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).
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Amino Acid
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Phosphoserine
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.
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»
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
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
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.
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
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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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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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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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.
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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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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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.
Sourced in United States
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.
Sourced in Italy, Germany
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.
Sourced in United States
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.
Sourced in France
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.
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.
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.
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.