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Cell Surface Proteins

Cell surface proteins are integral membrane proteins that are expressed on the outer surface of cells.
They play crucial roles in a wide range of biological processes, including cell signaling, adhesion, and recognition.
These proteins serve as receptors, transporters, and enzymes, mediating the interaction between cells and their extracellular environment.
Understanding the expression and function of cell surface proteins is essential for studying cellular physiology, development, and pathological conditions.
Researchers can leverage PubCompare.ai's AI-driven protocol comparison tool to optimize their cell surface protein research, identifying the best protocols and products from literature, preprints, and patents.
This powerful, data-driven platform enhances reproducibility and accuracy, enabling researchers to experience the future of biological research today.

Most cited protocols related to «Cell Surface Proteins»

1
SaOS2 cells' ER-to-surface transport analysis
Cited 69 times
SaOS2 cells were transfected with the respective siRNAs and then with the respective expression plasmids for VSVG-GFP, VSVG-Myc, VSVG-MT1-MMP, or VSVG-KDELR-Myc with or without expression plasmid for sr-IFT20 or IFT20. To examine the ER-to-cell surface transport, VSVG-GFP-transfected SaOS2 cells were incubated overnight at 40 °C in DMEM containing 1% FBS to accumulate VSVG-GFP at the ER, and then shifted to DMEM containing 1% FBS and 0.1 mg/ml cycloheximide pre-warmed at 32 °C to allow transport through the Golgi. After 30 or 60 min in culture, cell surface proteins were biotinylated with 0.5 mg/ml Sulfo-NHS-ss-biotin (Thermo) in Dulbecco’s PBS (DPBS) for 30 min at 4 °C and quenched with 50 mM NH4Cl in DPBS for 10 min at 4 °C. After washing with ice-cold DPBS, cells were solubilized with Triton X-100 lysis buffer [25 mM Tris-HCl (pH7.5), 150 mM NaCl, 5 mM EDTA, 1% (v/v) Triton X-100, 0.4% (w/v) sodium deoxycholate, 10 µg/ml leupeptin, 10 µg/ml aprotinin, 0.25 mM pAPMSF]. Biotinylated proteins were affinity-purified with streptavidin-Sepharose beads and subjected to SDS-PAGE followed Western blot analyses. ER-to-cis-Golgi and intra-Golgi transport of VSVG and VSVG-MT1-MMP and retrograde transport of VSVG-KDELR have been described previously48 (link).
Nishita M., Park S.Y., Nishio T., Kamizaki K., Wang Z., Tamada K., Takumi T., Hashimoto R., Otani H., Pazour G.J., Hsu V.W, & Minami Y. (2017). Ror2 signaling regulates Golgi structure and transport through IFT20 for tumor invasiveness. Scientific Reports, 7, 1.
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Publication 2017
Aprotinin Buffers Cells Cell Surface Proteins Cold Temperature Cycloheximide Deoxycholic Acid, Monosodium Salt Edetic Acid Golgi Apparatus leupeptin Plasmids Proteins RNA, Small Interfering SDS-PAGE Sodium Chloride streptavidin-agarose sulfosuccinimidyl-2-(biotinamido)ethyl-1,3-dithiopropionate Triton X-100 Tromethamine Western Blot
2
Recombinant Malaria Antigen Expression
Cited 16 times
The regions corresponding to the entire extracellular domains of 51 merozoite cell-surface proteins from the P. falciparum 3D7 strain were determined by using transmembrane and GPI-anchor (33 (link), 34 (link)), or signal peptide (35 (link)) prediction software. Sequences encoding the extracellular domains of these proteins, with the exception of their signal peptide, were made by gene synthesis (GeneartAG) and are presented in Table I. All sequences were codon-optimized for expression in human cells and all potential N-linked glycosylation sites (NXS/T) were modified by substituting the serine or threonine residue with an alanine residue to prevent the inappropriate addition of large glycans that are absent in the native P. falciparum proteins. The coding sequences were flanked by unique NotI and AscI sites and cloned into a derivative of the pTT3 expression vector (36 (link)) between the leader sequence of the mouse variable κ light chain 7–33 (37 (link)), and a rat Cd4 domains 3 and 4 tag followed by an enzymatic biotinylation sequence as previously described (38 (link)). All expression constructs were cotransfected with the BirA biotinylation enzyme into HEK293E cells and are available from Addgene, a non-profit plasmid repository (www.addgene.org). The soluble biotinylated recombinant proteins were collected from the cell culture supernatant 6 days post-transfection, and dialyzed into HBS before analysis. During gene synthesis, constructs encoding the full-length ectodomain of RH1, RH2b and RH4 proved to be toxic in bacteria, and only subfragments could be produced as presented in Table I.
Crosnier C., Wanaguru M., McDade B., Osier F.H., Marsh K., Rayner J.C, & Wright G.J. (2013). A Library of Functional Recombinant Cell-surface and Secreted P. falciparum Merozoite Proteins. Molecular & Cellular Proteomics : MCP, 12(12), 3976-3986.
Publication 2013
Alanine Anabolism Bacteria Biotinylation Cell Culture Techniques Cells Cell Surface Proteins Cloning Vectors Codon Enzymes Exons Genes Homo sapiens Immunoglobulin kappa-Chains Merozoites Mus Plasmids Polysaccharides Protein Domain Protein Glycosylation Proteins Recombinant Proteins Serine Signal Peptides Strains Synthetic Genes Threonine Transfection
3
Reconstructing Leukocyte DNA Profiles
Cited 12 times
Purified granulocytes, monocytes, CD4T, CD8T, natural killer cells, and B cells from normal human subjects were purchased from AllCells LLC (Emeryville, CA). As described (http://www.allcells.com/normal-peripheral-blood/) ethical approval, including all consents and protocols, have been approved by an independent review board. Both positive and negative selection for relevant cell surface proteins was conducted by AllCells using antibodies conjugated to magnetic beads and protocols from Miltenyi Biotec, Inc. (Auburn, CA). DNA was extracted from purified blood leukocyte subtypes using the DNeasy blood and tissue kit (QIAGEN, Valencia CA) or the AllPrep DNA/RNA/Protein Mini Kit (QIAGEN) using previously described protocols [31 (link)]. DsDNA was quantified using a Qubit 3.0 fluorometer (Life Technologies). Following quantification, DNA extracted from purified leukocyte subtypes were mixed in predetermined proportions to reconstruct two distinct sets, consisting of n=6 samples each. The first set of reconstructed samples used mixtures of purified leukocyte subtype DNA in relatively equivalent proportions across the leukocyte subtypes, hereafter referred to as the MethodA samples. For the second set of six samples, the proportion of DNA for each leukocyte subtype were selected to resemble their relative fractions in the peripheral blood of normal human adult subjects (MethodB samples). All DNA samples were bisulfite modified using the Zymo EZ DNA Methylation kit (Irvine, CA) and epigenome-wide DNA methylation assessment was performed using the Illumina HumanMethylation450 array platform.
Koestler D.C., Jones M.J., Usset J., Christensen B.C., Butler R.A., Kobor M.S., Wiencke J.K, & Kelsey K.T. (2016). Improving cell mixture deconvolution by identifying optimal DNA methylation libraries (IDOL). BMC Bioinformatics, 17, 120.
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Publication 2016
Adult Antibodies BLOOD Cells Cell Surface Proteins DNA, Double-Stranded DNA Methylation Epigenome Granulocyte hydrogen sulfite Leukocytes Monocytes Natural Killer Cells Proteins Tissues
4
Extraction and Analysis of Cell Surface Proteins
Cited 11 times
Overnight cultures of S. aureus strains were diluted 1:100 into fresh TSB and grown for 3 h at 37°C. Staphylococci were centrifuged and washed twice with PBS. 3 ml of cells was spun down and suspended in 100 µl TSM buffer (50 mM Tris-HCL [pH 7.5], 10 mM MgCl2, and 0.5 M sucrose); lysostaphin (final concentration = 70 µg/ml−1) was added and allowed to incubate for 30 min at 37°C. The solution was spun down for 5 min at 9,000 g, and supernatants containing released cell-surface proteins were collected. 15 µl of lysostaphin extracts were incubated with 3 µCi [14C]AMP for 30 min at 37°C. Samples were spotted on a silica plate, followed by separation by TLC using a (75:25 isopropanol/double-distilled H2O) 0.2-M ammonia bicarbonate solvent. For cell-wall extracts of S. aureus, E. faecilis, B. anthracis, and S. epidermidis digested with mutanolysin, mutanolysin was substituted for lysostaphin and used according to the manufacturer's recommended conditions. When assayed with purified proteins, 2 µM of purified AdsA or BasA was incubated in a final volume of 15 µl with 3 µCi [14C]AMP in the presence of the metal cations in TSM buffer indicated in the figures.
Thammavongsa V., Kern J.W., Missiakas D.M, & Schneewind O. (2009). Staphylococcus aureus synthesizes adenosine to escape host immune responses. The Journal of Experimental Medicine, 206(11), 2417-2427.
Publication 2009
Ammonia Bacillus anthracis Bicarbonates Buffers Cations Cells Cell Surface Proteins Cell Wall Isopropyl Alcohol Lysostaphin Magnesium Chloride Metals mutanolysin Proteins Silicon Dioxide Solvents Staphylococcus Staphylococcus epidermidis Strains Sucrose Tromethamine
5
Predicting Protein Disorder and Domains
Cited 7 times
Each sequence from each proteome was searched for similarities either with the Protein Data Bank (PDB), using the BLASTPGP program version 2.26. Only one iteration was done from each entire protein sequence. Hits sharing more than 95% of sequence identity were selected. The disorder was then filtered by using Mobi-DB ([34] , http://mobidb.bio.unipd.it/), which extends the experimental disorder observations found Disprot database to the whole PDB, or by only considering the classes a, b, c, d, e, f from the SCOP structural databases ([36] (link), http://scop.mrc-lmb.cam.ac.uk/scop/). These classes correspond to all alpha protein, all beta protein, all alpha and beta protein (mainly parallel beta sheet), all alpha and beta protein (mainly anti-parallel beta sheet), multi-domain proteins, membrane and cell surface proteins and peptides, respectively.
We obtained information on Conserved Domain(s) (CD) for each protein sequence through the NCBI server (http://www.ncbi.nlm.nih.gov/Structure/cdd/cdd.shtml), which has pre-computed domain architectures. These pre-computed architectures were fixed using the RPBLASTprogram (blast tools version 2.26) with the Conserved Domain Database (version 3.1) [24] (link).
IUPRED was used as a disorder predictor ([30] (link), [31] (link), http://iupred.enzim.hu/). We used the “long” mode (IUPRED-L) to predict disordered segments. A probability to be disordered up to 0.5 was used to consider a position to be disordered. The “glob” mode (IUPRED-G) was used to predict globular domain boundaries from the disordered positions. The “short” mode was not used as it focuses on small disordered regions such as both loops and termini tails.
We used ANCHOR to predict disorder to order transitions ([44] (link), [45] (link)
http://anchor.enzim.hu/). ANCHOR is developed from the IUPRED program, and was used with default parameters.
Faure G, & Callebaut I. (2013). Comprehensive Repertoire of Foldable Regions within Whole Genomes. PLoS Computational Biology, 9(10), e1003280.
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Publication 2013
Amino Acid Sequence Cell Surface Proteins Eye FCER2 protein, human Peptides Proteins Proteome Tail Tissue, Membrane

Most recents protocols related to «Cell Surface Proteins»

1
Antibody Binding to Cell Surface Proteins
Not available on PMC !

Example 10

To identify targets of CCR8 antibodies, CCR8 antibodies were incubated with cells forced to express about 4,500 cell surface proteins in a fixed or live state. Anti-CCR8-1 was demonstrated to bind to only CCR8 while anti-CCR8-2 also bound to amyloid precursor-like protein 2 (APLP2), but at a significantly lower concentration (data not shown).

US11859000B2. Anti-CCR8 antibodies and uses thereof (2024-01-02). Vaccinex, Inc. [US]. Inventors: Pamela M. Holland [US], Andrew Lake [US], Austin Dulak [US], Ernest Smith [US], Maria Scrivens [US], Caroline Harvey [US], Renee Kirk [US], Leslie Balch [US], Sonia G. Das [US], Christopher Converse Wells [US].
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Patent 2024
Antibodies APLP1 protein, human CCR8 protein, human Cells Cell Surface Proteins Immunoglobulins
2
CyTOF Immune Cell Profiling Panels
For CyTOF, two panels were used (Supplementary Table S1). The panel design tool provided by Fluidigm (now Standard BioTools Inc.) was used. Noisy channels (e.g., 157 Gd) were unused to minimize signal spill over. Antibodies against bright/widely expressed antigens were in “dimmer” channels and antibodies against rare or low expressing proteins were used in channels with high sensitivity/less prone to spill over. The first panel with 42 markers was used on live/nonfixed samples and consisted of antibodies targeting proteins on the cell surface of immune cells. This panel was used on BM cells and included marker used to identify progenitor cells in this tissue. The second panel contained lineage antibodies and antibodies targeting intracellular proteins. In this case, samples were fixed. Markers that were not required for delineating major cell populations (CD150, CD24) or targets that did not withstand fixation (e.g., CD103) were removed to reduce background. Flow cytometry antibodies are listed in Supplementary Table S2.
Matos I., Barvalia M., Chehal M.K., Robertson A.G., Kulic I., Silva J.A., Ranganathan A., Short A., Huang Y.H., Long E., Priatel J.J., Dhanji S., Nelson B.H., Krebs D.L, & Harder K.W. (2023). Tumor-derived GCSF Alters Tumor and Systemic Immune System Cell Subset Composition and Signaling. Cancer Research Communications, 3(3), 404-419.
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Publication 2023
alpha HML-1 Antibodies Antigens Cells Cell Surface Proteins Diet, Protein-Restricted Flow Cytometry Hypersensitivity Population Group Proteins Protoplasm signaling lymphocytic activation molecule, human Stem Cells Tissues
3
Regulation of Axon Growth by Vax1 Protein
Human cervical cancer HeLa cells and human embryonic kidney (HEK) 293 T cells were cultured in Dulbecco’s Modified Eagle’s Medium (DMEM) supplemented with 10% fetal bovine serum (FBS). For the luciferase assay, HEK293T cells (105) were transfected with 1 μg pCAGIG-V5 vectors encoding Vax1, Vax1AA, or Vax1(R152S) cDNA together with pGL3-Tcf7l2-luciferase (0.2 μg) and pCMV-β-gal (0.2 μg) reporter constructs. Luciferase activity in the transfected cells was measured at 24 h posttransfection and normalized to β-galactosidase activity to obtain the relative luciferase activity of the cells. To test the cellular penetration of the Vax1 protein, V5 peptides or V5-Vax1 proteins, which were purified from HEK293T cells, were added to the growth media (1.5 pmol/ml [final concentration]) of HeLa cells, which express GFP-Sdc2. The distribution of V5 peptides and V5-Vax1 proteins on the cell surface and inside the cells was examined by immunostaining with mouse anti-V5 and chicken anti-GFP antibodies.
Retinal explants were prepared as described previously16 . Briefly, the retina was prepared from mouse embryos at E13 and mixed with collagen in DMEM supplemented with 10% FBS. The retinal explants in collagen were then cultured in neurobasal medium containing B27 supplement (Invitrogen Inc.) for 48 h to allow the axons to grow from the explants. 6X-Histidine peptides or Vax1-6X-His proteins, which were purified from E. coli, were then added to the culture medium (2 pmol/ml [final concentration]) of retinal explants. Alternatively, the retinal explants were placed next to collagen droplets containing HEK293 cells (105 cells/droplet), which express Vax1 or Vax1AA. The lengths of retinal axons grown from the explants were measured before and after the treatments to determine the axon growth rate.
Min K.W., Kim N., Lee J.H., Sung Y., Kim M., Lee E.J., Kim J.M., Kim J.H., Lee J., Cho W., Yang J.M., Kim N., Kim J., Lee C.J., Park Y.G., Lee S.H., Lee H.W, & Kim J.W. (2023). Visuomotor anomalies in achiasmatic mice expressing a transfer-defective Vax1 mutant. Experimental & Molecular Medicine, 55(2), 385-400.
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Publication 2023
Anti-Antibodies Axon beta-Galactosidase Biological Assay Cells Cell Surface Proteins Cervical Cancer Chickens Cloning Vectors Collagen Culture Media Dietary Supplements DNA, Complementary Eagle Embryo Escherichia coli Fetal Bovine Serum HEK293 Cells HeLa Cells Histidine Homo sapiens Kidney Luciferases Mus Paragangliomas 3 Peptides Proteins Retina TCF7L2 protein, human
4
Single-cell sequencing analysis pipeline
Data were preprocessed with the 10x Genomics Cell Ranger 3.1.0 pipeline. The Seurat 3.1.3 R package (85 (link)) was used for downstream single-cell clustering and differential expression analysis. First, we aligned the reads from stomach single-cell data sets on the reference hg19 (for all analyses in this article) or Grch38 (hg38) (to specifically interrogate expression of TCR and Ig genes shown in Figure 2) genomes using the Cell Ranger pipeline for the quantification of the cells as well as genes and cell surface proteins. We performed quality check and a filtering protocol based on cutoff criteria for cells (number of feature expressions per cell >200 and <2500); gene expression (≥3 cells), mitochondria content (<10 %), ribosomal content (>5%), regression of cell cycle effect, and removing the noncoding gene from the expression data set. A total of 22,033 cells with 19,774 genes expressed in total were analyzed and visualized using UMAP and t-distributed stochastic neighbor embeddings. Topic modeling was performed as described elsewhere (33 (link)). Interactome analysis was performed using the SingleCellSignalR package (56 (link)).
Sorini C., Tripathi K.P., Wu S., Higdon S.M., Wang J., Cheng L., Banerjee S., Reinhardt A., Kreslavsky T., Thorell A., Engstrand L., Du J, & Villablanca E.J. (2023). Metagenomic and single-cell RNA-Seq survey of the Helicobacter pylori–infected stomach in asymptomatic individuals. JCI Insight, 8(4), e161042.
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Publication 2023
A 033 Cell Cycle Cells Cell Surface Proteins Gene Expression Genes Genes, Immunoglobulin Genome Mitochondria Ribosomes Stomach
5
Visualizing Endosome Localization of HA-tagged I329L
Vero cells grown on coverslips were transfected using X-treme9 (Roche) with pcDNA3-HA empty vector or pcDNA3-I329L-HA and EEA1 Ct-tomato plasmid (to visualize early endosome marker). At 48 h post-transfection, the cells were fixed with 4% paraformaldehyde in PBS for 15 min at room temperature. The cells were permeabilized with PBS containing 0.1% Triton X-100 for 20 min, washed and blocked with PBS containing 5% normal goat serum and 0.05% Tween 20 for 30 min. In an alternative protocol, the fixation and permeabilization step were omitted in order to stain cell surface proteins. The cells were then incubated with a rat monoclonal anti-HA (SIGMA, St. Louis, MO, USA), and then anti-mouse cy5 (Jackson, Chicago, IL, USA) to visualize the HA tagged I329L, and the cell nuclei were stained with DAPI.
Correia S., Moura P.L., Ventura S., Leitão A, & Parkhouse R.M. (2023). I329L: A Dual Action Viral Antagonist of TLR Activation Encoded by the African Swine Fever Virus (ASFV). Viruses, 15(2), 445.
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Publication 2023
Cell Nucleus Cells Cell Surface Proteins Cloning Vectors DAPI Endocytic Vesicles Goat Lycopersicon esculentum Mus paraform Plasmids Serum Transfection Triton X-100 Tween 20 Vero Cells

Top products related to «Cell Surface Proteins»

1
Pierce cell surface protein isolation kit by Thermo Fisher Scientific
Sourced in United States
The Pierce Cell Surface Protein Isolation Kit is a laboratory product designed to isolate and purify cell surface proteins from mammalian cells. It utilizes a biotinylation reagent and streptavidin-coated beads to selectively capture and extract cell surface proteins from cell lysates.
2
Ez link sulfo nhs ss biotin by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Canada
EZ-Link Sulfo-NHS-SS-Biotin is a water-soluble, cleavable biotinylation reagent. It attaches a biotin group to primary amines on proteins, enabling their detection and purification using streptavidin.
3
Facscalibur by BD
Sourced in United States, Germany, United Kingdom, China, Canada, Japan, Italy, France, Belgium, Singapore, Uruguay, Switzerland, Spain, Australia, 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.
4
Sulfo nhs ss biotin by Thermo Fisher Scientific
Sourced in United States, United Kingdom
Sulfo-NHS-SS-Biotin is a water-soluble, amine-reactive biotinylation reagent. It is used for the reversible labeling of proteins and other biomolecules containing primary amines.
5
Facscanto 2 by BD
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The FACSCanto II is a flow cytometer instrument designed for multi-parameter analysis of single cells. It features a solid-state diode laser and up to four fluorescence detectors for simultaneous measurement of multiple cellular parameters.
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Ez link sulfo nhs lc biotin by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, France
EZ-Link Sulfo-NHS-LC-Biotin is a water-soluble, amine-reactive biotinylation reagent. It is used to label proteins and other macromolecules with biotin, enabling detection and purification.
7
Cell surface protein isolation kit by Thermo Fisher Scientific
Sourced in United States
The Cell Surface Protein Isolation Kit is a laboratory tool designed to isolate cell surface proteins from biological samples. It provides a standardized method for the extraction and purification of cell surface proteins, which are important for various applications in cell biology, immunology, and proteomics research.
8
Guava by Merck Group
Sourced in Germany, United States, United Kingdom
The Guava is a compact, high-performance flow cytometry system designed for cell analysis. It offers automated sample processing, data acquisition, and analysis capabilities to support a variety of applications in life science research.
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Tripsin edta by Merck Group
Sourced in United States
Trypsin/EDTA is a cell culture reagent used to dissociate adherent cells from a culture substrate. Trypsin is a proteolytic enzyme that cleaves the proteins that hold cells together, while EDTA chelates divalent cations that are necessary for cell-cell and cell-substrate adhesion. This combination facilitates the detachment of cells from the culture surface, allowing for cell passaging, harvesting, or other downstream applications.
10
Protease inhibitor cocktail by Roche
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Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.

More about "Cell Surface Proteins"

Cell surface proteins, also known as transmembrane proteins or membrane proteins, are a class of integral membrane proteins that are expressed on the outer surface of cells.
These proteins play a crucial role in a wide range of biological processes, including cell signaling, adhesion, recognition, and interaction with the extracellular environment.
Cell surface proteins can serve as receptors, transporters, and enzymes, mediating the communication and exchange of information between cells and their surroundings.
Understanding the expression and function of these proteins is essential for studying cellular physiology, development, and pathological conditions.
Researchers can utilize various tools and techniques to investigate cell surface proteins, such as the Pierce Cell Surface Protein Isolation Kit, EZ-Link Sulfo-NHS-SS-Biotin, and FACSCalibur flow cytometer.
These tools can be used to isolate, label, and analyze cell surface proteins, providing valuable insights into their structure, function, and distribution.
Additionally, the EZ-Link Sulfo-NHS-LC-Biotin and Cell Surface Protein Isolation Kit can be employed to selectively label and purify cell surface proteins, while the FACSCanto II flow cytometer can be used for high-throughput analysis and sorting of cells based on their surface protein expression.
The Guava system, a compact flow cytometer, and the Tripsin/EDTA enzyme solution, along with a protease inhibitor cocktail, are also commonly used in cell surface protein research to dissociate and prepare cells for analysis.
By leveraging these tools and techniques, researchers can optimize their cell surface protein research, identify the best protocols and products from literature, preprints, and patents, and enhance the reproducibility and accuracy of their findings.
This data-driven approach, powered by AI-driven tools like PubCompare.ai, enables researchers to experience the future of biological research today.