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

Membrane Glycoproteins

Membrane glycoproteins are complex biomolecules found on the surface of cells, playing crucial roles in cellular communication, adhesion, and signaling.
These glycosylated proteins embedded within the lipid bilayer are involved in a wide range of physiological and pathological processes, making them important targets for biomedical research.
Membrane glycoproteins mediate interactions between cells and their extracellular environment, facilitating the transduction of signals across the cell membrane.
They are involved in processes such as cell-cell recognition, immune response, and disease pathogenesis.
Studying the structure, function, and regulation of membrane glycoproteins can provide valuable insights into fundamental biological mechanisms and support the development of novel therapeutic strategies.
Reserchers leveraging the power of PubCompare.ai can effeciently locate the best protocols from literature, preprints, and patents to enhance the reproducibility and accuracy of their membrane glycoprotein studies, unlocking new discoveries.

Most cited protocols related to «Membrane Glycoproteins»

1
Quadruple Immunofluorescence Quantification of OXPHOS
Cited 19 times
Quadruple immunofluorescence was carried out on transverse muscle sections (10 μm) using antibodies detecting subunits of OXPHOS complexes (Supplementary Table S1). Complex I was detected using an antibody against subunit NDUFB823 (link), and Complex IV using an antibody to mtDNA encoded subunit I (COX-I). Mitochondrial mass was quantified using an antibody to porin, an outer mitochondrial membrane voltage-gated ion channel. Laminin, a basement membrane glycoprotein, was used to label the myofibre boundaries (Supplementary Table S1). Briefly, the sections were fixed in cold 4% paraformaldehyde (Sigma) for 3 min and permeabilised in a methanol (Fisher) gradient (10 min 70% methanol, 10 min 95% methanol, 20 min 100% methanol, 10 min 95%.methanol and 10 min 70% methanol). Non-specific protein interactions were blocked with 10% normal goat serum (Sigma) and incubated with the primary antibodies in a humidified chamber at 4 °C overnight (Supplementary Table S1). Following washes in TBST (Sigma), the sections were incubated with the secondary antibodies for 2 h at 4 °C and subsequently with streptavidin conjugated with Alexa 647 (Life Technologies) for 2 h at 4 °C (Supplementary Table S1). The sections were washed and mounted in Prolong Gold (Sigma). No-primary antibody controls, incubated only with anti-laminin antibody, were processed for each muscle sample.
Rocha M.C., Grady J.P., Grünewald A., Vincent A., Dobson P.F., Taylor R.W., Turnbull D.M, & Rygiel K.A. (2015). A novel immunofluorescent assay to investigate oxidative phosphorylation deficiency in mitochondrial myopathy: understanding mechanisms and improving diagnosis. Scientific Reports, 5, 15037.
Full text: Click here
Publication 2015
Antibodies Antibodies, Anti-Idiotypic Cold Temperature DNA, Mitochondrial Fluorescent Antibody Technique Glycoproteins Goat Gold Immunoglobulins Ion Channel Laminin Membrane, Basement Membrane Glycoproteins Methanol Mitochondria Mitochondrial Membrane, Outer Muscle Tissue NADH Dehydrogenase Complex 1 Oxidase, Cytochrome-c paraform Porin Proteins Protein Subunits PTGS1 protein, human Serum Streptavidin
2
VSV Pseudotyping and Transduction Assay
Cited 16 times

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2020
ACE2 protein, human aloxistatin Antibodies, Anti-Idiotypic Beetles camostat mesylate Cardiac Arrest Centrifugation Chloride, Ammonium Cloning Vectors DC-specific ICAM-3 grabbing nonintegrin DNA Replication enhanced green fluorescent protein Goat Hybridomas Immunoglobulin G Immunoglobulins Luciferases, Firefly Membrane Glycoproteins Mus Plasmids Protease Inhibitors Serum Technique, Dilution Virus
3
Predicting SARS-CoV-2 B Cell Epitopes
Cited 15 times

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2020
Amino Acids B-Lymphocytes Cellular Immune Response Coronavirus Epitopes Epitopes, B-Lymphocyte Hypersensitivity Immunoglobulins Membrane Glycoproteins Nucleocapsid Phosphoproteins Proteins Severe acute respiratory syndrome-related coronavirus spike protein, SARS-CoV-2
4
Ebola Vaccine Antibody Response Measurement
Cited 12 times
IgG antibody levels against the Ebola surface glycoprotein were measured in serum at baseline and at week 1 and months 1, 6, and 12 with the use of the Filovirus Animal Nonclinical Group (FANG) assay (Section 3 in the Supplementary Appendix). Antibody levels were also measured in plasma at days 3, 10, and 14 in 24 participants for whom rVSVΔG-ZEBOV-GP shedding was measured on those days.
A participant was considered to have a positive vaccine response at a follow-up visit if the log10 titer was increased by a factor of 4 or more from the baseline value (see Section 3 in the Supplementary Appendix) and if the participant had not had an elevated titer at baseline. All the laboratory measurements were performed in Liberia. At the time of the trial, there were no facilities in the country for measuring T-cell responses.
Kennedy S.B., Bolay F., Kieh M., Grandits G., Badio M., Ballou R., Eckes R., Feinberg M., Follmann D., Grund B., Gupta S., Hensley L., Higgs E., Janosko K., Johnson M., Kateh F., Logue J., Marchand J., Monath T., Nason M., Nyenswah T., Roman F., Stavale E., Wolfson J., Neaton J.D, & Lane H.C. (2017). Phase 2 Placebo-Controlled Trial of Two Vaccines to Prevent Ebola in Liberia. The New England journal of medicine, 377(15), 1438-1447.
Publication 2017
Animals Biological Assay factor A Filoviridae Hemorrhagic Fever, Ebola Immunoglobulin G Immunoglobulins Membrane Glycoproteins Plasma Serum T-Lymphocyte Vaccines
5
Multicolor Fluorescent Staining of Cellular Organelles
Cited 11 times
When staining for surface glycoproteins, 50 μg/ml Alexa Fluor® 555-conjugated WGA (wheat-germ agglutinin; Invitrogen) was applied to the cells on ice for 5 min in DMEM (without Phenol Red or sodium pyruvate) supplemented with 25 mM Hepes (Invitrogen) and 10% FBS, rinsed twice in the same solution and then fixed as above. Staining for plasma membrane PtdIns(4,5)P2 or endosomal PtdIns3P were performed as described in the preceding two sections. For staining of the endoplasmic reticulum, after post-fixation and rinsing in PBS/NH4Cl, cells were incubated for 1 min with DiOC6 (3,3′-dihexyloxacarbocyanine iodide; Invitrogen) in PBS, rinsed once with distilled water and mounted in ProLong Gold with 1 μg/ml DAPI as above. A similar protocol was used to stain cells with 500 μM DiD (1,1′-dioctadecyl-3,3,3′,3′-tetramethylindodicarbocyanine perchlorate; Invitrogen). For Golgi staining, the slides were chilled on ice for 2 min following the post-fixation and rinsing. They were incubated with a 5 μM solution of NBD-C6-ceramide [N-(ε-7-nitrobenz-2-oxa-1,3-diazol-4-yl-aminocaproyl)-D-erythro-sphingosine] complexed to BSA (Invitrogen) in PBS for 30 min on ice. Unbound ceramide was removed with two rinses in ice-cold PBS, and extra-Golgi ceramide was extracted by four washes with 3% (w/v) defatted-BSA (Sigma–Aldrich) in PBS over 1 h at room temperature. Finally, slides were stained for 5 min in 1 μg/ml DAPI in PBS, rinsed once in distilled water and mounted in Fluoromount-G (Southern Biotech). Note that we found retention of this latter dye was poor in glycerol-based mountants, hence the use of aqueous Fluoromount-G. Furthermore, slides stained with NBD-C6-ceramide were imaged promptly after staining, since we noticed progressive loss of the stain from the Golgi over a time course of hours.
Hammond G.R., Schiavo G, & Irvine R.F. (2009). Immunocytochemical techniques reveal multiple, distinct cellular pools of PtdIns4P and PtdIns(4,5)P2. Biochemical Journal, 422(Pt 1), 23-35.
Publication 2009
3,3'-dihexaoxycarbocyanine iodide Alexa Fluor 555 Cells Ceramides Cold Temperature DAPI Endoplasmic Reticulum Endosomes erythro-(2R,3S)-sphingosine Glycerin Gold Golgi Apparatus HEPES Iodides Membrane Glycoproteins N-(7-(4-nitrobenzo-2-oxa-1,3-diazole))-6-aminocaproyl sphingosine perchlorate phosphatidylinositol 3-phosphate Phosphatidylinositols Plasma Membrane Pyruvate Retention (Psychology) Sodium Stains Wheat Germ Agglutinins

Most recents protocols related to «Membrane Glycoproteins»

1
Evaluation of mRNA-based hMPV Vaccines
Not available on PMC !

Example 13

The instant study is designed to test the efficacy in cotton rats of candidate hMPV vaccines against a lethal challenge using an hMPV vaccine comprising mRNA encoding Fusion (F) glycoprotein, major surface glycoprotein G, or a combination of both antigens obtained from hMPV. Cotton rats are challenged with a lethal dose of the hMPV.

Animals are immunized intravenously (IV), intramuscularly (IM), or intradermally (ID) at week 0 and week 3 with candidate hMPV vaccines with and without adjuvant. Candidate vaccines are chemically modified or unmodified. The animals are then challenged with a lethal dose of hMPV on week 7 via IV, IM or ID. Endpoint is day 13 post infection, death or euthanasia. Animals displaying severe illness as determined by >30% weight loss, extreme lethargy or paralysis are euthanized. Body temperature and weight are assessed and recorded daily.

In experiments where a lipid nanoparticle (LNP) formulation is used, the formulation may include a cationic lipid, non-cationic lipid, PEG lipid and structural lipid in the ratios 50:10:1.5:38.5. The cationic lipid is DLin-KC2-DMA (50 mol %) or DLin-MC3-DMA (50 mol %), the non-cationic lipid is DSPC (10 mol %), the PEG lipid is PEG-DOMG (1.5 mol %) and the structural lipid is cholesterol (38.5 mol %), for example.

US11872278B2. Combination HMPV/RSV RNA vaccines (2024-01-16). ModernaTX, Inc. [US]. Inventors: Giuseppe Ciaramella [US], Sunny Himansu [US].
Full text: Click here
Patent 2024
Animals Antigens Body Temperature Cations Cholesterol Euthanasia Glycoproteins Human Metapneumovirus Infection Lethargy Lipid Nanoparticles Lipids Membrane Glycoproteins Pharmaceutical Adjuvants Rats, Cotton RNA, Messenger Rodent Vaccines
2
Evaluating Immunogenicity of hMPV Vaccine Candidates
Not available on PMC !

Example 12

The instant study is designed to test the immunogenicity in mice of candidate hMPV vaccines comprising a mRNA polynucleotide encoding Fusion (F) glycoprotein, major surface glycoprotein G, or a combination thereof, obtained from hMPV.

Mice are immunized intravenously (IV), intramuscularly (IM), or intradermally (ID) with candidate vaccines. Candidate vaccines are chemically modified or unmodified. A total of four immunizations are given at 3-week intervals (i.e., at weeks 0, 3, 6, and 9), and sera are collected after each immunization until weeks 33-51. Serum antibody titers against Fusion (F) glycoprotein or major surface glycoprotein (G) protein are determined by ELISA. Sera collected from each mouse during weeks 10-16 are pooled, and total IgG purified. Purified antibodies are used for immunoelectron microscopy, antibody-affinity testing, and in vitro protection assays.

US11872278B2. Combination HMPV/RSV RNA vaccines (2024-01-16). ModernaTX, Inc. [US]. Inventors: Giuseppe Ciaramella [US], Sunny Himansu [US].
Full text: Click here
Patent 2024
Antibodies Antibody Affinity Antigens Biological Assay Enzyme-Linked Immunosorbent Assay Glycoproteins GTP-Binding Proteins Human Metapneumovirus Immunization Immunogenicity, Vaccine Immunoglobulins Membrane Glycoproteins Microscopy, Immunoelectron Mus Polynucleotides RNA, Messenger Serum Vaccines
3
Structural Analysis of SARS-CoV-2 Spike Protein
The instructor provided to the students a brief introduction
to the most important features of the structure of SARS-CoV-2. The
four major structural proteins are displayed: the envelope (E), membrane
(M), nucleocapsid (N), and spike (S) proteins (Figure 1).7 (link)It is highlighted that spike protein (approximately 180–200
kDa) is the surface glycoprotein anchored to the viral membrane that
plays an essential role when the infection process of SARS-CoV-2 takes
place. This protein is a trimer of three identical protomers (Figure 2). Each protomer
contains three segments: a short intracellular tail (IC), a transmembrane
anchor (TM), and a large ectodomain that extends outward from the
virus which is coated with sugar chains to hide the virus from the
immune system8 (link) and comprises S1 and S2
subunits.
Next, the students are invited to study the ectodomain by analyzing
the requested structural features that they must observe manipulating
PyMOL.
Although hundreds of structures of this spike protein
are already
available in the Protein Data Bank, the one with the code 7DWY(9 (link)) has been selected and must be loaded in a PyMOL session.
They are encouraged to distinguish the four different levels of the
protein structures: primary, secondary, tertiary, and quaternary,
changing the representation of the molecule from lines or wireframe
to cartoon.
They must learn how to select individual residues
or different
chains, how to change their colors, how to generate objects, how to
show and hide different parts of the protein, how to measure distances
and angles for bonds, and how to generate surfaces.
They have
to realize that the spike protein is a complex of three
identical chains. A schematic illustration of the spike protein (Figure 3) is given to the
students, and they must recognize every single domain in the ectodomain,
extracting them as different objects and coloring them in the suggested
color.
The S1 subunit has an N-terminal
domain (NTD) and a receptor-binding
domain (RBD) located in the C-terminal domain, which is implied in
recognition and binding to the host cell receptor. S2 consists of
the fusion peptide (FP), two heptad repeats 1 (HR1 and HR2) which
operate the fusion of viral and host membranes, a transmembrane domain
(TM), and a cytoplasmic tail (CT).
When different species of
coronavirus are compared, the S2 subunit
is highly conserved, but the sequence of the S1 subunit varies greatly.
S1 and S2 are connected to the S1/S2 cleavage site in which specific
proteases act. The cleavage transforms the spike protein into a fusion
competent form that suffers several conformational changes and allows
it to anchor to the host membrane leading to the membrane fusion.10 (link)
, & Maya C. (2023). Using PyMOL to Understand Why COVID-19 Vaccines Save Lives. Journal of Chemical Education, 100(3), 1351-1356.
Full text: Click here
Publication 2023
Carbohydrates Cells COVID 19 Cytokinesis Cytoplasm Membrane Fusion Membrane Glycoproteins M protein, multiple myeloma Nucleocapsid Peptides Proteins Protein Subunits Protomers Protoplasm SARS-CoV-2 Student Tail Tissue, Membrane Virus
4
Serosurvey of Canine Distemper Virus in Nepalese Tigers and Leopards
The study focused on two geographic regions of Nepal, the Terai and the Mid-hills. The lowland Terai runs along the country’s southern border and is home to five national parks: Shuklaphanta National Park (ShNP), Bardia National Park (BNP), Banke National Park (BaNP), Chitwan National Park (CNP) and Parsa National Park (PNP). Between them, these protected areas total 3402 km2 and accommodate most of Nepal’s tigers. Inside the national parks, the landscape is a matrix of grassy floodplains and tropical forests, but outside these areas, the region is widely settled and heavily cultivated. The Mid-hills lie north of the Terai and range between 600 and 4800 m. Here, the majority of settlements are found in the valleys, while much of the hillside remain densely forested. The region includes a large portion of Annapurna Conservation Area (ACA). However, unlike the national parks, people are not excluded from living or working in this area.
The samples analyzed in this study were collected opportunistically and archived in the molecular lab at the Biodiversity Conservation Center, Sauraha, in CNP. They included sera from 28 tigers and 20 leopards. Captures took place between 2011 and 2021 and were carried out jointly by the Department of National Parks and Wildlife Conservation (DNPWC) and the National Trust for Nature Conservation (NTNC). Almost all (47/48) captures were conducted as part of routine wildlife management and conflict resolution. The only exception to this was a single tiger, which was captured as part of a collaring study in 2021. Animals were immobilized using a standard protocol of medetomidine (0.07 mg/kg) and ketamine (3 mg/kg) delivered intramuscularly via dart gun or hand injection. Blood samples were collected during immobilization, and the separated serum was archived at −20 °C.
Most tigers (26/28) were captured in and around the Chitwan–Parsa Complex (CPC; 27°46′ N, 84°53′ E) which includes CNP, PNP and the surrounding buffer zones. The remaining two tigers were captured in or around the Bardia–Banke Complex (BBC; 28°33′ N, 81°65′ E) which includes BNP, BaNP and the surrounding buffers zones. Meanwhile, most leopards (17/20) were captured in the central Mid-hill districts, two were captured in the CPC and one was captured in Koshi Thappu Wildlife Reserve (KTWR; 26°65′ N, 87°00′ E).
Prior to testing, all samples were heat inactivated at 56 °C for 30 min. A modified version of a previously described serum neutralization test [52 (link)] was used to screen the heat-inactivated samples. This protocol uses an engineered cell line, HEK293dogSLAM, which expresses the canine signaling lymphocytic activation molecule (SLAM-F1, the receptor used by CDV for cell entry) and a replication deficient vesicular stomatitis virus pseudotype expressing hemagglutinin and fusion surface glycoproteins from the Onderstepoort strain of CDV. The referenced protocol was adapted by substituting green fluorescent protein (GFP) for luciferase as the marker for infection [12 (link)]. Cell lines HEK293dogSLAM and HEK293T were supplied by the University of Glasgow. Tests were read by examining wells using an inverted fluorescent microscope under low power. Dilutions which achieved a 90% reduction in the number of infected cells compared to the mean count of four serum-free controls were considered to have effectively neutralized the virus.
All samples were tested in quadruplicate using a 1:16 serum dilution along with a panel of 20 dog sera as positive controls. Samples which tested positive on the initial assay were re-tested to determine the titer using four-fold serial serum dilutions from 1:16 to 1:16,384. The Spearman–Karber method [53 ] was then used to calculate the final titer. Samples with a titer of 1:16 or greater were considered positive. Seroprevalence was calculated as the number of animals testing positive, which was divided by the total number of animals tested and expressed with 95% binomial confidence intervals. Population comparisons were conducted using a two-proportions z-test in R [54 ]. Results were reviewed in conjunction with the clinical histories for the individuals concerned.
Mortality records from the Central Zoo in Lalitpur and in CNP were reviewed for the period September 2019 to September 2022 to identify additional tigers and leopards that had suffered fatal neurological disease, which was characterized by seizures.
Bodgener J., Sadaula A., Thapa P.J., Shrestha B.K., Gairhe K.P., Subedi S., Rijal K.R., Pandey P., Joshi J.D., Kandel P., Lamichane B.R., Pokheral C.P., Subedi N., Kandel R.C., Luitel H., Techakriengkrai N, & Gilbert M. (2023). Canine Distemper Virus in Tigers (Panthera tigris) and Leopards (P. pardus) in Nepal. Pathogens, 12(2), 203.
Full text: Click here
Publication 2023
Animals Biological Assay BLOOD Buffers Cell Lines Cells DNA Replication Green Fluorescent Proteins Hemagglutinin Immobilization Infection Ketamine Leopard Luciferases Medetomidine Membrane Glycoproteins Microscopy Nervous System Disorder Neutralization Tests Poaceae Seizures Serum signaling lymphocytic activation molecule, human Strains Technique, Dilution Tigers Vesicular stomatitis Indiana virus Virus
5
Structural Modeling and Membrane Interaction of Viral Proteins
To compare differences in the structure of WT UL37 and UL37 C819S, we generated tertiary structural models using AlphaFold2 (Google Colaboratory). UL37 WT and UL37 C819S were aligned using PyMol to determine the root mean standard deviation value (RMSD). To determine structural changes and differences in membrane interaction of the gK/UL20 complex, we predicted protein–protein complex formation using AlphaFold2- multimer (Google Colaboratory). The amino acid sequences of human alphaherpesvirus-1 glycoprotein K (gK) (Accession Number AFH41179.1) and UL20 (Accession Number QFQ61390.1) were retrieved from GenBank and used as input, alongside the gKΔ31–68/UL20Δ4–22 amino acid sequences. The predicted models were inserted into a bilipid membrane using MemProtMD. Briefly, MEMEMBED was used to orient the protein relative to a lipid membrane. A box of 80 Å in size (z-axis) was generated to contain the protein. The protein was contained in the box, and the x and y axes were determined by providing a distance of 30 Å from the protein. Dipalmitoylphosphatidylcholine (DPPC) lipid models were used to insert the protein into a bilipid membrane. The bilipid membrane was built with the following using the MARTINI 2.1 forcefield: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG), cardiolipin (CL) and glucosyl-lipopolysaccharide (UDP1). The coarse-grained molecular dynamics (CGMD) simulation was completed at 60 ns. At the end of the simulation, a snapshot was taken to convert the coarse-grained resolution to atomistic resolution using CG2AT-align.
Clark C.M., Jambunathan N., Collantes T.M, & Kousoulas K.G. (2023). Inactivation of the UL37 Deamidase Enhances Virus Replication and Spread of the HSV-1(VC2) Oncolytic Vaccine Strain and Secretion of GM-CSF. Viruses, 15(2), 367.
Full text: Click here
Publication 2023
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol Amino Acid Sequence Cardiolipins colfosceril palmitate Epistropheus Glycoproteins Human Herpesvirus 1 Lipid A Lipids Lipopolysaccharides Membrane Glycoproteins Membrane Proteins Plant Roots Protein Biosynthesis Proteins Tissue, Membrane

Top products related to «Membrane Glycoproteins»

1
Facscalibur by BD
Sourced in United States, Germany, United Kingdom, China, Canada, Japan, Italy, France, Belgium, Switzerland, Singapore, Uruguay, Australia, Spain, Poland, India, Austria, Denmark, Netherlands, Jersey, Finland, Sweden
The FACSCalibur is a flow cytometry system designed for multi-parameter analysis of cells and other particles. It features a blue (488 nm) and a red (635 nm) laser for excitation of fluorescent dyes. The instrument is capable of detecting forward scatter, side scatter, and up to four fluorescent parameters simultaneously.
2
Dulbecco modified eagle medium (dmem) by Thermo Fisher Scientific
Sourced in United States, China, United Kingdom, Germany, France, Australia, Canada, Japan, Italy, Switzerland, Belgium, Austria, Spain, Israel, New Zealand, Ireland, Denmark, India, Poland, Sweden, Argentina, Netherlands, Brazil, Macao, Singapore, Sao Tome and Principe, Cameroon, Hong Kong, Portugal, Morocco, Hungary, Finland, Puerto Rico, Holy See (Vatican City State), Gabon, Bulgaria, Norway, Jamaica
DMEM (Dulbecco's Modified Eagle's Medium) is a cell culture medium formulated to support the growth and maintenance of a variety of cell types, including mammalian cells. It provides essential nutrients, amino acids, vitamins, and other components necessary for cell proliferation and survival in an in vitro environment.
3
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.
4
Opti mem by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, China, Japan, Canada, France, Switzerland, Italy, Australia, Belgium, Spain, Denmark, Ireland, Netherlands, Holy See (Vatican City State), Israel
Opti-MEM is a cell culture medium designed to support the growth and maintenance of a variety of cell lines. It is a serum-reduced formulation that helps to reduce the amount of serum required for cell culture, while still providing the necessary nutrients and growth factors for cell proliferation.
5
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.
6
Fitc conjugated anti p selectin by BD
Sourced in United States
FITC-conjugated anti-P-selectin is a fluorescently labeled antibody that binds to the P-selectin cell surface receptor. P-selectin is involved in cell adhesion and plays a role in inflammatory processes.
7
Geneticin g418 sulfate by Thermo Fisher Scientific
Sourced in United States, Switzerland
Geneticin (G418 Sulfate) is a broad-spectrum antibiotic used as a selectable marker in eukaryotic cell culture. It acts by inhibiting protein synthesis, which leads to cell death in non-resistant cells. Geneticin is commonly used for the selection and maintenance of stable cell lines expressing recombinant proteins.
8
Dimethyl sulfoxide (dmso) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Sao Tome and Principe, France, Macao, India, Canada, Switzerland, Japan, Australia, Spain, Poland, Belgium, Brazil, Czechia, Portugal, Austria, Denmark, Israel, Sweden, Ireland, Hungary, Mexico, Netherlands, Singapore, Indonesia, Slovakia, Cameroon, Norway, Thailand, Chile, Finland, Malaysia, Latvia, New Zealand, Hong Kong, Pakistan, Uruguay, Bangladesh
DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
9
Cellquest software by BD
Sourced in United States, Germany, United Kingdom, Italy, Canada, China, Japan, Belgium, France, Spain, Switzerland, Poland, Uruguay, Denmark, Singapore
CellQuest software is a data acquisition and analysis software designed for flow cytometry applications. It provides tools for acquiring, processing, and analyzing flow cytometry data.
10
4 6 diamidino 2 phenylindole (dapi) by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, Japan, China, Canada, Italy, Australia, France, Switzerland, Spain, Belgium, Denmark, Panama, Poland, Singapore, Austria, Morocco, Netherlands, Sweden, Argentina, India, Finland, Pakistan, Cameroon, New Zealand
DAPI is a fluorescent dye used in microscopy and flow cytometry to stain cell nuclei. It binds strongly to the minor groove of double-stranded DNA, emitting blue fluorescence when excited by ultraviolet light.

More about "Membrane Glycoproteins"

Membrane glycoproteins are complex biomolecules that play crucial roles in cellular communication, adhesion, and signaling.
These glycosylated proteins embedded within the lipid bilayer are involved in a wide range of physiological and pathological processes, making them important targets for biomedical research.
Membrane glycoproteins mediate interactions between cells and their extracellular environment, facilitating the transduction of signals across the cell membrane.
They are involved in processes such as cell-cell recognition, immune response, and disease pathogenesis.
Studying the structure, function, and regulation of membrane glycoproteins can provide valuable insights into fundamental biological mechanisms and support the development of novel therapeutic strategies.
Researchers can leverage the power of AI-driven platforms like PubCompare.ai to efficiently locate the best protocols from literature, preprints, and patents, enhancing the reproducibility and accuracy of their membrane glycoprotein studies.
This can unlock new discoveries and elevate their research.
Membrane glycoproteins can be analyzed using various techniques, such as flow cytometry with FACSCalibur instruments, cell culture in DMEM media supplemented with FBS, and transfection with Lipofectamine 2000 in Opti-MEM.
Researchers may also use FITC-conjugated anti-P-selectin antibodies, Geneticin (G418 Sulfate) for selection, and DMSO for cryopreservation.
CellQuest software can be utilized for data analysis, and DAPI staining can be employed for nuclear visualization.
By incorporating these techniques and tools, researchers can gain a deeper understanding of membrane glycoproteins and their role in biological processes.