KMD Bioscience Co., Ltd.
400-621-6806
Service Line：+1-315-239-3085
Address：FL-4, Building A5, International Enterprise Community, Tianjin, China
Email：info@kmdbioscience.com
KMD Bioscience is not only a company specializing in the synthesis of various modified peptides, but also provides a range of peptide analysis services to support your different needs. Physical testing can reflect the performance at the macro level, while chemical analysis focuses more on the microstructure, elemental composition and spectral characteristics. Both physical testing and chemical analysis are available, depending on your requirements.
The analytical services we can provide include but are not limited to:
Peptide Identification
KMD Bioscience has developed a comprehensive peptide identification pathway, including sample preparation, peptide isolation and purification, and finally mass spectrometry technology platform for quality analysis. And this channel is being optimized all the time.
Net Peptide Content Determination
The net peptide content can be determined by amino acid analysis and elemental analysis in a small dosage. Experimental results reflect the variability between peptide batches.
Peptide Purity Determination
The purity of the peptide was determined by HPLC analysis, and the detection wavelength was 220nm, peptide bond absorbed here. The technique is used to separate, identify and quantify components in mixtures, such as target peptides and potential impurities.
Peptide Molecular Weight Determination
We usually use mass spectrometry to analyze the molecular weight of peptides. Different ion sources and mass spectrometry types will be selected according to the properties of different peptides and their associated detectability. For example, MALDI-TOF, ion trap or quadrupole.
Peptide Sequencing
Two common peptide sequencing methods are used: short peptides (less than 30 amino acids) are directly shredded by secondary mass spectrometry, and the peptide sequence is deduced from the data obtained. Long peptides are identified after enzyme digestion, that is, by de novo sequencing. Some peptide mixtures can also be sequenced based on the above method.
Peptide Charge identification (isoelectric point)
Accurate determination of isoelectric points is often used as an effective method to identify peptides. The isoelectric points of a particular peptide are fixed, which is related to the composition and conformation of the peptide. KMD Bioscience can accurately determine the isoelectric point based on capillary isoelectric focusing (cIEF). This method has the advantages of high short-term efficiency, high precision and small sample size.
Peptide & Building Block Structure Confirmation
For precise structural identification of very small peptides and components, KMD Bioscience usually uses NMR. This process is mainly based on the different chemical environments of 1H and 13C to obtain experimental data.
Peptide Solubility Testing
According to the application of the target peptide, different organic solvents can be selected, and the solubility can be determined by TSA.
Peptide Stability Testing
KMD Bioscience is equipped with high-precision stability chambers, and we can come up with different solutions, from influencing factor experiments to short-term storage conditions to long-term stability studies that meet ICH standards.
Residual Solvent (e.g., DMF, Acetonitrile, DMSO, NMP…) Determination
Most of the solvents left during the synthesis and purification of peptides are cytotoxic and may lead to erroneous results during application. KMD Bioscience uses gas chromatography to determine the residual solvent, and then calculate the content by external standard method.
Residual Water Determination
Lyophilized peptides are more stable at lower water content. KMD Bioscience provides gas chromatography for the determination of residual moisture in peptides.
Residual Counter-Ion (e.g., TFA, HCl, HOAc) Determination
Due to the chemical properties of polypeptides, the protonated amino functional groups of lyophilized peptides may still contain countervator ions. Ion chromatography can be used to analyze the amount of residual countervator ions in synthesized peptides to determine the accurate content of lyophilized peptides.
Disulfide Bridges Determination
Disulfide bonds play an important role in the structure and function of proteins as the basis of single-shift folding. The analysis of disulfide bonds is also of great significance. KMD Bioscience provides services to map unknown protein disulfide bond locations and validate disulfide bond structures in protein samples. The basic steps include peptide extraction, peptide isolation, and data analysis.
Charge Variant Analysis
Charge heterogeneity may be caused by sequence variations (such as C-terminal lysine clamp), chemical degradation products (such as deamidation), and some post-modifications. We analyze the protein charge by ion exchange chromatography.
Peptide Crystallization
Peptide crystals can produce ordered crystals with uniform content, reasonable and stable conformation, and retain natural structure and function. KMD Bioscience can provide small peptide crystals.
Our Advantages:
-- Highly skilled and committed scientific staff
-- Corresponding cost-effective analytical services
-- Analysis techniques include LC-MS/MS, MALDI-MS, HPLC, AAA, NMR
-- Mass spec analysis and HPLC chromatogram
-- Free peptide consultation and design
How to Order?
If you have any questions regarding our services or products, please feel free to contact us by E-mail: info@kmdbioscience.com or Tel: +86-400-621-6806;
FL-4, Building A5, International Enterprise Community, Tianjin, China
Email：info@kmdbioscience.com
Hot Line： +1-315-239-3085
Technical Support：sales@kmdbiosci.com