the RNAs using In-Fusion® SMARTer® Directional cDNA Library Construction Kit from Clontech Inc. cDNA libraries were diluted to 100 ng/μl and used as the template for candidate gene PCR screening.

PCR amplifications were performed in 50 μl final volumes that contained 50-100 ng of template DNA (i.e., the cDNA library) and 0.2 μM of primers (Fisher Scientific) using the Platinum® Taq DNA Polymerase High Fidelity kit (Life Technology Inc.). Thermocycling conditions included a 5 min incubation at 94° C.; followed by 34 cycles of 30 seconds at 94° C., 30 seconds at 58° C., 1 min 30 seconds at 68° C.; with a final reaction step of 68° C. for 7 mins. The PCR products were evaluated by agarose gel electrophoresis, and desired bands were gel purified and sequenced using an ABI 3730 DNA Analyzer (ABI).

51 candidate genes (listed in Table 4) were cloned from F401, Wt, M207 and M544 lines, and sequenced for single nucleotide polymorphism (SNP) detection.

TABLE 4
Listing of Candidate Genes for Screening
Quinolinate Synthase A-1Pathogenesis related protein 1
Allene oxide synthaseAllene oxide cyclase
ET861088.1 Methyl esteraseFH733463.1 TGACG-sequence specific transcription factor
FH129193.1 Aquaporin-TransportFH297656.1 Universal stress protein
Universal stress protein Tabacum sequenceFH077657.1 Scarecrow-like protein
FH864888.1 EIN3-binding F-box proteinFH029529.1 4,5 DOPA dioxygenase
FI010668.1 Ethylene-responsive transcription EB430189 Carboxylesterase
factor
DW001704 Glutathione S transferaseEB683763 Bifunctional inhibitor/lipid transfer protein/seed
storage 2S albumin
DW002318 Serine/threonine protein kinaseDW004086 Superoxide dismutase
DW001733 Lipid transfer protein DIRIDW001944 Protein phosphatase 2C
DW002033EB683763 Bifunctional inhibitor/lipid transfer protein/seed
storage 2S albumin
DW002318 Serine/threonine protein kinaseDW002576 Glycosyl hydrolase of unknown function DUF1680
EB683279EB683763
EB683951FG141784 (FAD Oxidoreductase)
BBLa-Tabacum sequencesBBLb
BBLeBBLd
PdrlPdr2
Pdr3Pdr5a
Pdr5bNtMATEl
NtMATE2NtMATE3
WRKY8EIG-I24
WRKY3WRKY9
EIG-E17AJ748263.1 QPT2 quinolinate phosphoribosyltransferase
AJ748262.1 QPT1

US11873500B2. Genetic locus imparting a low anatabine trait in tobacco and methods of using (2024-01-16). ALTRIA CLIENT SERVICES LLC [US]. Inventors: Chengalrayan Kudithipudi [US], Alec J. Hayes [US], Robert Frank Hart [US], Yanxin Shen [US], Jesse Frederick [US], Dongmei Xu [US].
Full text: Click here
Patent 2024
Albumins allene oxide cyclase allene oxide synthase Amino Acid Sequence anatabine Carboxylesterase cDNA Library Dioxygenases Dopa Electrophoresis, Agar Gel Esterases Ethylenes Genes Glutathione S-Transferase Heat Shock Proteins Histocompatibility Testing Hydrolase lipid transfer protein Neoplasm Metastasis Nicotiana Nicotinate-nucleotide pyrophosphorylase (carboxylating) NOS1 protein, human Oligonucleotide Primers Oxidoreductase pathogenesis Plant Leaves Plant Roots Platinum Protein-Serine-Threonine Kinases Protein-Threonine Phosphatase Protein Kinases protein methylesterase Protein Phosphatase Protein Phosphatase 2C Proteins Quinolinate RNA Single Nucleotide Polymorphism Superoxide Dismutase Synapsin I Taq Polymerase Transcription, Genetic Transcription Factor Transfer Factor Water Channel
2
Characterization of Plasmodium falciparum Glutamine Synthetase
Not available on PMC !

Example 2

Prokaryotic GS-I proteins found in some eukaryotes frequently display no GS catalytic activity and may have different functions. In humans, for example, most tissues/organs express only catalytically-active GS-II. In contrast, human GS-I does not exhibit GS activity. It is expressed only in the lens of the eye and has designated lengsin (lens GS-like protein), probably with a structural role.

To examine the catalytic activity of PfGS-I, PfGS-I gene was cloned and expressed in E. coli and then GS activity of the purified protein was assayed. PfGS-I produced glutamine from glutamate in the presence of ATP, Mg2+ and ammonia (FIG. 2A) demonstrates that PfGS-I is a functional GS.

US11877996B1. Arsinothricin as a multi-stage antimalarial (2024-01-23). None [US], None [US], None [US], None [US]. Inventors: Masafumi Yoshinaga [US], Barry P. Rosen [US], Jun Li [US], Guodong Niu [US].
Full text: Click here
Patent 2024
Ammonia enzyme activity Escherichia coli Eukaryota Genes Glutamate Glutamine Homo sapiens Lens, Crystalline Prokaryotic Cells Proteins Synapsin I Tissues
3
Quantifying Bacterial Adhesion to Nasal Cells

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2023
Buffers Dialysis Epithelial Cells Flow Cytometry Fluorescein Fluorescein-5-isothiocyanate Healthy Volunteers Homo sapiens isothiocyanate Nose prisma Proteins Septums, Nasal Sodium Chloride Stains Synapsin I Tromethamine
4
Transcriptome Assembly and Annotation of Siberian Salamander
Total RNA was extracted separately from testis (n = 4) and ovary (n = 4) tissues using TRIzol (Invitrogen). For each sample, RNA quality and concentration were assessed using agarose gel electrophoresis, a NanoPhotometer spectrophotometer (Implen, CA), a Qubit 2.0 Fluorometer (ThermoFisher Scientific), and an Agilent BioAnalyzer 2,100 system (Agilent Technologies, CA), requiring an RNA integrity number (RIN) of 8.5 or higher; one ovary sample failed to meet these quality standards and was excluded from downstream analyses. Sequencing libraries were generated using the NEBNext Ultra RNA Library Prep Kit for Illumina following the manufacturer’s protocol. After cluster generation of the index-coded samples, the library was sequenced on one lane of an Illumina Hiseq 4,000 platform (PE 150). Transcriptome sequences were filtered using Trimmomatic-0.39 with default parameters (Bolger et al., 2014 (link)). 30, 848, 170 to 39, 695, 323 reads were retained for each testis or ovary sample, and in total, 290, 925, 984 reads remained, with a total length of 42, 385, 060,050 bp. Remaining reads of all testis and ovary samples were combined and assembled using Trinity 2.12.0 (Haas et al., 2013 (link)), yielding 573,144 contigs (i.e., putative assembled transcripts). Contigs were clustered using CD-hit-est (95% identity). Completeness of this final de novo transcriptome assembly were assessed using the BUSCO pipeline (Simao et al., 2015 (link)).
Expression levels of contigs in each sample were measured with Salmon (Patro et al., 2017 (link)), and contigs with no raw counts were removed. To annotate the remaining contigs containing autonomous TEs, BLASTp and BLASTx were used against Repbase with an E-value cutoff of 1E-5 and 1E-10, respectively. The aligned length coverage was set to exceed 80% of the queried transcriptome contigs. To annotate contigs containing non-autonomous TEs, RepeatMasker was used with our Ranodon-derived genomic repeat library of non-autonomous TEs (LARD-, TRIM-, MITE-, and SINE-annotated contigs) and the requirement that the transcriptome/genomic contig overlap was >80 bp long, >80% identical in sequence, and covered >80% of the length of the genomic contig. Contigs annotated as conflicting autonomous and non-autonomous TEs were filtered out.
To identify contigs that contained endogenous R. sibiricus genes, the Trinotate annotation suite (Bryant et al., 2017 (link)) was used with an E-value cutoff of 1E-5 for both BLASTx and BLASTp against the Uniport database, and 1E-5 for HMMER against the Pfam database (Wheeler and Eddy, 2013 (link)). To identify contigs that contained both a TE and an endogenous gene (i.e., putative cases where a TE and a gene were co-transcribed on a single transcript), all contigs that were annotated both by Repbase and Trinotate were examined, and the ones annotated by Trinotate to contain a TE-encoded protein (i.e., the contigs where Repbase and Trinotate annotations were in agreement) were not further considered. The remaining contigs annotated by Trinotate to contain a non-TE gene (i.e., an endogenous Ranodon gene) and also annotated either by Repbase to include a TE-encoded protein or by blastn to include a non-autonomous TE were filtered out for the expression analysis.
Wang J., Yuan L., Tang J., Liu J., Sun C., Itgen M.W., Chen G., Sessions S.K., Zhang G, & Mueller R.L. (2023). Transposable element and host silencing activity in gigantic genomes. Frontiers in Cell and Developmental Biology, 11, 1124374.
Full text: Click here
Publication 2023
DNA Library Electrophoresis, Agar Gel Genes Genome Genomic Library Mites Ovary Proteins Salmo salar Short Interspersed Nucleotide Elements Synapsin I Testis Tissues TNFRSF25 protein, human Transcriptome trizol Uniport
5
AP-MS Data Preprocessing and Differential Analysis
The data were first filtered based on the label-free quantification intensities (LFQi) using the following five steps: (i) removal of proteins that were labeled as “only identified by site”, “potential contaminant”, and “reverse”; (ii) removal of all observations with LFQi equals to 0; (iii) removal of outlier samples (based on low overall LFQi; see Fig S3); (iv) removal of proteins that are not present in at least 60% of the samples of a group for each group (a group is defined as the collection of three biological with two technical replicates for one condition, which results in a group size of maximum 6); and (v) filtering against the negative control sample, which is only the beads used for the AP-MS sample preparations, by only considering proteins for further analysis that are significantly higher found in the samples compared with the negative control. In MS analysis–based proteomics data, there are typically two types of missing values, the missing not at random (MNAR) and the missing at random (MAR) (Lazar et al, 2016 (link)). A mixed imputation strategy was chosen, with kNN imputation as the strategy for MAR values (Gatto & Lilley, 2012 (link); Gatto et al, 2021 (link); Rainer et al, 2022 (link)). Other missing values were considered MNAR values and imputed at value 0. After the imputation, differential interaction analysis was performed for each group against the bead control. P-values were adjusted using FDR correction as described by Benjamini and Hochberg (1995) (link). Afterward, all proteins were extracted for each group, which were significantly enriched in the sample (cutoffs: P-value–adjusted: <0.01, log fold change: >1). The data were transformed to have consistent protein and gene name annotations after the data filtering. The data are received from MaxQuant software in UniProt IDs and mapped to HGNC gene names using the HGNC database (retrieved 12/2021). However, one UniProt ID can correspond to multiple HGNC gene names. In this case, manual selection of the gene names of interest was performed. Finally, the HGNC names were mapped to gene IDs of the SysGO database (Luthert & Kiel, 2020 (link)). A couple of proteins could not be found in the SysGO database, and one protein was renamed (i.e., HGNC name: PHB1, which was renamed PHD for SysGO). Then, the technical replicates were merged using the median. In summary, we obtain a dataset with raw LFQi (Table S2) or log2-transformed (Table S3) data with biological triplicates. Data preparation was performed in R (http://www.r-project.org/index.html) using the following packages: dplyr (Beckerman et al, 2017 ), tidyr (Wickham et al, 2019 (link)), stringr (Wickham, 2010 (link)), tidyxl, purr (Mailund, 2019 ), DEP (Zhang et al, 2018 (link)), and limma (Ritchie et al, 2015 (link); Phipson et al, 2016 (link)). The script file for the data preparation and the data pre- and post-preparation are available on Zenodo (Camille et al, 2022 (link)).

Table S2. Raw AP-MS LFQ intensity data with biological triplicates.

Table S3. Log2-transformed AP-MS data with biological triplicates.

Ternet C., Junk P., Sevrin T., Catozzi S., Wåhlén E., Heldin J., Oliviero G., Wynne K, & Kiel C. (2023). Analysis of context-specific KRAS–effector (sub)complexes in Caco-2 cells. Life Science Alliance, 6(5), e202201670.
Full text: Click here
Publication 2023
Biopharmaceuticals Genes Multiple Birth Offspring Proteins Staphylococcal Protein A Synapsin I

Top products related to «Synapsin I»

1
Pvdf membrane by Merck Group
Sourced in United States, Germany, China, United Kingdom, Morocco, Ireland, France, Italy, Japan, Canada, Spain, Switzerland, New Zealand, India, Hong Kong, Sao Tome and Principe, Sweden, Netherlands, Australia, Belgium, Austria
PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.
2
Trizol reagent by Thermo Fisher Scientific
Sourced in United States, China, Japan, Germany, United Kingdom, Canada, France, Italy, Australia, Spain, Switzerland, Netherlands, Belgium, Lithuania, Denmark, Singapore, New Zealand, India, Brazil, Argentina, Sweden, Norway, Austria, Poland, Finland, Israel, Hong Kong, Cameroon, Sao Tome and Principe, Macao, Taiwan, Province of China, Thailand
TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
3
Protein calibration standard 1 by Bruker
Sourced in Germany, France, United States
The Protein Calibration Standard I is a laboratory equipment product designed to provide a set of well-characterized proteins for calibrating and validating protein analysis instruments. The standard includes a mixture of purified proteins with known molecular weights, allowing users to assess the performance of their analytical equipment.
4
β actin by Merck Group
Sourced in United States, United Kingdom, Germany, China, Canada, Japan, Macao, Italy, Sao Tome and Principe, Israel, Spain, Denmark, France, Finland, Australia, Morocco, Ireland, Czechia, Sweden, Uruguay, Switzerland, Netherlands, Senegal
β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.
5
Protease inhibitor cocktail by Merck Group
Sourced in United States, Germany, China, United Kingdom, Italy, Japan, Sao Tome and Principe, France, Canada, Macao, Switzerland, Spain, Australia, Israel, Hungary, Ireland, Denmark, Brazil, Poland, India, Mexico, Senegal, Netherlands, Singapore
The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.
6
Fetal bovine serum (fbs) by Thermo Fisher Scientific
Sourced in United States, China, United Kingdom, Germany, Australia, Japan, Canada, Italy, France, Switzerland, New Zealand, Brazil, Belgium, India, Spain, Israel, Austria, Poland, Ireland, Sweden, Macao, Netherlands, Denmark, Cameroon, Singapore, Portugal, Argentina, Holy See (Vatican City State), Morocco, Uruguay, Mexico, Thailand, Sao Tome and Principe, Hungary, Panama, Hong Kong, Norway, United Arab Emirates, Czechia, Russian Federation, Chile, Moldova, Republic of, Gabon, Palestine, State of, Saudi Arabia, Senegal
Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
7
β actin by Cell Signaling Technology
Sourced in United States, United Kingdom, China, Germany, Japan, Canada, Morocco, Sweden, Netherlands, Switzerland, Italy, Belgium, Australia, France, India, Ireland
β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is an important component of the microfilament system and is involved in various cellular processes such as cell motility, structure, and integrity.
8
Synapsin 1 by Abcam
Sourced in United Kingdom, United States
Synapsin-1 is a neuronal phosphoprotein that plays a crucial role in the regulation of neurotransmitter release and synaptic vesicle trafficking. It is a key component of the presynaptic machinery and is involved in the anchoring and clustering of synaptic vesicles at the active zones of synapses.
9
Psd95 by Cell Signaling Technology
Sourced in United States, Israel, United Kingdom
PSD95 is a protein that functions as a scaffold in the postsynaptic density of neuronal synapses. It plays a role in the organization and clustering of neurotransmitter receptors, ion channels, and signaling molecules at the postsynaptic membrane.
10
Rneasy mini kit by Qiagen
Sourced in Germany, United States, United Kingdom, Netherlands, Spain, Japan, Canada, France, China, Australia, Italy, Switzerland, Sweden, Belgium, Denmark, India, Jamaica, Singapore, Poland, Lithuania, Brazil, New Zealand, Austria, Hong Kong, Portugal, Romania, Cameroon, Norway
The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.

More about "Synapsin I"

Synapsin I, also known as Synapsin-1, is a crucial member of the synapsin family of phosphoproteins.
These proteins play a vital role in the regulation of neurotransmitter release and the proper functioning of the central nervous system.
Synapsin I is involved in the tethering of synaptic vesicles to the actin cytoskeleton, as well as the modulation of neurotransmitter release.
Researchers can utilize various techniques and materials to study Synapsin I, such as PVDF membranes, TRIzol reagent, and Protein Calibration Standard I.
These tools can be employed to analyze the expression and function of Synapsin I in neuronal cells.
Additionally, the measurement of the β-actin protein, a common housekeeping gene, can provide valuable insights into the overall cellular activity.
The use of Protease inhibitor cocktail and FBS (Fetal Bovine Serum) can also be beneficial in maintaining the integrity and stability of Synapsin I during experimentation.
Researchers may also leverage the RNeasy Mini Kit to extract and purify RNA, which can be used to study the gene expression of Synapsin I.
Furthermore, Synapsin I is closely associated with other key neuronal proteins, such as PSD95, which play a critical role in the structure and function of synapses.
Understanding the interplay between Synapsin I and these related proteins can provide valuable insights into the complex mechanisms underlying neurological processes and disorders.
By utilizing the insights gained from the MeSH term description and the Metadescription, researchers can streamline their Synapsin I optimization process, leveraging the PubCompare.ai platform to locate the best protocols from literature, preprints, and patents, and enhance the reproducibility and accuracy of their research.
This powerful tool can help take the guesswork out of Synapsin I research, allowing for more efficient and effective investigations.