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Phosphoserine

Phosphoserine is an amino acid derivative that plays a crucial role in cellular signaling and regulation.
It is formed by the addition of a phosphate group to the amino acid serine, creating a phosphorylated form.
Phosphoserine is involved in a variety of biological processes, including protein structure, enzyme activity, and signal transduction.
It serves as a important post-translantional modification that can alter the function and localization of target proteins.
Researchers utilize phosphoserine in a range of applications, such as studying cell signaling pathways, investigating protein-protein interactions, and developing therapeutic interventions.
Optimizing phosphoserine research can be facilitated by AI-driven platforms like PubCompare.ai, which help identify the best protocols and products to enhance the reliability and reproducibility of phosphoserine experiments.

Most cited protocols related to «Phosphoserine»

For overexpression of GST-CaM incorporating phosphoserine, DH10B ΔserB or C321(DE3) ΔserB E. coli cells were transformed by electroporation with pRSF and pKW vectors, and recovered in 1 ml SOB medium for one hour at 37°C prior to aliquoting to 100 ml LB-KC (LB media with 25 μg/ml kanamycin, and 17.5 μg/ml chloramphenicol) and incubated overnight (37°C, 250 r.p.m., 16 h). The overnight culture was diluted to OD600=0.1 in LB-KC. At OD600=0.5, IPTG (1 mM final concentration) and phosphoserine (2 mM) were added to the culture. The culture was incubated (37°C, 250 r.p.m.) for 5 h, pelleted (3,000g, 10 min, 4°C) and washed twice with 1 ml PBS. The overexpressed proteins were purified using the glutathione affinity chromatography. Cell pellets were resuspended in 1 ml of BugBuster Protein Extraction Reagent (Novagen) (supplemented with 1× protease inhibitor cocktail tablet (Roche), 1 mg ml−1 lysozyme (Sigma), 1 mg ml−1 DNase I (Sigma)) and lysed (25°C, 250 r.p.m., 1 h). The lysate was clarified by centrifugation (25,000g, 30 min, 4°C). GST containing proteins from the lysate were bound in batch (1 h, 4°C) to 70 μl of glutathione sepharose beads (GE Healthcare). Beads were washed 4 times with 1 ml PBS prior to elution by heating in 1× NuPAGE LDS sample buffer (Invitrogen, 95°C, 5 min) supplemented with 100 mM DTT. All samples were analysed on 4-12% Bis-Tris gels (Invitrogen) with BIO-RAD Low Range Molecular Weight Standard as marker. The gels were subsequently stained with Coomassie Blue (InstantBlue, Expedeon).
Publication 2015
Bistris Buffers Cells Centrifugation Chloramphenicol Chromatography, Affinity Cloning Vectors Coomassie blue Deoxyribonucleases Electroporation Escherichia coli Gels Glutathione Isopropyl Thiogalactoside Kanamycin LB-100 Muramidase Pellets, Drug Phosphoserine Proteins Sepharose SERPINA1 protein, human Tablet

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Publication 2010
Antibodies Antibodies, Blocking Biological Assay Biotin CD4 Positive T Lymphocytes CD44 protein, human Cells Chromatin Immunoprecipitation Sequencing DNA Chips Gene Chips Gene Expression Genes Genome Histone Code histone H3 trimethyl Lys4 Histones Interferon Type II isolation Microarray Analysis MicroRNAs Muromonab-CD3 Mus Oligonucleotide Primers Phosphoserine Ribosomal RNA SELL protein, human STAT3 Protein T-Lymphocyte TGFB2 protein, human

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Publication 2011
Chromatin Immunoprecipitation Sequencing DNA Chips Immune Sera MECP2 protein, human Phosphoserine Rabbits
All lipids were obtained from Avanti Polar Lipids, Inc. For t-SNARE reconstitution, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine (POPS), and cholesterol were mixed in a molar ratio of 60:20:10:10. For v-SNARE reconstitution, POPC, POPE, POPS, cholesterol, N-(7-nitro-2,1,3-benzoxadiazole-4-yl)-1,2-dipalmitoyl phosphatidylethanolamine (NBD-DPPE), and N-(Lissamine rhodamine B sulfonyl)-DPPE (rhodamine-DPPE) were mixed at a molar ratio of 60:17:10:10:1.5:1.5. SNARE proteoliposomes were prepared by detergent dilution and isolated on an Accudenz density gradient flotation (Weber et al., 1998 (link)). SNARE proteins were kept at physiologically relevant densities, with protein/lipid ratios at 1:200 for v-SNAREs (similar to VAMP2 densities reported for native synaptic vesicles; Jahn and Südhof, 1994 (link); Walch-Solimena et al., 1995 (link)) and at 1:500 for t-SNARE liposomes. Reconstituted liposomes were routinely monitored by dynamic light scattering and electron microscopy with negative staining.
Publication 2010
1,2-dipalmitoyl-3-phosphatidylethanolamine 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine-N-(7-nitro-2-1,3-benzoxadiazol-4-yl) 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine 1-palmitoyl-2-oleoylphosphatidylcholine bis(diphenylphosphine)ethane Cholesterol Detergents Electron Microscopy Lipids Liposomes lissamine rhodamine B Molar Phosphatidylethanolamines Phosphorylcholine Phosphoserine Proteins proteoliposomes Rhodamine SNAP Receptor Synaptic Vesicles Target Membrane SNARE Proteins Technique, Dilution Vesicle-Associated Membrane Protein 2 Vesicle SNARE Proteins
Farnesylated and non-farnesylated wild-type K-Ras4B1–185 proteins were previously constructed using a crystal structure (PDB code 3GFT) [40 (link),42 (link),43 (link)]. Ensembles of monomeric structure of GTP-bound K-Ras4B were extracted from the trajectories of K-Ras4B-GTP monomer simulations in solution [40 (link)]. These monomer conformations were used to construct the dimer structures of K-Ras4B-GTP. Four different types of K-Ras4B-GTP dimers based on earlier predictions for the K-Ras4B catalytic domain dimers [5 (link)] contain two allosteric lobe and two effector lobe dimer interfaces. For the GTP-bound H-Ras dimers, we followed the protocol of the K-Ras4B-GTP dimer simulations [40 (link),42 (link),43 (link)]. The crystal structure of H-Ras-GTP (PBD code 5P21) served as the catalytic domain structure. Preliminary simulations of H-Ras-GTP with the HVR containing the palmitoyl and farnesyl modifications generated ensembles of monomeric H-Ras structures in solution. Four H-Ras-GTP dimers with different dimer interfaces were also constructed on the basis of the predictions [5 (link)]. The initial configurations of both K-Ras4B-GTP and H-Ras-GTP dimers were subject to simulations in water and membrane environments. For the water simulations, the initially pre-assembled dimer configurations were solvated by the modified TIP3P water model [44 ] and gradually relaxed with the proteins held rigid. The unit cell box of 120 Å3 contains almost 180000 atoms, 30 Na+, 3 Mg2+ and 38 Cl for the K-Ras4B-GTP dimers and 40 Na+, 4 Mg2+ and 34 Cl for the H-Ras-GTP dimers. For the membrane simulations, the same initial configurations of both dimers for the water simulations were translated on to the surface of an anionic lipid bilayer containing DOPC (1,2-dioleoyl-sn-glycero-3-phosphocholine) and DOPS (1,2-dioleoyl-sn-glycero-3-phosphoserine) (molar ratio 4:1). In the initial construction of the bilayer system, no portion of the catalytic domain and the HVR including the farnesyl and palmitoyl groups was inserted into the lipid bilayer before the start of the simulations. Instead, the HVR backbone marginally touched the surface of the anionic bilayer at the starting points. The lipid bilayers were generated using the bilayer-building protocol involving the interactions of pseudospheres through the vdW (van der Waals) force field [34 (link),40 (link),45 (link)–51 (link)]. A unit cell containing a total of 400 lipids (320 DOPC and 80 DOPS) constitutes the bilayer with TIP3P waters, added at both sides with a lipid/water ratio of ∼1:122. The updated CHARMM [52 ] all-atom additive force field for lipids (C36) [53 (link)] was used to construct the set of starting points and to relax the systems to a production-ready stage. To neutralize the bilayer system and to also obtain a salt concentration near 100 mM, 80 Na+,8 Mg2+ and 18 Cl for the K-Ras4B-GTP dimer and 90 Na+,9 Mg2+ and 14 Cl for the H-Ras-GTP dimer were added to the bilayer systems.
A total of 3.2 μs simulations were performed for the 16 systems; each has 200 ns simulation with an integration step of 2 fs and with a constant temperature of 310 K. Our water simulations employed the NPT (constant number of atoms, pressure and temperature) ensemble. For the membrane simulations to 30 ns, we employed the NPAT (constant number of atoms, pressure, surface and temperature) ensemble with a constant normal pressure applied in the direction perpendicular to the membrane. In the production runs from 30 ns to 200 ns, the simulations employed the NPT ensemble. We used the NAMD parallel computing code [54 (link)] for the simulations on a Biowulf cluster at the NIH. Averages were taken after 30 ns, discarding initial transients trajectories, with the CHARMM programming package [52 ].
Publication 2016
1,2-oleoylphosphatidylcholine ARID1A protein, human Catalytic Domain Cells Droxidopa Glycerylphosphorylcholine K-ras Genes K 185 Lipid A Lipid Bilayers Lipids Molar Muscle Rigidity Phosphoserine Pressure Proteins Sodium Chloride Tissue, Membrane Transients Vertebral Column

Most recents protocols related to «Phosphoserine»

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Publication 2023
Antibodies Antibodies, Anti-Idiotypic Buffers Cells Centrifugation GAPDH protein, human Horseradish Peroxidase inhibitors MDM2 protein, human Milk, Cow's Mus Peptide Hydrolases Phosphoric Monoester Hydrolases Phosphoserine polyvinylidene fluoride Proteins Rabbits Radioimmunoprecipitation Assay RUNX2 protein, human SDS-PAGE Sodium Chloride Sulfate, Sodium Dodecyl Threonine Tissue, Membrane Tromethamine Tubulin Tween 20 Western Blotting
X. tropicalis embryos at St. 26–30 were fixed in 4% Paraformaldehyde for 3 h at RT except for Atp6v1a and Itln1 staining, which employed Dent’s Fix (4:1 Methanol:DMSO) for 3 h at −20 °C. After several washing steps, the samples were incubated in PPBSTB (0.1% Triton X-100, 2% BSA in PBS) for 1 h before the primary antibodies were added in a 1:300 dilution overnight at 4 °C (Rabbit monoclonal anti-LRP6, Cell Signaling Technology, Cat#2560; Mouse monoclonal anti-acetylated alpha tubulin, Sigma-Aldrich, Cat#T7451; Rabbit polyclonal anti-CCNY, homemade,14 (link); Rabbit monoclonal anti-GSK3α/β, Cell Signaling Technology, Cat# 5676; Rabbit polyclonal anti-Phospho-LRP6 (S1490), Cell Signaling Technology, Cat#2568S; Rabbit polyclonal anti-Phospho-LRP6 (T1479), homemade,36 (link); Mouse monoclonal anti-FLAG M2, Sigma Aldrich, Cat#F3165; Mouse monoclonal anti-Phosphoserine (Clone 4A4), Millipore, Cat#05-1000; Rabbit polyclonal anti-ATP6V1A, Abcam, Cat#ab137574; Rabbit monoclonal anti-Ubiquitin, Lys48-Specific, clone Apu2, Millipore, Cat#05-1307; Rabbit polyclonal anti-ITLN1, Proteintech, Cat#11770-1-AP; Rabbit monoclonal anti-Acetyl-α-Tubulin (Lys40), Cell Signaling Technology, Cat#5335T; Mouse monoclonal anti-TSG101 (4A10), Abcam, Cat#ab83). Secondary antibodies (Donkey polyclonal Anti-Mouse IgG, Alexa Fluor 647, Jackson ImmunoResearch, Cat#715-605-151; Donkey polyclonal Anti-Mouse IgG, Alexa Fluor 488, Jackson ImmunoResearch, Cat#715-545-150; Donkey polyclonal Anti-Rabbit IgG, Alexa Fluor 647, Jackson ImmunoResearch, Cat#711-605-152; Goat polyclonal Anti-Rabbit IgG, Alexa Fluor 488, Invitrogen, Cat#A11008) were diluted 1:500 in PBSTB and applied for 3 h at RT together with 1:1000 Phalloidin-iFluor 405 or −488 Reagent (Abcam; Cat#ab176752 and Cat#ab176753, respectively). Small embryo pockets were prepared by putting 2 layers of isoelectric tape on a glass slide and cutting rectangles with a scalpel. One embryo was mounted in each pocket.
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Publication 2023
alexa fluor 488 Alexa Fluor 647 alpha-Tubulin anti-IgG Antibodies CAT-152 Clone Cells Embryo Equus asinus GIT1 protein, human glycogen synthase kinase 3 alpha Goat LRP6 protein, human Methanol Mus paraform Phalloidine Phosphoserine Rabbits Sulfoxide, Dimethyl Technique, Dilution Triton X-100 TSG101 protein, human Ubiquitin
X. tropicalis embryos were harvested at indicated stages, homogenized in 20 µl per embryo of NOP + lysis buffer (20 mM Tris-HCl pH 7.5, 150 mM NaCl, 2% Triton X-100, 0.2% DTT, and cOmplete Protease Inhibitor Cocktail (Roche; Cat#11697498001)). Lysates were cleared with CFC-113 (Honeywell, 34874) and centrifugation (18,800 × g, 10 min at 4 °C). After boiling at 95 °C for 5 min with NuPAGE LDS Buffer (+50 mM DTT), 0.5–1 embryos per lane were loaded for SDS-PAGE analysis. X. tropicalis lysates and immunoprecipitation samples were separated on polyacrylamide gels, transferred to nitrocellulose and blocked with 5% skim-milk powder or 5% BSA in Tris-buffered saline with 0.1% Tween-20 (TBST) for 1 h at room temperature. Primary antibody was diluted 1:1000 in blocking 1% buffer and incubated overnight at 4 °C. Membranes were incubated with peroxidase-linked secondary antibodies diluted 1:5000 for 1 h at RT and then treated with Supersignal West Pico solution (Thermo Scientific; Cat#34580). Images were acquired on an LAS-3000 system (Fuji Film). Primary antibodies used for immunoblotting: Rabbit monoclonal anti-GAPDH, Cell Signaling Technology, Cat#2118S; Rabbit monoclonal anti-LRP6, Cell Signaling Technology, Cat#2560; Mouse monoclonal anti-acetylated alpha tubulin, Sigma-Aldrich, Cat#T7451; Mouse monoclonal anti-GSK3β, BD Biosciences, Cat#610201; Mouse monoclonal anti-FLAG M2, Sigma Aldrich, Cat#F3165; Mouse monoclonal anti-Phosphoserine (Clone 4A4), Millipore, Cat#05-1000; Mouse monoclonal anti-Phosphothreonine (Q7), Qiagen, Cat#37420. Secondary antibodies: Goat anti-mouse IgG (H + L) HRP, Jackson ImmunoResearch, Cat#115-035-146; Goat anti-rabbit IgG (H + L) HRP, Jackson ImmunoResearch, Cat#111-035-144 and Donkey anti-Goat IgG-HRP, Santa Cruz, Cat#sc-2020.
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Publication 2023
alpha-Tubulin anti-IgG Antibodies Cardiac Arrest Centrifugation CFC 113 Clone Cells Embryo Equus asinus GAPDH protein, human Goat GSK3B protein, human Immunoglobulins Immunoprecipitation LRP6 protein, human Milk, Cow's Mus Nitrocellulose Peroxidase Phosphoserine Phosphothreonine polyacrylamide gels Powder Protease Inhibitors Rabbits Saline Solution SDS-PAGE Sodium Chloride Tissue, Membrane Triton X-100 Tween 20
The PP2C and AC domain-coding sequences of BAC and BACS1407P were isolated from the wild-type and mutant strains and inserted into pET28a+ (Supplementary Figure S4) to produce the BAC-His6 PP2C-AC and BACS1407P-His6 PP2C-AC vectors, respectively. These vectors were transformed into Escherichia coli BL21 cells by a heat-shock method. Target proteins were produced by the addition of 1.5 mM isopropyl β-d-1-thiogalactopyranoside (IPTG) at 30°C. The BAC PP2C-AC domain and BACS1407P PP2C-AC domain were individually linked to six histamines (His6) and expressed as fusion proteins; eventually, the BAC-His6 PP2C-AC domain and BACS1407P-His6 PP2C-AC domain fusion proteins were produced and then purified using the Ni-NTA 6FF Sefinose (TM) Resin Kit (Shenggong, Shanghai, China).
For the gel retardation assay, the purified protein was run in SDS-PAGE or mixed with Phos-tag (FUJIFILM Wako Pure Chemical Corporation, Osaka, Japan) to examine the phosphorylation levels of different proteins following the reported method (Gou et al., 2015 (link)). In this assay, the phosphate group on the protein binds the Phos-tag with the manganese ion in the gel. Eventually, the relative mass of the protein becomes larger, and therefore, the mobility in the gel becomes slower. The variance of the position of the protein is representative of the phosphorylation levels between different proteins. The fusion proteins were specified by binding with anti-His6 and secondary antibody goat anti-mouse IgG HRP (AB-M-M100, GOOD HERE, Hangzhou, China) according to the manufacturer’s instructions. This binding was detected by the Western Blot test reagent dye solution (34,580, Thermo Scientific™, Shanghai, China), where the second antibody was bound to HRP, and the substrate of ECL produced chemiluminescence after being catalyzed by HRP.
For the total protein phosphorylation level test, the mycelia growth on cellophane-covered CM medium for 3 days under light or dark conditions, and the protein extraction buffer (Yang et al., 2013 (link)) was used to extract mycelia protein. The anti-phosphoserine antibody (ab9332, Abcam, United Kingdom) was used to analyze the total phosphorylation level.
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Publication 2023
1,3-bis(bis(pyridin-2-ylmethyl)amino)propan-2-ol anti-IgG Antibodies, Anti-Idiotypic Biological Assay Buffers Cellophane Cells Chemiluminescence Cloning Vectors Culture Media Escherichia coli Exons Gel Shift Analysis Goat Heat-Shock Response Histamine Histamine Antagonists Immunoglobulins Manganese Mus Mutant Proteins Mycelium Phosphates Phosphorylation Phosphoserine Proteins Proto-Oncogene Mas Range of Motion, Articular Resins, Plant SDS-PAGE Strains TNFSF14 protein, human Western Blot
Miltefosine (#850337) and most NBD-lipids were purchased from Avanti Polar Lipids (Alabaster, AL, USA), including 1-palmitoyl-2-{6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl}-sn-glycero-3-phosphocholine (NBD-PC; #810130), 1-palmitoyl-2-{6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl}-sn-glycero-3-phosphoethanol-amine (NBD-PE; #810153), 1-palmitoyl-2-{6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl}-sn-glycero-3-phosphoserine (ammonium salt) (NBD-PS; #810192), 1-palmitoyl-2-{6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl}-sn-glycero-3-[phospho-rac-(1-glycerol)] (ammonium salt) (NBD-PG; #810163), N-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sphingosine-1-phosphocholine (NBD-SM; #810218), N-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-D-galactosyl-β1-1′-sphingosine (NBD-GalCer; #810220), and N-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-D-glucosyl-β1-1′-sphingosine (NBD-GlcCer; #810222). N-[(1S,2R,3E)-1-[[(4-O-beta-D-galactopyranosyl-beta-D-glucopyranosyl)oxy]methyl]-2-hydroxy-3-heptadecen-1-yl]-hexadecanamide-d3 (NBD-LacCer, #Cay24625-1) was purchased from Biomol (Hamburg, Germany). The detergent n-dodecyl-β-D-maltopyranoside (DDM) was purchased from GlyconBiochemicals GmbH (Luckenwalde, Germany). Unless otherwise indicated, chemicals were obtained from Sigma-Aldrich (München, Germany). Protease inhibitor cocktail contained aprotinin (1 mg/mL), leupeptin (1 mg/mL), pepstatin A (1 mg/mL; Roth), antipain (5 mg/mL), and benzamidine (0.157 mg/mL) in dimethylsulfoxide and was used at a 1:1000 dilution.
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Publication 2023
Alabaster Antipain Aprotinin benzamidine Chloride, Ammonium Detergents Glucosylceramides Glycerin Glycerylphosphorylcholine hexadecanamide leupeptin Lipids miltefosine N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylserine N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)phosphatidylethanolamine NBD-galactosylceramide nitrobenzoxadiazolyl-conjugated phosphatidylcholine pepstatin phosphoethanolamine Phosphorylcholine Phosphoserine Protease Inhibitors Sphingosine sphingosyl beta-glucoside Sulfoxide, Dimethyl Technique, Dilution

Top products related to «Phosphoserine»

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Ab9332 is a mouse monoclonal antibody that recognizes human Integrin alpha V. It is suitable for use in various immunological techniques such as immunoprecipitation and immunohistochemistry.
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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.
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Anti-FLAG is a lab equipment product used for the detection and purification of proteins tagged with the FLAG epitope. It functions as an affinity reagent that binds to the FLAG tag, enabling the isolation and identification of the tagged proteins.
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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.
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Anti-phosphoserine is a primary antibody used to detect and study phosphorylation of serine residues in proteins. It is a useful tool for analyzing cellular signaling pathways and post-translational modifications.
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Anti-phosphoserine is a reagent used in laboratory analysis to detect and quantify phosphorylated serine residues in proteins. It serves as a key tool in the study of protein phosphorylation, a ubiquitous post-translational modification with important regulatory roles in cellular processes.
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Phosphoserine is a chemical compound used in various laboratory applications. It is a type of amino acid derivative that contains a phosphate group attached to the serine residue. Phosphoserine serves as a key component in many biochemical processes and is widely utilized in research and analytical procedures.
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1,2-dioleoyl-sn-glycero-3-phosphoserine is a phospholipid compound used in various research applications. It is a naturally occurring lipid that serves as a structural component in biological membranes. This product can be used as a reagent in cell culture, liposome formulation, and other biochemical studies.
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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.
The AB1603 is a laboratory centrifuge designed for general purpose applications. It features a compact and durable construction, and can accommodate a variety of sample tube sizes. The centrifuge is capable of reaching speeds up to 6,000 RPM, providing efficient separation of samples.

More about "Phosphoserine"

Phosphoserine, also known as phospho-serine or p-serine, is a crucial amino acid derivative that plays a vital role in cellular signaling, regulation, and various biological processes.
This modified form of the amino acid serine is created by the addition of a phosphate group, resulting in a phosphorylated serine residue.
Phosphoserine serves as an important post-translational modification that can alter the function, structure, and localization of target proteins, making it a key player in enzyme activity, signal transduction, and protein-protein interactions.
Researchers often utilize phosphoserine in a range of applications, such as studying cell signaling pathways, investigating protein-protein interactions, and developing therapeutic interventions.
To optimize phosphoserine research, scientists can leverage AI-driven platforms like PubCompare.ai, which help identify the best protocols and products from literature, preprints, and patents.
These platforms provide accurate and reproducible comparisons, taking the guesswork out of phosphoserine experiments and enhancing the reliability and reproducibility of the research.
In addition to phosphoserine, related terms and concepts include PVDF membranes, which are commonly used for protein transfer and detection, and Anti-FLAG, a widely used affinity tag for protein purification and identification.
Other relevant substances include 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, a phospholipid used in cell membrane studies, and 1,2-dioleoyl-sn-glycero-3-phosphoserine, a phospholipid that can be used as a phosphoserine analog.
Antibodies like Anti-phosphoserine are also valuable tools for the detection and analysis of phosphoserine-containing proteins.
By understanding the broader context of phosphoserine research, scientists can more effectively navigate the field and achieve their research goals.