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T6567

Trypsin Protease

Hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues, suitable for mass spectrometry, from Porcine pancreas

Synonym(s):

Porcine Trypsin, Trypsin for Mass Spectropetry

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5 x 20 μg
Ships within 2 weeks. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)
$99.40
20 μg
Ships within 2 weeks. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)
$101.00
1 mg
Ships within 2 weeks. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)
$920.00

About This Item

UNSPSC Code:
12352204
NACRES:
NA.56
EC Number:
232-650-8
MDL number:
Biological source:
Porcine pancreas

$99.40


Ships within 2 weeks. (Orders outside of US and Europe, please allow an additional 1-2 weeks for delivery)

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Product Name

Trypsin from porcine pancreas, Proteomics Grade, BioReagent, Dimethylated

biological source

Porcine pancreas

Quality Segment

product line

BioReagent

solubility

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

shipped in

wet ice

storage temp.

2-8°C

General description

Trypsin is a serine protease that is usually used in biochemistry and biology as an important enzymatic reagent.[1] 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[2]
  • Electrospray Ionization Mass Spectrometry (ESI-MS) analysis[3]
  • Surface proteome profiling of L. plantarum[4]
  • Gel Filtration, Ultracentrifugation, and Rotary Shadowing Electron Microscopy[5]
  • Mass spectrometry[6][7]

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.[8] Trypsin acts as a cell culture tool. It is used to hydrolyze allergenic proteins to produce hypoallergenic milk in industries.[1]

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This Item
T4799T0303T7168
biological source

Porcine pancreas

biological source

Porcine pancreas

biological source

-

biological source

Porcine pancreas

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

shipped in

wet ice

shipped in

ambient

shipped in

-

shipped in

-

solubility

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

solubility

-

solubility

-

solubility

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

product line

BioReagent

product line

BioReagent

product line

-

product line

-


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pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves



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Protocols

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

Articles

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.

Pretreatment with Mucinase StcE increases glycopeptide identification from mucin samples, enhancing sample preparation efficiency for glycopeptide analysis.

Get better detection and quantification of proteases with this high-sensitivity red protease detection assay.

View All Articles





Global Trade Item Number

SKUGTIN
T6567-20UG04061835519132
T6567-1MG04061835491971
T6567-5X20UG04061835575015

Questions

1–6 of 6 Questions  
  1. What can I use to solubilize this Product T6567, Trypsin from porcine pancreas?

    1 answer
    1. This product is soluble in 1mM HCL.

      Helpful?

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

    1 answer
    1. 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.

      Helpful?

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

    1 answer
    1. Each vial content 20 ug of the product.

      Helpful?

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

    1 answer
    1. 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.

      Helpful?

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

    1 answer
    1. 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.

      Helpful?

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

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

      Helpful?

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