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Serine

Serine is a non-essential amino acid that plays a crucial role in various biological processes.
It is involved in the synthesis of proteins, lipids, and other important molecules, and also serves as a precursor for the formation of other amino acids.
Serine is found in a wide range of foods, including meat, fish, dairy products, and legumes.
It is also produced naturally in the body through the metabolism of other amino acids.
Serine has been studied for its potential health benefits, including its role in supporting cognitive function, immune system health, and cardiovascular health.
However, more research is needed to fully understand the impacts of serine supplementation.
Experiene the future of scientific research today with PubCompare.ai, an innovative platform that can enhance your serine research accuracy and reproducibility.

Most cited protocols related to «Serine»

1
Automated HDX-WB Peptide Detection
Cited 90 times
As in previous solutions [6 (link), 8 (link)–10 , 18 (link)], the software attempts to determine the correct RT range for each peptide automatically. The input retention times are provided in the peptide set, presented in the downstream interface, and used to define RT range in the event that the peptide is not found within the specified limits of the detection algorithm (e.g., signal intensity, ppm, and fit score). The HDX-WB peptide isotope detection algorithm follows a similar approach to HD Desktop, in which the theoretical distribution for the peptide is initially calculated with Qmass [29 (link), 30 (link)], and is then compared with the experimental spectra with a least squares regression. For this version of software, we precalculate and save all possible theoretical distributions for a given peptide, and then compare them with the experimental data from individual scans. Because we now exclusively acquire data with high resolution FT-MS instruments (Orbitrap), we no longer require a co-add moving window approach as described in HD Desktop. Filters are then applied such as mass accuracy, m/z range, retention time range, and intensity to define the best matched %D value. This approach of indexing all possible theoretical distributions for each scan increases the speed of peptide detection without compromising accuracy.
In cases where MS/MS-based peptide identification is unavailable or limited in sequence coverage, HDX-WB provides the ability to extract all possible peptides from the protein sequence in place of a predetermined input peptide list. This operates in a manner similar to Hexicon [5 (link)]. To account for low enzymatic specificity, the software determines all possible combinations of peptide sequences between user defined residues in length and runs them through the detect algorithm however cleavage after H, K, P, and R may be eliminated from consideration based upon the Hamuro rules of pepsin specificity [31 (link)]. This has been shown to be a reasonable approach with novel or common enzymes used in HDX, such as pepsin or Fungal XIII, albeit somewhat more computationally expensive. The input list of peptides is not a requirement if this option is used and the approach has been shown to provide increased sequence coverage [5 (link)]. However, care should be taken when using this approach, as no product ion information is considered in the peptide identification.
An important consideration when searching MS1 data from predefined peptide sets is the detection of mass conflicts, in which a putative peptide can share the same or nearly the same mass with one, or many, other peptides within the peptide set. The software defines a mass conflict as two or more peptides within the peptide set whose theoretical monoisotopic mass is less than or equal to the error tolerance designated in the experiment set up. A mass conflict will indicate potential false positives from the detection process, as peptides with the same elemental composition will result in the same isotopic distribution and mass. HDX-WB provides the ability to automatically detect and flag peptides with mass conflicts within a user’s dataset, and allow the user to validate them manually.
HDX-WB is able to detect the potential presence of modifications from raw data; however, site localization is not possible because it is MS1 raw data being interrogated. For example, a search for one serine phosphorylation site on the peptide LULSSTVK would need to consider the forms LULpSSTVK and LULSpSTVK. Both of these are comprised of the same elemental composition and, as a result, the MS1 spectra are identical. The configuration of the available modifications within HDX-WB is made available in an external file allowing users to customize them as needed. These installed modifications are subsequently made available via the detection interface. Modifications may also be added directly into the peptide set if the site is well characterized. The software additionally provides support for detection of point mutations.
Pascal B.D., Willis S., Lauer J.L., Landgraf R.R., West G.M., Marciano D., Novick S., Goswami D., Chalmers M.J, & Griffin P.R. (2012). HDX Workbench: Software for the Analysis of H/D Exchange MS Data. Journal of the American Society for Mass Spectrometry, 23(9), 10.1007/s13361-012-0419-6.
Publication 2012
Amino Acid Sequence Cytokinesis Enzymes FLAG peptide Immune Tolerance Isotopes Pepsin A Peptides Phosphorylation Point Mutation Radionuclide Imaging Retention (Psychology) Serine Tandem Mass Spectrometry
2
Negative Selection RNAi Screening in Solid Tumors
Cited 78 times
To undertake negative selection RNAi screening in solid tumours, pools of MCF10DCIS.com cells expressing an shRNA library were injected into the 4th mammary fat pad of immunocompromised mice and allowed to form tumours. Abundances of shRNAs in the tumours was determined using massively parallel sequencing and compared to shRNA abundance in the injected cells. Genes targeted by shRNAs that were significantly depleted during tumour growth were considered hits and prioritized by analyzing gene copy number data from human tumours and cancer cell lines. Lentiviral shRNAs were used to suppress PHGDH expression in breast cancer cell lines with and without PHGDH genomic amplification. Serine synthesis pathway activity and anaplerosis were measured via flux analyses utilizing isotopically labeled molecules.
Possemato R., Marks K.M., Shaul Y.D., Pacold M.E., Kim D., Birsoy K., Sethumadhavan S., Woo H.K., Jang H.G., Jha A.K., Chen W.W., Barrett F.G., Stransky N., Tsun Z.Y., Cowley G.S., Barretina J., Kalaany N.Y., Hsu P.P., Ottina K., Chan A.M., Yuan B., Garraway L.A., Root D.E., Mino-Kenudson M., Brachtel E.F., Driggers E.M, & Sabatini D.M. (2011). Functional genomics reveals serine synthesis is essential in PHGDH-amplified breast cancer. Nature, 476(7360), 346-350.
Publication 2011
Biosynthetic Pathways Breast cDNA Library Cell Lines Cells Genes Genome Homo sapiens Malignant Neoplasms MCF-7 Cells Mus Neoplasms Pad, Fat RNA Interference Serine Short Hairpin RNA
3
Negative Selection RNAi Screening in Solid Tumors
Cited 74 times
To undertake negative selection RNAi screening in solid tumours, pools of MCF10DCIS.com cells expressing an shRNA library were injected into the 4th mammary fat pad of immunocompromised mice and allowed to form tumours. Abundances of shRNAs in the tumours was determined using massively parallel sequencing and compared to shRNA abundance in the injected cells. Genes targeted by shRNAs that were significantly depleted during tumour growth were considered hits and prioritized by analyzing gene copy number data from human tumours and cancer cell lines. Lentiviral shRNAs were used to suppress PHGDH expression in breast cancer cell lines with and without PHGDH genomic amplification. Serine synthesis pathway activity and anaplerosis were measured via flux analyses utilizing isotopically labeled molecules.
Possemato R., Marks K.M., Shaul Y.D., Pacold M.E., Kim D., Birsoy K., Sethumadhavan S., Woo H.K., Jang H.G., Jha A.K., Chen W.W., Barrett F.G., Stransky N., Tsun Z.Y., Cowley G.S., Barretina J., Kalaany N.Y., Hsu P.P., Ottina K., Chan A.M., Yuan B., Garraway L.A., Root D.E., Mino-Kenudson M., Brachtel E.F., Driggers E.M, & Sabatini D.M. (2011). Functional genomics reveals serine synthesis is essential in PHGDH-amplified breast cancer. Nature, 476(7360), 346-350.
Publication 2011
Biosynthetic Pathways Breast cDNA Library Cell Lines Cells Genes Genome Homo sapiens Malignant Neoplasms MCF-7 Cells Mus Neoplasms Pad, Fat RNA Interference Serine Short Hairpin RNA
4
Applying BioBERT to Biomedical Text Mining
Cited 67 times
With minimal architectural modification, BioBERT can be applied to various downstream text mining tasks. We fine-tune BioBERT on the following three representative biomedical text mining tasks: NER, RE and QA.
Named entity recognition is one of the most fundamental biomedical text mining tasks, which involves recognizing numerous domain-specific proper nouns in a biomedical corpus. While most previous works were built upon different combinations of LSTMs and CRFs (Giorgi and Bader, 2018 (link); Habibi et al., 2017 (link); Wang et al., 2018 ), BERT has a simple architecture based on bidirectional transformers. BERT uses a single output layer based on the representations from its last layer to compute only token level BIO2 probabilities. Note that while previous works in biomedical NER often used word embeddings trained on PubMed or PMC corpora (Habibi et al., 2017 (link); Yoon et al., 2019 (link)), BioBERT directly learns WordPiece embeddings during pre-training and fine-tuning. For the evaluation metrics of NER, we used entity level precision, recall and F1 score.
Relation extraction is a task of classifying relations of named entities in a biomedical corpus. We utilized the sentence classifier of the original version of BERT, which uses a [CLS] token for the classification of relations. Sentence classification is performed using a single output layer based on a [CLS] token representation from BERT. We anonymized target named entities in a sentence using pre-defined tags such as @GENE$ or @DISEASE$. For instance, a sentence with two target entities (gene and disease in this case) is represented as “Serine at position 986 of @GENE$ may be an independent genetic predictor of angiographic @DISEASE$.” The precision, recall and F1 scores on the RE task are reported.
Question answering is a task of answering questions posed in natural language given related passages. To fine-tune BioBERT for QA, we used the same BERT architecture used for SQuAD (Rajpurkar et al., 2016 ). We used the BioASQ factoid datasets because their format is similar to that of SQuAD. Token level probabilities for the start/end location of answer phrases are computed using a single output layer. However, we observed that about 30% of the BioASQ factoid questions were unanswerable in an extractive QA setting as the exact answers did not appear in the given passages. Like Wiese et al. (2017) , we excluded the samples with unanswerable questions from the training sets. Also, we used the same pre-training process of Wiese et al. (2017) , which uses SQuAD, and it largely improved the performance of both BERT and BioBERT. We used the following evaluation metrics from BioASQ: strict accuracy, lenient accuracy and mean reciprocal rank.
Lee J., Yoon W., Kim S., Kim D., Kim S., So C.H, & Kang J. (2019). BioBERT: a pre-trained biomedical language representation model for biomedical text mining. Bioinformatics, 36(4), 1234-1240.
Full text: Click here
Publication 2019
Angiography Gene Order Genes Hereditary Diseases Mental Recall Serine
5
Engineered ArnA Mutations Optimize Protein Expression
Cited 61 times
Wild type arnA was PCR amplified from E. coli genomic DNA with NdeI and XhoI restriction site overhangs on the 5’ and 3’ ends, respectively, using primers 1F and 1R (See all primer details in Table S1), and cloned into the bacterial expression vector pColaDuet (EMD Millipore). Two serine point mutations were introduced at site 1 (H359S and H361S) using primers 2F and 2R. Two additional serine point mutations were introduced at site 2 (H592S and H593S) using primers 3F and 3R to generate the final arnA mutant containing a total of four histidine to serine mutations.
The arnA knockout strain was generated with the E. coli recombineering technique10 (link), using the pKD4 plasmid as a template for the selectable marker and BL21(DE3) as the parental strain. The forward and reverse primers, 4F and 4R, were designed to maintain the reading frame of arnB, which shares its start codon with the stop codon of arnA within the arn operon11 (link) (also called pmrHFIJKLM operon12 (link)). A slightly modified scheme was used to introduce the arnA mutant back into the arnA knockout strain at the original locus (Fig. S1). First, mutant arnA was amplified and combined with the amplified selectable marker in a second PCR step. The resulting PCR product containing mutated arnA and the selectable marker was transformed into the arnA knockout strain for recombination using the λ Red recombinase plasmid (pKD46). The selectable marker was eliminated using the FLP plasmid (pCP20). For the modification in slyD, the arnA mutant strain was transformed with a PCR product (generated using primers 5F and 5R) containing a selectable marker flanked by homologous overhangs that, after recombination, result in the elimination of the 46-residue C-terminal, histidine-rich segment of SlyD. Again, the selectable marker was later removed using pCP20. Proper genomic integration was confirmed by PCR and sequencing. The RIL plasmid (Agilent Technologies) encoding rare tRNAs was transformed into the final expression strain to improve the expression of our eukaryotic target proteins.
The binding affinity of wild type and mutant ArnA were assessed by immobilizing purified protein onto a 1 ml His-Trap FF column (GE Healthcare) equilibrated in 50 mM potassium phosphate pH 8.0, 300 mM NaCl, and 5 mM beta-mercaptoethanol. Protein was eluted with a linear gradient of 0–150 mM imidazole. The imidazole concentration at the elution peak of each protein was recorded and compared.
Growth analysis was performed at 18, 25 and 37°C for both LOBSTR and the BL21(DE3) strains carrying the same test expression plasmid (See table S2 for a list of all test constructs). Cultures of 1L were grown in LB medium supplemented with 0.4% (w/v) glucose and antibiotic selection at 37°C to OD600 ~0.7. Protein expression was induced with 0.2 mM IPTG 20 minutes after the cultures were shifted to the desired expression temperature. OD600 was measured from the initial synchronization time and until the cells were harvested ~20–22 hours after induction.
To test protein purification, BL21(DE3) and LOBSTR cultures were started at 37°C in LB medium supplemented with 0.4% (w/v) glucose and appropriate antibiotic selection. At OD600 ~0.7, cultures were shifted to 18°C and induced with 0.2 mM IPTG ~20 min later. Cultures were harvested after 18–20 hours. For each strain and construct tested, a total of ~3.5g of cells were resuspended in 50 mL of resuspension buffer (40 mM potassium phosphate pH 8.0, 150 mM NaCl, 40 mM imidazole, and 3mM beta-mercaptoethanol) and lysed with a cell disrupter (Constant Systems). Lysates were cleared for 25 min at 9500×g and the soluble fraction was incubated with 400 µl bed volume of Ni Sepharose 6 Fast Flow (GE Healthcare) resin for 1 hour while stirring at 4°C. The resin was collected and washed with 6 mL of resuspension buffer and eluted with 2 mL of elution buffer (40 mM potassium phosphate pH 8.0, 150 mM NaCl, 250 mM imidazole, and 3 mM beta-mercaptoethanol). Elution fractions were analyzed on a 4–15 % SDS-PAGE gradient gel (Bio-RAD) and stained with Coomassie Blue R250. Purifications using Ni-NTA (Qiagen) and Talon (Clontech) resins were performed using resuspension buffer containing 20 mM or 5 mM imidazole, respectively, following manufacturer’s recommendations.
Andersen K.R., Leksa N.C, & Schwartz T.U. (2013). Optimized E. coli expression strain LOBSTR eliminates common contaminants from His-tag purification. Proteins, 81(11), 1857-1861.
Publication 2013
2-Mercaptoethanol Antibiotics Autosomal Recessive Polycystic Kidney Disease Bacteria Buffers Cells Claw Cloning Vectors Codon, Initiator Coomassie blue Escherichia coli Eukaryotic Cells Genome Glucose Histidine imidazole Isopropyl Thiogalactoside Mutation Oligonucleotide Primers Parent Plasmids Point Mutation potassium phosphate Proteins Protein Targeting, Cellular Reading Frames Recombinase Recombination, Genetic Resins, Plant SDS-PAGE Sepharose Serine Sodium Chloride Strains Transfer RNA

Most recents protocols related to «Serine»

1
Selectivity of FAAH Inhibitors Against Serine Hydrolases
Not available on PMC !

Example 39

Generally, pharmacophores for FAAH inhibitors, urea and non-urea based, interact by either carbamoylating or forming transition-state mimics with the catalytic serine residue. However, since a large number of hydrolases utilize a similar catalytic serine residue, many FAAH inhibitors have suffered from poor selectivity. Therefore, the potency of t-TUCB, A-14 and A-21 on several other serine hydrolases was tested. Included in this panel were carboxylesterases, hydrolases involved in xenobiotic detoxification, and paraoxonases and esterases involved in the regulation of arterosclerosis. As is shown in Table 5 below, none of these serine hydrolases were inhibited by t-TUCB, A-14, or A-21.

TABLE 5
Selectivity of A-14 and A-15 against other serine hydrolases.
IC50 (nM)
Enzyme1728A-14A-21
FAAH14024120
sEH0.832
MAGL>10,000>10,000>10,000
hCE1>10,000>10,000>10,000
hCE2>10,000>10,000>10,000
PON1>10,000>10,000>10,000
PON2>10,000>10,000>10,000
PON3>10,000>10,000>10,000
AADAC>10,000>10,0005,400

US11873288B2. Inhibitors for soluble epoxide hydrolase (sEH) and fatty acid amide hydrolase (FAAH) (2024-01-16). The Regents of the University of California [US]. Inventors: Bruce Hammock [US], Sean Kodani [US].
Full text: Click here
Patent 2024
Aryldialkylphosphatase Carboxylic Ester Hydrolases Catalysis Enzymes Esterases Genetic Selection Hydrolase inhibitors Metabolic Detoxication, Drug PON1 protein, human PON2 protein, human Serine Urea Xenobiotics
2
Preparation of Fluorescent Lipid Bilayers
Stock solutions (1–10 mg/mL)
of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
(POPC), 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-l-serine (POPS, Avanti Polar Lipids, Alabaster, AL, USA), and
ATTO 390-1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine
(Atto 390-DPPE, ATTO-TEC, Siegen, Germany) were prepared in chloroform. l-α-Phosphatidylinositol-4,5-bisphosphate (PtdIns[4,5]P2, brain porcine, Avanti Polar Lipids, Alabaster, AL, USA)
was freshly dissolved in chloroform/methanol/H2O (10:20:8)
to a final concentration of 1 mg/mL. Lipid mixtures (0.4 mg) were
prepared in chloroform/methanol (10:1), and organic solvents were
evaporated with a nitrogen stream followed by 3 h in vacuum. The dried
lipid films were stored at 4 °C until needed.
Small unilamellar
vesicles (SUVs) were prepared by rehydrating a lipid film in spreading
buffer (50 mM KCl, 20 mM Na-citrate, 0.1 mM NaN3, 0.1 mM
ethylenediaminetetraacetic acid (EDTA), pH 4.8),38 (link) incubating for 30 min, subsequent vortexing (3 × 30
s at 5 min intervals), and a final sonification step for 30 min at
room temperature (cycle 4, 60%, Sonopuls HD2070, resonator cup; Bandelin,
Berlin, Germany). PtdIns[4,5]P2 containing SUVs were used
immediately for the preparation of SLBs to avoid PtdIns[4,5]P2 degradation.65 (link)
Liebe N.L., Mey I., Vuong L., Shikho F., Geil B., Janshoff A, & Steinem C. (2023). Bioinspired Membrane Interfaces: Controlling Actomyosin Architecture and Contractility. ACS Applied Materials & Interfaces, 15(9), 11586-11598.
Full text: Click here
Publication 2023
1-palmitoyl-2-oleoylphosphatidylcholine Acids Alabaster bis(diphenylphosphine)ethane Brain Chloroform Citrates Edetic Acid Lipid A Lipids Methanol Nitrogen Phosphatidylethanolamines Phosphatidylinositols Pigs Serine Sodium Azide Solvents Vacuum
3
HPLC-ESI-MS/MS Proteomic Analysis of Mouse
HPLC-ESI-MS/MS was performed in positive ion mode on a Thermo Fisher Scientific Orbitrap Fusion Lumos tribrid mass spectrometer fitted with an EASY-Spray Source as previously described (Parker et al., 2019 (link)). NanoLC was performed using a Thermo Fisher Scientific UltiMate 3000 RSLCnano System with an EASY Spray C18 LC column (Thermo Fisher Scientific, 50 cm × 75 μm inner diameter, packed with PepMap RSLC C18 material, 2 μm, cat. # ES803); loading phase for 15 min; mobile phase, linear gradient of 1–47% ACN in 0.1% FA for 106 min, followed by a step to 95% ACN in 0.1% FA over 5 min, hold 10 min, and then a step to 1% ACN in 0.1% FA over 1 min and a final hold for 19 min (total run 156 min); Buffer A = 100% H2O in 0.1% FA; Buffer B = 80% ACN in 0.1% FA; flow rate, 250–300 nl/min. All solvents were liquid chromatography mass spectrometry grade. Spectra were acquired using XCalibur, version 2.1.0 (Thermo Fisher Scientific). A “top 15” data-dependent MS/MS analysis was performed (acquisition of a full scan spectrum followed by collision-induced dissociation mass spectra of the 15 most abundant ions in the survey scan). Dynamic exclusion was enabled with a repeat count of 1, a repeat duration of 30 s, an exclusion list size of 500, and an exclusion duration of 40 s. Tandem mass spectra were extracted from Xcalibur ‘RAW’ files and charge states were assigned using the ProteoWizard 2.1.x msConvert script using the default parameters. The fragment mass spectra were searched against the 2016 Mus musculus SwissProt database (16838 entries) using Mascot (Matrix Science; version 2.4) using the default probability cut-off score. The search variables that were used were: 10 ppm mass tolerance for precursor ion masses and 0.5 Da for product ion masses; digestion with trypsin; a maximum of two missed tryptic cleavages; variable modifications of oxidation of methionine and phosphorylation of serine, threonine, and tyrosine. Cross-correlation of Mascot search results with X! Tandem was accomplished with Scaffold (version Scaffold_4.8.7; Proteome Software). Probability assessment of peptide assignments and protein identifications were made using Scaffold. Only peptides with ≥95% probability were considered.
Parker S.S., Ly K.T., Grant A.D., Sweetland J., Wang A.M., Parker J.D., Roman M.R., Saboda K., Roe D.J., Padi M., Wolgemuth C.W., Langlais P, & Mouneimne G. (2023). EVL and MIM/MTSS1 regulate actin cytoskeletal remodeling to promote dendritic filopodia in neurons. The Journal of Cell Biology, 222(5), e202106081.
Full text: Click here
Publication 2023
Buffers Cytokinesis Digestion High-Performance Liquid Chromatographies Immune Tolerance Liquid Chromatography Mass Spectrometry Methionine Mice, House Peptides Phosphorylation Proteins Proteome Radionuclide Imaging Serine Solvents Tandem Mass Spectrometry Threonine Trypsin Tyrosine
4
Enzyme Kinetics of CK2 in Tat and Morphine Exposure
An enzyme activity assay was performed to determine whether Tat and morphine exposure alters CK2 enzyme kinetics. CK2 activity was determined in cytoplasmic extracts using the CycLex CK2 activity kit (# CY-1170, MBL Life Science, CycLex Co. Ltd, Nagano, Japan) per the manufacturer's instructions and previous publications (Jung et al., 2014 (link); Lee et al., 2014 (link); Oinuma et al., 2010 (link)). Briefly, 5 µg samples obtained from lysates of cells co-treated with Tat and morphine, or vehicle-treated control striatal neurons (receiving no experimental treatments) were incubated in wells pre-coated with a synthetic CK2-specific peptide with a serine 46 moiety that can be phosphorylated by CK2. A peroxidase-coupled monoclonal antibody was used to selectively detect phosphorylation of the serine 46 moiety of CK2 via the conversion of tetramethylbenzidine (TMB) to a chromogenic reaction product. The TMB reaction product was read at an absorbance of 450 nm on a PHERAstar FS plate reader (BMG LabTech; Cary, NC). For this study, reaction/incubation times used were 0 min, 20 min, and 40 min. Due to the unavailability of a CK1 enzyme activity kit and since CK1 levels were not changed in HIV- or Tat-exposed tissues in the present study, further evaluation of CK1 activity did not seem warranted.
Ohene-Nyako M., Nass S.R., Richard H.T., Lukande R., Nicol M.R., McRae M., Knapp P.E, & Hauser K.F. (2023). Casein Kinase 2 Mediates HIV- and Opioid-Induced Pathologic Phosphorylation of TAR DNA Binding Protein 43 in the Basal Ganglia. ASN NEURO, 15, 17590914231158218.
Publication 2023
3,3',5,5'-tetramethylbenzidine azo rubin S Cells Cytoplasm enzyme activity Enzyme Assays Enzymes Kinetics Monoclonal Antibodies Morphine Neurons Peptides Peroxidase Phosphorylation Serine Striatum, Corpus Therapies, Investigational Tissues
5
Artificial Saliva Preparation and Matrix Interactions

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Publication 2023
Alanine Albumins Ammonia Amylase Ascorbic Acid Aspartic Acid Biological Assay Buffers Calcium chloride Cysteine Glutamic Acid Glycine Histidine Homo sapiens Isoleucine Leucine Lysine Magnesium Chloride Methionine Phenylalanine Potassium Chloride potassium phosphate, monobasic Proline Rivers Saliva, Artificial Serine Serum Sodium Chloride sodium phosphate, monobasic Technique, Dilution tecogalan sodium Threonine Tryptophan Tyrosine Urea Valine

Top products related to «Serine»

1
L serine by Merck Group
Sourced in United States, Germany, Italy, United Kingdom, China, Canada
L-serine is a naturally occurring amino acid that serves as a building block for proteins. It is a colorless, crystalline solid that is soluble in water and alcohol. L-serine is commonly used in various laboratory applications, including cell culture media, biochemical assays, and as a reagent in analytical procedures.
2
Proteome discoverer by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, Austria, China
Proteome Discoverer is a software solution for the analysis of mass spectrometry-based proteomic data. It provides a comprehensive platform for the identification, quantification, and characterization of proteins from complex biological samples.
3
Serine by Merck Group
Sourced in United States, Germany, Spain, Sao Tome and Principe
Serine is a laboratory equipment product used for measuring and analyzing various biological and chemical samples. It is a versatile instrument that serves as a key tool in many research and testing applications.
4
Glycine by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, India, France, Canada, China, Sao Tome and Principe, Spain, Belgium, Macao, Ireland, Australia, Poland
Glycine is a colorless, crystalline amino acid that is used as a raw material in the production of various pharmaceutical and chemical products. It serves as a key component in buffer solutions and is commonly employed in the preparation of cell culture media and various biological assays.
5
1 palmitoyl 2 oleoyl sn glycero 3 phosphocholine by Avanti Polar Lipids
Sourced in United States
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine is a phospholipid consisting of a glycerol backbone with a palmitic acid and an oleic acid esterified to the first and second carbons, respectively, and a phosphocholine group attached to the third carbon. This compound is a commonly used lipid in various biochemical and biophysical applications.
6
1 2 dioleoyl sn glycero 3 phosphocholine by Avanti Polar Lipids
Sourced in United States
1,2-dioleoyl-sn-glycero-3-phosphocholine is a synthetic lipid compound. It is a phospholipid that consists of two oleic acid chains attached to a glycerol backbone, with a phosphocholine headgroup.
7
1 2 dioleoyl sn glycero 3 phospho l serine by Avanti Polar Lipids
Sourced in United States
1,2-dioleoyl-sn-glycero-3-phospho-L-serine is a phospholipid compound used in research applications. It is a synthetic version of the naturally occurring phospholipid phosphatidylserine. The compound consists of a glycerol backbone with two oleic acid chains and a serine head group.
8
1 palmitoyl 2 oleoyl sn glycero 3 phospho l serine by Avanti Polar Lipids
Sourced in United States
1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine is a phospholipid compound that can be used in various laboratory applications. It is a synthetic analog of the naturally occurring phospholipid, phosphatidylserine, which is a key component of biological membranes.
9
D serine by Merck Group
Sourced in United States, United Kingdom
D-serine is a biochemical product used in laboratory research. It is a naturally occurring amino acid that functions as a co-agonist at the glycine binding site of the N-methyl-D-aspartate (NMDA) receptor. This product is intended for use in scientific research applications.
10
Lipofectamine 2000 by Thermo Fisher Scientific
Sourced in United States, China, Germany, United Kingdom, Canada, Japan, France, Italy, Switzerland, Australia, Spain, Belgium, Denmark, Singapore, India, Netherlands, Sweden, New Zealand, Portugal, Poland, Israel, Lithuania, Hong Kong, Argentina, Ireland, Austria, Czechia, Cameroon, Taiwan, Province of China, Morocco
Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.

More about "Serine"

Serine, a non-essential amino acid, plays a vital role in numerous biological processes.
It is involved in the synthesis of proteins, lipids, and other essential molecules, serving as a precursor for the formation of other amino acids like glycine.
Serine can be found in a wide range of food sources, including meat, fish, dairy products, and legumes, and is also produced naturally in the body through the metabolism of other amino acids.
Experieneing the benefits of serine, research has suggested its potential role in supporting cognitive function, immune system health, and cardiovascular well-being.
However, more comprehensive studies are needed to fully understand the impacts of serine supplementation.
L-serine, the naturally occurring form of serine, is commonly utilized in scientific research and various applications.
Proteome Discoverer, a software tool, can assist in the identification and quantification of serine-containing proteins, contributing to a deeper understanding of serine's physiological functions.
Beyond serine, related compounds such as 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, 1,2-dioleoyl-sn-glycero-3-phosphocholine, 1,2-dioleoyl-sn-glycero-3-phospho-L-serine, and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine have been studied for their potential roles in cellular processes and signaling pathways.
Furthremore, D-serine, the stereoisomer of serine, has been investigated for its involvement in neurotransmission and its potential therapeutic applications.
Lipofectamine 2000, a transfection reagent, has been utilized in research to facilitate the delivery of genetic material, including serine-related compounds, into cells, enabling the exploration of their functional roles.
Experiene the future of scientific research today with PubCompare.ai, an innovative platform that can enhance your serine research accuracy and reproducibility by effortlessly locating the best protocols from literature, pre-prints, and patents, optimizing your research with intelligent comparisons.