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T6567

Sigma-Aldrich

Trypsin from porcine pancreas

Proteomics Grade, BioReagent, Dimethylated

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Synonym(s):
Porcine Trypsin, Trypsin for Mass Spectropetry
EC Number:
232-650-8
MDL number:
MFCD01775455
NACRES:
NA.56

biological source

Porcine pancreas

product line

BioReagent

solubility

1 mM HCl: soluble 1 mg/mL, clear, colorless

shipped in

wet ice

storage temp.

2-8°C

Related Categories

General description

Trypsin is a serine protease that is usually used in biochemistry and biology as an important enzymatic reagent. This method produces a highly purified trypsin product suitable for proteomics research. Proteomics Grade ideal for use in both solution and in-gel tryptic digestions. Trypsin, a serine protease, is present in the digestive system of several vertebrates.

Application

Trypsin from porcine pancreas is used for the following applications:
  • In-gel protein digestion and MALDI-TOF mass spectrometry analysis
  • Electrospray Ionization Mass Spectrometry (ESI-MS) analysis
  • Surface proteome profiling of L. plantarum
  • Gel Filtration, Ultracentrifugation, and Rotary Shadowing Electron Microscopy
  • Mass spectrometry

Biochem/physiol Actions

Trypsin is routinely used in proteomics research for peptide mapping and protein sequence work, due to its highly specific cleavage resulting in a limited number of tryptic peptides. It hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues.. The enzyme also exhibits esterase and amidase activities. Trypsin acts as a cell culture tool. It is used to hydrolyze allergenic proteins to produce hypoallergenic milk in industries.

related product

Product No.
Description
Pricing

Pictograms

Exclamation markHealth hazard
GHS07,GHS08

Signal Word

Danger

Hazard Statements

H315 - H319 - H334 - H335

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

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  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  4. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. What can I use to solubilize this Product T6567, Trypsin from porcine pancreas?

    This product is soluble in 1mM HCL.

  6. What is the package size of Product T6567, Trypsin from porcine pancreas?

    Each vial content 20 ug of the product.

  7. Is Product T6567, Trypsin from porcine pancreas, TPCK treated?

    The product has been treated with TPCK to remove chymotryptic activity, further purified through affinity chromatography, and lyophilized, resulting in convenient use and highly specific cleavage. This information is on the product page under application.

  8. How can we get Trypsin sequence information for Product T6567, Trypsin from porcine pancreas?

    If you are looking for trypsin sequence information, you have to go to the NCBI Protein Data Bank.

  9. How can we digest protein using Product T6567, Trypsin from porcine pancreas?

    As per Sigma R and D the information is as follows: In order to efficiently digest a protein with trypsin, it must be denatured and the disulfide bonds modified by reduction and alkylation, or at least reduced. Many intact proteins are highly resistant to digestion with trypsin. If you do not want to reduce and alkylate, you can then just boil the protein with 5 mM DTT or 20 mM 2ME for 10 minutes, and then quickly cool on ice to denature the protein. This may result in a precipitate, but the trypsin will still digest the protein and it will clear within an hour or two. You can also dissolve the protein in 6 M guanidine-HCl or 8 M urea. Reduce and alkylate using the PROT-RA kit or other suitable method. Then they would have to dilute the solution to less than 2 M of either denaturant and then add the trypsin. This is the method that we use routinely in the lab.

  10. My question is not addressed here, how can I contact Technical Service for assistance?

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Pauline Floch et al.
Gut pathogens, 6, 20-20 (2014-07-06)
A gamma-glutamyl transpeptidase (GGT) is produced by up to 31% of strains of Campylobacter jejuni isolates. C. jejuni GGT is close to Helicobacter pylori GGT suggesting a conserved activity but unlike the latter, C. jejuni GGT has not been studied
Yusuke Murasawa et al.
The Journal of biological chemistry, 288(40), 29170-29181 (2013-08-22)
Versican G1 domain-containing fragments (VG1Fs) have been identified in extracts from the dermis in which hyaluronan (HA)-versican-fibrillin complexes are found. However, the molecular assembly of VG1Fs in the HA-versican-microfibril macrocomplex has not yet been elucidated. Here, we clarify the role
Daniela M Remus et al.
Journal of bacteriology, 195(3), 502-509 (2012-11-24)
Sortases are transpeptidases that couple surface proteins to the peptidoglycan of Gram-positive bacteria, and several sortase-dependent proteins (SDPs) have been demonstrated to be crucial for the interactions of pathogenic and nonpathogenic bacteria with their hosts. Here, we studied the role
Hui Zheng et al.
Molecules (Basel, Switzerland), 18(11), 13425-13433 (2013-11-02)
A novel chemoenzymatic one-pot multicomponent synthesis of thiazole derivatives was developed. A series of thiazole derivatives were synthesized with high yields up to 94% under mild enzyme-catalyzed conditions. The blank and control experiments reveal that trypsin from porcine pancreas (PPT)
Maciej Suski et al.
Biochimica et biophysica acta, 1834(12), 2463-2469 (2013-08-31)
Excessive action of angiotensin II on mitochondria has been shown to play an important role in mitochondrial dysfunction, a common feature of atherogenesis and kidney injury. Angiotensin-(1-7)/Mas receptor axis constitutes a countermeasure to the detrimental effects of angiotensin II on
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Articles

Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays

Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays

Validation of RNAi Knockdown Using Multiple Reaction Monitoring and Protein-AQUA

The field of proteomics is continually looking for new ways to investigate protein dynamics within complex biological samples. Recently, many researchers have begun to use RNA interference (RNAi) as a method of manipulating protein levels within their samples, but the ability to accurately determine these protein amounts remains a challenge. Fortunately, over the past decade, the field of proteomics has witnessed significant advances in the area of mass spectrometry. These advances, both in instrumentation and methodology, are providing researchers with sensitive assays for both identification and quantification of proteins within complex samples. This discussion will highlight some of these methodologies, namely the use of Multiple Reaction Monitoring (MRM) and Protein-AQUA.

Protocols

Procedure for Enzymatic Assay of Trypsin (EC 3.4.21.4)

This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).

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