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MS Bioworks

Ann Arbor, Michigan, US

MS Bioworks is a state of the art protein mass spectrometry service provider delivering the highest quality data to Industrial and government organizations and academic institutions. We believe in developing long term relationships with our clients and partnering for our mutual success. Whether you are trying to identify a protein, discover new biomarkers or characterize the glycoforms of a therapeutic protein let us be your partner in innovation.

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Biomarker Analysis
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MRM Assay
LC-MS/MS
Biomarker Discovery
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LC-MS
Liquid Chromatography-Coupled Mass Spectrometry
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Proteins are digested with trypsin and the resulting peptides are analyzed by LC/MS/MS. The peptides are fragmented in the mass spectrometer to yield diagnostic patterns that can be matched to protein sequence databases via computer algorithms. The sensitivity of this technique is 1ng or less starting material for a given protein.

Proteins are digested with trypsin and the resulting peptides are analyzed by LC/MS/MS. The peptides are fragmented in the mass spectrometer to yield diagnostic patterns that can be matched to protein sequence databases via computer algorithms. The sensitivity of this technique is 1ng or less starting material for a given protein.

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Label-Free Mass Spectrometry
Starting at $775.00 per sample

This service enables the quantitative and qualitative analysis of complex samples such as cell lysates, tissue homogenates or biofluids. The results from this experiment provide a catalogue of the proteins present in all samples and a statistical analysis reflecting the changes in the protein levels observed across the samples, along with associated pathway information.

This service enables the quantitative and qualitative analysis of complex samples such as cell lysates, tissue homogenates or biofluids. The results from this experiment provide a catalogue of the proteins present in all samples and a statistical analysis reflecting the changes in the protein levels observed across the samples, along with associated pathway information.

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Molecular Mass Measurement
Starting at $390.00 per sample

This service enables the determination of the molecular weight of a protein. High purity samples are required

This service enables the determination of the molecular weight of a protein. High purity samples are required

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MRM/SRM
Multiple Reaction Monitoring/Selected Reaction Monitoring Mass Spectrometry
Starting at $9,500.00 per sample

Liquid Chormatography-Selected Reaction Monitoring/Mass Spectrometry (LC-SRM/MS) is a technique commonly associated with the selective and sensitive detection of small molecules (<1000Da). The technique is commonplace in the clinical, pharmaceutical and environmental monitoring fields and is recognized for enabling robust, high... Show more »

Liquid Chormatography-Selected Reaction Monitoring/Mass Spectrometry (LC-SRM/MS) is a technique commonly associated with the selective and sensitive detection of small molecules (<1000Da). The technique is commonplace in the clinical, pharmaceutical and environmental monitoring fields and is recognized for enabling robust, high throughput assays. LC-SRM/MS is an emerging technology for the quantitation of proteins. The principle underlying this approach is one of surrogacy; a proteolytic peptide produced from the enzymatic digestion of a protein can be monitored and quantified using LC-SRM/MS. The calculated molar amount of the surrogate peptide can be used to infer the concentration of the protein, assuming a 1:1 mole ratio between the peptide and the protein. This method offers an opportunity to dramatically reduce assay development times for proteins of interest and has all of the positive attributes associated with small molecule applications.

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N-Glycosylation Screening
Starting at $1,000.00 per sample

This screening service can be used to determine presence or absence of N-glycosylation sites on an antibody, recombinant or highly purified protein. Modified asparagine (Asn) residues are converted to the deamidated aspartic acid (Asp) following treatment with PNGase F, this is a simple modification to pick up in a database... Show more »

This screening service can be used to determine presence or absence of N-glycosylation sites on an antibody, recombinant or highly purified protein. Modified asparagine (Asn) residues are converted to the deamidated aspartic acid (Asp) following treatment with PNGase F, this is a simple modification to pick up in a database search. Analysis without treatment accounts for any artifactual deamidation.

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Peptide mapping
Starting at $800.00 per sample

This service involves processing your sample with multiple enzymes (trypsin, chymotrypsin and elastase) prior to LC/MS/MS analysis. Post-acquisition protein and peptide identification data are reported for individual enzymes and also compiled to give the summed data from all three enzymes. This approach maximizes the sequence coverage observed for your protein(s).

This service involves processing your sample with multiple enzymes (trypsin, chymotrypsin and elastase) prior to LC/MS/MS analysis. Post-acquisition protein and peptide identification data are reported for individual enzymes and also compiled to give the summed data from all three enzymes. This approach maximizes the sequence coverage observed for your protein(s).

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Phosphoproteomics
Starting at $2,400.00 per sample

This targeted workflow uses peptide level TiO2 enrichment to select for phosphorylated species. The phosphorylated peptides may be profiled in a single sample or monitored for differential analysis across multiple samples.

This targeted workflow uses peptide level TiO2 enrichment to select for phosphorylated species. The phosphorylated peptides may be profiled in a single sample or monitored for differential analysis across multiple samples.

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Post-Translational Modification Analysis
Starting at $310.00 per sample

This service is used to detect post-translational modifications (PTMs) on proteins. The service can be applied to purified proteins, recombinant proteins or proteins in complex mixtures. Samples should be submitted as gel bands. The range of modifications is limited to those readily identifiable in a database search, such as... Show more »

This service is used to detect post-translational modifications (PTMs) on proteins. The service can be applied to purified proteins, recombinant proteins or proteins in complex mixtures. Samples should be submitted as gel bands. The range of modifications is limited to those readily identifiable in a database search, such as methylation of lysine or arginine, ubiquitination of lysine, deamidation of glutamine or asparagine, glycation of lysine, phosphorylation of serine, threonine or tyrosine (without enrichment), or acetylation of lysine.

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Protein Identification
Starting at $250.00 per sample

in gel digest

in gel digest

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SILAC
Stable Isotope Labeling by Amino Acids in Cell Culture
Starting at $4,100.00 per sample

This service is designed for the quantitative and qualitative analysis of cell based systems. The results from this experiment provide a catalogue of the proteins present in all samples and a statistical analysis reflecting the changes in the protein levels observed across the samples, along with associated pathway... Show more »

This service is designed for the quantitative and qualitative analysis of cell based systems. The results from this experiment provide a catalogue of the proteins present in all samples and a statistical analysis reflecting the changes in the protein levels observed across the samples, along with associated pathway information.

Stable isotope labeling with amino acids in cell culture (SILAC) is a quantitative proteomics technique that involves the incorporation of a label into proteins in vitro prior to analysis by LC/MS/MS. Cells are labeled during the culturing process using media containing light or heavy amino acids, the heavy amino acids have stable isotope atoms incorporated e.g. lysine (13C6H1215N2O) or arginine (13C6H1215N4O2). The labeled amino acids are used in protein synthesis, after several passages the labeled residues have been fully incorporated into the proteins. The labeled amino acids are equivalent to their unlabeled counterparts and their presence has no impact on the biological system.

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Tandem Mass Tags
Tandem Mass Tags
Starting at $7,875.00 per sample

Chemical labeling methods such as iTRAQ and TMT enable increased throughput in quantitative proteomics experiments. Samples are digested with trypsin and are subsequently labeled with isobaric tagging reagents, tagged samples are then pooled prior to analysis. The tag chemistry is such that tagged peptides from different samples... Show more »

Chemical labeling methods such as iTRAQ and TMT enable increased throughput in quantitative proteomics experiments. Samples are digested with trypsin and are subsequently labeled with isobaric tagging reagents, tagged samples are then pooled prior to analysis. The tag chemistry is such that tagged peptides from different samples in a pool will have the same precursor ion m/z and under collision induced dissociation conditions will yield diagnostic tag specific reporter ions that can be used for quantitation. Thus a peptide fragmentation spectrum contains not only information on the identity of the peptide but also information on the relative amounts of that peptide in each pooled sample. Data processing software is used to interpret the peptide level data and report quantitative results for detected proteins.

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iTRAQ Protein Labeling
Isobaric Tags for Relative and Absolute Quantitation
Starting at $9,200.00 per sample

Chemical labeling methods such as iTRAQ and TMT enable increased throughput in quantitative proteomics experiments. Samples are digested with trypsin and are subsequently labeled with isobaric tagging reagents, tagged samples are then pooled prior to analysis. The tag chemistry is such that tagged peptides from different samples... Show more »

Chemical labeling methods such as iTRAQ and TMT enable increased throughput in quantitative proteomics experiments. Samples are digested with trypsin and are subsequently labeled with isobaric tagging reagents, tagged samples are then pooled prior to analysis. The tag chemistry is such that tagged peptides from different samples in a pool will have the same precursor ion m/z and under collision induced dissociation conditions will yield diagnostic tag specific reporter ions that can be used for quantitation. Thus a peptide fragmentation spectrum contains not only information on the identity of the peptide but also information on the relative amounts of that peptide in each pooled sample. Data processing software is used to interpret the peptide level data and report quantitative results for detected proteins.

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Mass Spectrometry
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Spectroscopy
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Omics
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Protein Sequencing
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Protein Services
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Biology
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Protein Characterization Services
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Proteomics
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Imaging & Spectroscopy
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Physical Analysis Methods
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Mass and Weight Analysis
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Tandem Mass Spectrometry Methods
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Liquid Chromatography Coupled Mass Spectrometry Methods
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Engineering & Devices
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Pharmacology & Toxicology
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Bioanalysis
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Biomarkers
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Biochemistry & Molecular Biology
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Specialty Mass Spectrometry Methods
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2017-12-19 11:42:43 -0500

Net Promoter Score of 10 received for Protein Identification.

Additional Ratings: satisfaction with deliverable: 10, satisfaction with timeliness: 10.

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