Heavy-labeled Full-length Proteins

    Recombinant Human IL1F10 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 IL1F10-669H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human PIK3R1 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 PIK3R1-670H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human EIF6 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 EIF6-671H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length:  1-245 aa

    Recombinant Human BCAT2 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 BCAT2-672H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human SLC34A3 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 SLC34A3-673H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human UNC5C Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 UNC5C-674H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human PHETA1 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 PHETA1-675H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human ZDHHC15 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 ZDHHC15-676H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human LRRC8A Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 LRRC8A-677H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human STARD5 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 STARD5-678H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human ASMTL Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 ASMTL-679H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human ECD Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 ECD-680H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human NOXO1 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 NOXO1-681H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human ANKS4B Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 ANKS4B-682H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

    Recombinant Human TOR1AIP2 Protein, Myc/DDK-tagged, C13 and N15-labeled

    🧪 TOR1AIP2-683H

    Source:  HEK293

    Species:  Human

    Tag:  DDK&Myc

    Conjugation: 

    Protein Length: 

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    Background

    What is isotopic labeling?

    Isotopic labeling is a technique used in chemistry and biology where one or more of the atoms in a molecule is replaced with an isotope of that atom - usually a radioactive or a stable isotope. This is often done to help trace the path of atoms through a chemical reaction or metabolic pathway, or to measure the movement or distribution of a substance within a system. It can also be used to gain information about the structure or function of a molecule.

    What is isotopic labeling

    Due to the costly manners of producing isotopic chemicals and heterologous proteins, an economic 15N/13C isotopic labeling strategy is critically in demand. Stable isotope labeling by amino acids in cell culture (SILAC) is a multiplexing quantitative proteomic method that incorporates isotopically (heavy) labeled amino acids metabolically into the whole proteome.

    Creative BioMart now offers an extensive collection of Mass Spectrometry (MS) standards for 6,000 proteins. Produced in HEK293T cells and labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, these full-length proteins with appropriate post-translational modifications are ideal identification and quantification standards.

    Advantages

    • Precision: Isotopic labeling allows for a very specific and precise identification and quantification of proteins.
    • Stability: Isotopes are chemically identical to their non-radioactive counterparts and thus do not interfere with the normal function or behavior of the protein.
    • Sensitivity: Isotopic labeling is highly sensitive and can detect even small changes in protein expression or function.
    • Non-destructive
    • Multiple Labeling: With isotopic labeling, multiple isotopes can be incorporated into the same protein, allowing for a detailed study of not only the protein's location but also its interactions with other proteins or molecules.
    • Authentic post-translational modifications
    • High data consistency
    • High reproducibility
    • Identifying the best SRM and MRM transitions
    • Suitable for most types of MS equipment
    • Over 90% incorporation efficiency

    Applications

    Structural Determination: NMR (nuclear magnetic resonance) spectroscopy and other techniques use isotopic labeling to determine the three-dimensional structure of proteins. Specifically labeled isotopes provide greater resolution and clarity in the data.

    Reaction Tracing: Isotopic labeling can track how a protein reacts or metabolizes within a system. For example, a labeled atom could be used to trace the metabolic pathway of a protein in a biological system.

    Quantification: Isotopic labeling can aid in the quantification of proteins in a complex mixture using mass spectrometry.

    Enzyme/Substrate Studies: In enzyme-substrate studies, isotopic labeling helps in identifying the mechanisms and pathways.

    Protein-Protein Interaction: Isotopic labeling is also used to study protein-protein interactions, protein folding, and dynamics.

    Biomolecular research: Isotopic labeling is fundamental for biomolecular research, including drug discovery and development.

    Protein Turnover Studies: It can be used to measure the synthesis and breakdown rates of proteins.

    It also allows for kinetic studies by helping to understand reaction rates and mechanisms.

    Related Resource