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L-Lysine-2HCl, 4,4,5,5-D4 for SILAC (Thermo Scientific™)

Thermo Scientific Heavy and Light Amino Acids are used to specifically analyze protein expression by mass spectrometry using stable isotope labeling with amino acids in cell culture (SILAC) quantification kits. This is a lyophilized preparation of L-Lysine-2HCl (4,4,5,5-D4), sufficient for 10 SILAC experiments.

General features of heavy and light amino acids for SILAC labeling:

Efficient—100% label incorporation into proteins of living cells
Flexible—different isotopes of heavy and/or light amino acids for arginine, lysine, leucine and proline enable the quantitation of peptides derived from MS-grade proteases
Multiplex capabilities—several alternative isotopes of arginine and lysine are available that allow the analysis of multiple treatment conditions in each experiment
High-quality supplements—heavy amino acids with >99% isotope purity

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

Thermo Scientific Heavy and Light Amino Acids for SILAC are used together with specialized cell culture media that are deficient in essential amino acids. Heavy and light L-lysine and L-arginine are the most common amino acids used for SILAC analysis of tryptic peptides. Up to three different experimental conditions can be readily analyzed with different isotopes of lysine and arginine. For lysine three-plex experiments, 4,4,5,5-D4 L-lysine and 13C6 15N2 L-lysine are used to generate peptides with 4- and 8-Da mass shifts, respectively, compared to peptides generated with light lysine. For arginine three-plex experiments, 13C6 L-arginine and 13C6 15N4 L-arginine are used to generate peptides with 6- and 10-Da mass shifts, respectively, compared to peptides generated with light arginine. L-leucine is another amino acid commonly used for SILAC labeling, because it is one of the most common amino acids found in protein sequences. Proline is a non-essential amino acid that is sometimes added to SILAC media to prevent the metabolic conversion of heavy arginine to heavy proline in mammalian cell lines with high arginine dehydrogenase activity.

Related Products
L-Arginine-HCl for SILAC
L-Proline for SILAC
L-Leucine for SILAC
L-Lysine-2HCl for SILAC

SILAC Protein Quantitation Kit - DMEM:F12 (Thermo Scientific™)

Thermo Scientific SILAC Protein Quantitation Kit - DMEM:F12 is used for the specific analysis of protein expression by mass spectrometry using stable isotope labeling with amino acids in cell culture (SILAC).

Features of SILAC Protein Quantitation Kit - DMEM:F12:

Efficient—100% label incorporation into proteins of living cells
Reproducible—eliminates intra-experimental variability caused by differential sample preparation
Flexible—media deficient in both L-lysine and L-arginine, allowing for more complete proteome coverage through dual amino acid isotope labeling
Compatible—label proteins expressed in a wide variety of mammalian cell lines adapted to grow in DMEM:F12 medium, including HeLa, 293T, COS7, U2OS, A549, A431, HepG2, NIH 3T3, Jurkat and others
High-quality supplements—heavy amino acids with >99% isotope purity; dialyzed FBS tested to ensure that it is sterile, endotoxin-free, and cell culture compatible

Applications of SILAC Protein Quantitation Kit:
• Quantitative analysis of relative changes in protein abundance from different cell treatments
• Quantitative analysis of proteins for which there are no antibodies available
• Protein expression profiling of normal vs. disease cells
• Identification and quantification of hundreds to thousands of proteins in a single experiment

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

Because peptides labeled with heavy and light amino acids are chemically identical, they co-elute during reverse-phase column pre-fractionation and therefore are detected simultaneously during MS analysis. The relative peak intensities of multiple isotopically distinct peptides from each protein are then used to determine the average change in protein abundance in the treated sample.

Each kit includes all necessary reagents to isotopically label cells with 13C6 L-lysine-2HCl, including media, heavy and light amino acids and dialyzed serum. Heavy L-arginine-HCl derivatives (Part No. 88210, 89990) are available separately and can be combined with Pierce SILAC Protein Quantitation Kits to enhance peptide isotope label coverage. Kits are compatible with mammalian cell lines adapted to grow in either DMEM or RPMI 1640 media. Kits with specialized media formulations are also available for human and murine stem cell lines. When combined with Thermo Scientific Protein/Peptide Sample Enrichment Products, Pierce SILAC Protein Quantitation Kits also enable MS analysis of low-abundance proteins such as cell surface proteins, organelle-specific proteins and post-translational protein modifications such as phosphorylation or glycosylation.

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SILAC Protein Quantitation Kit – RPMI 1640
SILAC Protein Quantitation Kit – DMEM

IMDM for SILAC (Thermo Scientific™)

Thermo Scientific™ IMDM for SILAC is optimized for use with stable isotope labeling with amino acids in cell culture (SILAC) to analyze protein expression by mass spectrometry (MS).

Features of IMDM for SILAC:
• Flexible—liquid media deficient in both L-lysine and L-arginine, allowing for more complete proteome coverage through multiple isotopic amino acid labeling
• High quality—medium is sterile, endotoxin-free, and cell culture-compatible

SILAC is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization, and quantitation of proteins.

This SILAC medium is used together with heavy and light amino acids for the differential isotopic labeling of cells for SILAC analysis. SILAC media supplemented with heavy amino acids are capable of nearly 100% label incorporation into proteins of living cells.

Related products
NeuCode™ Lysine -080, 50 mg
Fetal Bovine Serum, dialyzed, US origin
DMEM for SILAC

McCoy's 5A Media for SILAC (Thermo Scientific™)

Thermo Scientific McCoy's 5A Media for SILAC is optimized for use with stable isotope labeling with amino acids in cell culture (SILAC) to analyze protein expression by mass spectrometry (MS).

Features of McCoy's 5A Media for SILAC:

Flexible—liquid media deficient in both L-lysine and L-arginine, allowing for more complete proteome coverage through multiple isotopic amino acid labeling
High quality—media are sterile, endotoxin-free and cell culture-compatible

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

This SILAC media is used together with heavy and light amino acids for the differential isotopic labeling of cells for SILAC analysis. SILAC media supplemented with heavy amino acids are capable of nearly 100% label incorporation into proteins of living cells.

NeuCode™ Lysine 4-plex Bundle (Thermo Scientific™)

Thermo Scientific NeuCode amino acids augment the level of multiplexing achievable for the metabolic labeling of proteins for mass spectrometry analysis. The NeuCode Lysine 4-plex Bundle utilizes four heavy lysines to increase the level of multiplexing for SILAC to four samples.

Features of NeuCode Lysine 4-plex labeling:
• Labeling efficiency—100% label incorporation into proteins of living cells without toxicity
• Improved multiplexing—uses a combination of four heavy lysines for higher multiplexing
• Time-saving—100% label incorporation not necessary when using only heavy amino acids
• High-quality supplements—heavy amino acids with >97% isotope purity

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. NeuCode metabolic labeling is similar to SILAC, but differs in that the labeling only utilizes heavy amino acids. The increased multiplexing capability of NeuCode amino acids is possible through the use of mass defects from extra neutrons in the stable isotopes. These small mass differences may be resolved on high resolution mass spectrometers (Thermo Scientific™ Orbitrap™ Elite™, Orbitrap™ Fusion™ Tribrid™, and Orbitrap™ Fusion™ Lumos™ Tribrid™ mass spectrometers). Use of only heavy amino acids eliminates the need for 100% incorporation of amino acids used for SILAC (both heavy and light), and may be especially useful for studies with primary cells.

The NeuCode Lysine 4-plex Bundle contains NeuCode Lysine-080, NeuCode Lysine-602, NeuCode Lysine-440, and NeuCode Lysine-521, which are used together with specialized cell culture media that are deficient in essential amino acids to isotopically label proteins. Heavy lysine-labeled proteins are typically digested with trypsin or LysC proteases for peptide quantitation using high resolution mass spectrometry.

Related products
NeuCode Lysine-080
NeuCode Lysine-602
NeuCode Lysine-440
NeuCode Lysine-521

NeuCode is a trademark of WARF.

MEM for SILAC (Thermo Scientific™)

Thermo Scientific™ MEM for SILAC is optimized for use with stable isotope labeling with amino acids in cell culture (SILAC) to analyze protein expression by mass spectrometry (MS).

Features of MEM for SILAC:
• Flexible—liquid media deficient in both L-lysine and L-arginine, allowing for more complete proteome coverage through multiple isotopic amino acid labeling
• High quality—medium is sterile, endotoxin-free, and cell culture-compatible

SILAC is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization, and quantitation of proteins.

This SILAC medium is used together with heavy and light amino acids for the differential isotopic labeling of cells for SILAC analysis. SILAC media supplemented with heavy amino acids are capable of nearly 100% label incorporation into proteins of living cells.

Related products
NeuCode™ Lysine -080, 50 mg
Fetal Bovine Serum, dialyzed, US origin
DMEM for SILAC

L-Leucine, 13C6 for SILAC (Thermo Scientific™)

Thermo Scientific Heavy and Light Amino Acids are used to specifically analyze protein expression by mass spectrometry using stable isotope labeling with amino acids in cell culture (SILAC) quantification kits. This is a lyophilized preparation of L-Leucine (13C6), sufficient for 1 SILAC experiment.

General features of heavy and light amino acids for SILAC labeling:

Efficient—100% label incorporation into proteins of living cells
Flexible—different isotopes of heavy and/or light amino acids for arginine, lysine, leucine and proline enable the quantitation of peptides derived from MS-grade proteases
Multiplex capabilities—several alternative isotopes of arginine and lysine are available that allow the analysis of multiple treatment conditions in each experiment
High-quality supplements—heavy amino acids with >99% isotope purity

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

Thermo Scientific Heavy and Light Amino Acids for SILAC are used together with specialized cell culture media that are deficient in essential amino acids. Heavy and light L-lysine and L-arginine are the most common amino acids used for SILAC analysis of tryptic peptides. Up to three different experimental conditions can be readily analyzed with different isotopes of lysine and arginine. For lysine three-plex experiments, 4,4,5,5-D4 L-lysine and 13C6 15N2 L-lysine are used to generate peptides with 4- and 8-Da mass shifts, respectively, compared to peptides generated with light lysine. For arginine three-plex experiments, 13C6 L-arginine and 13C6 15N4 L-arginine are used to generate peptides with 6- and 10-Da mass shifts, respectively, compared to peptides generated with light arginine. L-leucine is another amino acid commonly used for SILAC labeling, because it is one of the most common amino acids found in protein sequences. Proline is a non-essential amino acid that is sometimes added to SILAC media to prevent the metabolic conversion of heavy arginine to heavy proline in mammalian cell lines with high arginine dehydrogenase activity.

Related Products
L-Arginine-HCl for SILAC
L-Proline for SILAC
L-Leucine for SILAC
L-Lysine-2HCl for SILAC

DMEM:F-12 for SILAC (Thermo Scientific™)

Thermo Scientific™ DMEM:F-12 for SILAC is optimized for use with stable isotope labeling with amino acids in cell culture (SILAC) to analyze protein expression by mass spectrometry (MS).

Features of DMEM:F-12 for SILAC:
• Flexible—liquid media deficient in both L-lysine and L-arginine, allowing for more complete proteome coverage through multiple isotopic amino acid labeling
• High quality—medium is sterile, endotoxin-free, and cell culture-compatible

SILAC is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization, and quantitation of proteins.

This SILAC medium is used together with heavy and light amino acids for the differential isotopic labeling of cells for SILAC analysis. SILAC media supplemented with heavy amino acids are capable of nearly 100% label incorporation into proteins of living cells.

Related products
NeuCode™ Lysine -080, 50 mg
Fetal Bovine Serum, dialyzed, US origin
DMEM for SILAC

L-Proline for SILAC (Thermo Scientific™)

Thermo Scientific Heavy and Light Amino Acids are used to specifically analyze protein expression by mass spectrometry using stable isotope labeling with amino acids in cell culture (SILAC) quantification kits. This is a lyophilized preparation of L-Proline, sufficient for 10 SILAC experiments.

General features of heavy and light amino acids for SILAC labeling:

Efficient—100% label incorporation into proteins of living cells
Flexible—different isotopes of heavy and/or light amino acids for arginine, lysine, leucine and proline enable the quantitation of peptides derived from MS-grade proteases
Multiplex capabilities—several alternative isotopes of arginine and lysine are available that allow the analysis of multiple treatment conditions in each experiment
High-quality supplements—heavy amino acids with >99% isotope purity

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

Thermo Scientific Heavy and Light Amino Acids for SILAC are used together with specialized cell culture media that are deficient in essential amino acids. Heavy and light L-lysine and L-arginine are the most common amino acids used for SILAC analysis of tryptic peptides. Up to three different experimental conditions can be readily analyzed with different isotopes of lysine and arginine. For lysine three-plex experiments, 4,4,5,5-D4 L-lysine and 13C6 15N2 L-lysine are used to generate peptides with 4- and 8-Da mass shifts, respectively, compared to peptides generated with light lysine. For arginine three-plex experiments, 13C6 L-arginine and 13C6 15N4 L-arginine are used to generate peptides with 6- and 10-Da mass shifts, respectively, compared to peptides generated with light arginine. L-leucine is another amino acid commonly used for SILAC labeling, because it is one of the most common amino acids found in protein sequences. Proline is a non-essential amino acid that is sometimes added to SILAC media to prevent the metabolic conversion of heavy arginine to heavy proline in mammalian cell lines with high arginine dehydrogenase activity.

Related Products
L-Arginine-HCl for SILAC
L-Proline for SILAC
L-Leucine for SILAC
L-Lysine-2HCl for SILAC

L-Arginine-HCl for SILAC (Thermo Scientific™)

Thermo Scientific Heavy and Light Amino Acids are used to specifically analyze protein expression by mass spectrometry using stable isotope labeling with amino acids in cell culture (SILAC) quantification kits. This is a lyophilized preparation of L-Arginine-HCl, sufficient for 1 SILAC experiment.

General features of heavy and light amino acids for SILAC labeling:

Efficient—100% label incorporation into proteins of living cells
Flexible—different isotopes of heavy and/or light amino acids for arginine, lysine, leucine and proline enable the quantitation of peptides derived from MS-grade proteases
Multiplex capabilities—several alternative isotopes of arginine and lysine are available that allow the analysis of multiple treatment conditions in each experiment
High-quality supplements—heavy amino acids with >99% isotope purity

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

Thermo Scientific Heavy and Light Amino Acids for SILAC are used together with specialized cell culture media that are deficient in essential amino acids. Heavy and light L-lysine and L-arginine are the most common amino acids used for SILAC analysis of tryptic peptides. Up to three different experimental conditions can be readily analyzed with different isotopes of lysine and arginine. For lysine three-plex experiments, 4,4,5,5-D4 L-lysine and 13C6 15N2 L-lysine are used to generate peptides with 4- and 8-Da mass shifts, respectively, compared to peptides generated with light lysine. For arginine three-plex experiments, 13C6 L-arginine and 13C6 15N4 L-arginine are used to generate peptides with 6- and 10-Da mass shifts, respectively, compared to peptides generated with light arginine. L-leucine is another amino acid commonly used for SILAC labeling, because it is one of the most common amino acids found in protein sequences. Proline is a non-essential amino acid that is sometimes added to SILAC media to prevent the metabolic conversion of heavy arginine to heavy proline in mammalian cell lines with high arginine dehydrogenase activity.

Related Products
L-Proline for SILAC
L-Leucine for SILAC
L-Lysine-2HCl for SILAC

DMEM for SILAC (Thermo Scientific™)

Thermo Scientific™ DMEM for SILAC is optimized for use with stable isotope labeling with amino acids in cell culture (SILAC) to analyze protein expression by mass spectrometry (MS).

Features of DMEM for SILAC:
• Flexible—liquid media deficient in both L-lysine and L-arginine, allowing for more complete proteome coverage through multiple isotopic amino acid labeling
• High quality—medium is sterile, endotoxin-free, and cell culture-compatible

SILAC is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization, and quantitation of proteins.

This SILAC medium is used together with heavy and light amino acids for the differential isotopic labeling of cells for SILAC analysis. SILAC media supplemented with heavy amino acids are capable of nearly 100% label incorporation into proteins of living cells.

Related products
NeuCode™ Lysine -080, 50 mg
Fetal Bovine Serum, dialyzed, US origin
RPMI 1640 Media for SILAC

L-Leucine for SILAC (Thermo Scientific™)

Thermo Scientific Heavy and Light Amino Acids are used to specifically analyze protein expression by mass spectrometry using stable isotope labeling with amino acids in cell culture (SILAC) quantification kits. This is a lyophilized preparation of L-Leucine, sufficient for 10 SILAC experiments.

General features of heavy and light amino acids for SILAC labeling:

Efficient—100% label incorporation into proteins of living cells
Flexible—different isotopes of heavy and/or light amino acids for arginine, lysine, leucine and proline enable the quantitation of peptides derived from MS-grade proteases
Multiplex capabilities—several alternative isotopes of arginine and lysine are available that allow the analysis of multiple treatment conditions in each experiment
High-quality supplements—heavy amino acids with >99% isotope purity

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

Thermo Scientific Heavy and Light Amino Acids for SILAC are used together with specialized cell culture media that are deficient in essential amino acids. Heavy and light L-lysine and L-arginine are the most common amino acids used for SILAC analysis of tryptic peptides. Up to three different experimental conditions can be readily analyzed with different isotopes of lysine and arginine. For lysine three-plex experiments, 4,4,5,5-D4 L-lysine and 13C6 15N2 L-lysine are used to generate peptides with 4- and 8-Da mass shifts, respectively, compared to peptides generated with light lysine. For arginine three-plex experiments, 13C6 L-arginine and 13C6 15N4 L-arginine are used to generate peptides with 6- and 10-Da mass shifts, respectively, compared to peptides generated with light arginine. L-leucine is another amino acid commonly used for SILAC labeling, because it is one of the most common amino acids found in protein sequences. Proline is a non-essential amino acid that is sometimes added to SILAC media to prevent the metabolic conversion of heavy arginine to heavy proline in mammalian cell lines with high arginine dehydrogenase activity.

Related Products
L-Arginine-HCl for SILAC
L-Proline for SILAC
L-Lysine-2HCl for SILAC

NeuCode™ Lysine-341 (Thermo Scientific™)

Thermo Scientific NeuCode amino acids augment the level of multiplexing achievable for the metabolic labeling of proteins for mass spectrometry analysis. NeuCode Lysine-341 (3,4,5-13C3, 5,5,6,6-D4, 15N L-Lysine-2HCl) may also be used with traditional SILAC to improve flexibility of multiplexing options or to reduce complexity of analysis.

General features of NeuCode SILAC labeling:
• Labeling efficiency—100% label incorporation into proteins of living cells without toxicity
• Compatible—may be multiplexed with existing SILAC amino acids
• Time-saving—not necessary to label to 100% incorporation if only using heavy amino acids
• High-quality supplements—heavy amino acids with >98% isotope purity

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. NeuCode metabolic labeling is similar to SILAC, but differs in that the labeling only utilizes heavy amino acids. The increased multiplexing capability of NeuCode amino acids is possible through the use of mass defects from extra neutrons in the stable isotopes. These small mass differences may be resolved on high resolution mass spectrometers (Thermo Scientific™ Orbitrap™ Elite™, Orbitrap™ Fusion™ Tribrid™, and Orbitrap™ Fusion™ Lumos™ Tribrid™ mass spectrometers). Use of only heavy amino acids eliminates the need for 100% incorporation of amino acids used for SILAC (both heavy and light), and may be especially useful for studies with primary cells.

NeuCode amino acids are used together with specialized cell culture media that are deficient in essential amino acids. Heavy L-lysine is used for SILAC analysis of peptides that have been digested with trypsin or LysC. NeuCode Lysine-341 may be used with13C6 15N2 L-Lysine 2HCl (NeuCode Lysine-602) and NeuCode Lysine-080 for NeuCode three-plex experiments and may be combined with light lysine and 4,4,5,5-D4 L-Lysine for SILAC three-plex experiments.

Related products
L-Lysine-2HCl, 4,4,5,5-D4
13C6 15N2 L-Lysine-2HCl
NeuCode Lysine-080
Neucode Lysine-202

NeuCode is a trademark of WARF.

Powdered RPMI Media for SILAC (Thermo Scientific™)

Thermo Scientific Powdered RPMI Media for SILAC is optimized for use with stable isotope labeling with amino acids in cell culture (SILAC) to analyze protein expression by mass spectrometry (MS).

Features of Powdered RPMI Media for SILAC:

Flexible—powdered media deficient in L-leucine, L-lysine and L-arginine, allowing for more complete proteome coverage through multiple isotopic amino acid labeling
High quality—media are sterile, endotoxin-free and cell culture-compatible

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

This SILAC media is used together with heavy and light amino acids for the differential isotopic labeling of cells for SILAC analysis. SILAC media supplemented with heavy amino acids are capable of nearly 100% label incorporation into proteins of living cells.

Ham's F12 Media for SILAC (Thermo Scientific™)

Thermo Scientific Ham's F12 Media for SILAC is optimized for use with stable isotope labeling with amino acids in cell culture (SILAC) to analyze protein expression by mass spectrometry (MS).

Features of Ham's F12 for SILAC:

Flexible—liquid media deficient in both L-lysine and L-arginine, allowing for more complete proteome coverage through multiple isotopic amino acid labeling
High quality—media are sterile, endotoxin-free and cell culture-compatible

Stable isotope labeling with amino acids in cell culture (SILAC) is a powerful method to identify and quantify relative differential changes in complex protein samples. This approach entails the in vivo metabolic incorporation of "heavy" 13C- or 15N-labeled amino acids into proteins followed by mass spectrometry (MS) for the accelerated and comprehensive identification, characterization and quantitation of proteins.

This SILAC media is used together with heavy and light amino acids for the differential isotopic labeling of cells for SILAC analysis. SILAC media supplemented with heavy amino acids are capable of nearly 100% label incorporation into proteins of living cells.