>Heavy-labeled Products (MS Standards) and Services
ACROBiosystems offers heavy-labeled proteins and material generation service for customers who want to do quantification of human protein biomarkers through Mass Spectrometry (MS) analysis. The proteins are expressed through 293 cells in a chemically defined environment where the protein will be labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine. Due to the correct post-translational modifications mechanism of human cell, the proteins will be excellent identification and quantification standards.
Greater than 99.9% incorporation efficiency
Authentic posttranslational modification and protein conformation
Higher accuracy, higher consistency than synthetic peptide
Compatible with all types of MS equipments
Custom protein generation service available
Guaranteed quality and short lead-time
Greater than 99.9% incorporation efficiency,guarantee
4-6 weeks lead time from sequence to end product
Host cell has been adapted to serum free, chemically defined SILAC medium over 10 passages
Avoid residual amino acid interface in traditional approach using serum contained medium
|ACRO protein||Other Company peptide|
|Identification of best SRM and MRM transitions||Yes||No|
|PT modification and processing||Yes||No|
Case 1: rh ADAM12 MS Standard
Case 2: rh Apo-A1 MS Standard
Recombinant Human ADAM12 MS Standard Protein, C13 and N15-labeled (rhADAM12, Heavy Labeled) Arg 29 - Asp 513 (Accession # AAH60804.1) was produced through human 293 cells (HEK293) in chemically defined medium.
Recombinant Human Apo-A1 MS Standard Protein, C13 and N15-labeled (rh Apo-A1, Heavy Labeled) Asp 25 - Gln 267 (Accession # NP_000030.1) was produced through human 293 cells (HEK293) in chemically defined medium.
Stable isotope labeling by amino acids in cell culture (SILAC) is a technique based on mass spectrometry that detects differences in protein abundance among samples using non-radioactive isotopic labeling. It is a popular method for (MS)-based quantitative proteomics. SILAC labels cellular proteomes through normal metabolic processes, incorporating non-radioactive, stable isotope containing amino acids into the proteins. The method relies on the incorporation of amino acids with substituted stable isotopic nuclei (e.g. 13C, 15N). For example, the growth medium can contain arginine labeled with six carbon-13 atoms (13C), heavy amino acid, instead of the normal carbon-12 (12C), light amino acids. Cells grown in this medium incorporate the heavy amino acids after five cell doublings and SILAC amino acids have no effect on cell morphology or growth rates, they incorporate the heavy amino acid,13C6-arginine, into all of cell proteins(Figure 1).
SILAC has emerged as a very powerful method to study cell signaling, post translation modifications such as phosphorylation, protein–protein interaction and regulation of gene expression. In addition, SILAC has become an important method in secretomics, the global study of secreted proteins and secretory pathways. It can be used to distinguish between proteins secreted by cells in culture and serum contaminants. Standardized protocols of SILAC for various application have also been published.
Cells are differentially labeled by growing them in light medium with normal arginine (Arg-0, blue color) or medium with heavy arginine (Arg-6, red color). Metabolic incorporation of the amino acids into the proteins results in a mass shift of the corresponding peptides. This mass shift can be detected by a mass spectrometer as indicated by the depicted mass spectra. When both samples are combined, the ratio of peak intensities in the mass spectrum reflects the relative protein abundance. In this example, the labeled protein has the same abundance in both samples (ratio 1).
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