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T6567

Sigma-Aldrich

Trypsin from porcine pancreas

Proteomics Grade, BioReagent, Dimethylated

Synonym(s):

Porcine Trypsin, Trypsin for Mass Spectropetry

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20 μG
¥10,100
5 X 20 μG
¥20,200
1 MG
¥196,000

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20 μG
¥10,100
5 X 20 μG
¥20,200
1 MG
¥196,000

About This Item

EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.56

¥10,100


In StockDetails

New, lower price on this item!

Request a Bulk Order

biological source

Porcine pancreas

Quality Level

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.[2]

Application

Trypsin from porcine pancreas is used for the following applications:
  • In-gel protein digestion and MALDI-TOF mass spectrometry analysis[3]
  • Electrospray Ionization Mass Spectrometry (ESI-MS) analysis[4]
  • Surface proteome profiling of L. plantarum[5]
  • Gel Filtration, Ultracentrifugation, and Rotary Shadowing Electron Microscopy[6]
  • Mass spectrometry[7][8]

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.[2]. The enzyme also exhibits esterase and amidase activities.[9] 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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Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

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 Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

ISHL Indicated Name

Substances Subject to be Indicated Names

ISHL Notified Names

Substances Subject to be Notified Names

JAN Code

T6567-5X20UG-KC:
T6567-BULK:
T6567-5VL:
T6567PROC:
T6567-1VL:
T6567-20UG:
T6567-1MG:
T6567-5X20UG:
T6567-20UG-KC:
T6567-VAR:


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Cristina C Santini et al.
Scientific reports, 9(1), 10865-10865 (2019-07-28)
Small molecule inhibitors of BRAF and MEK have proven effective at inhibiting tumor growth in melanoma patients, however this efficacy is limited due to the almost universal development of drug resistance. To provide advanced insight into the signaling responses that
Families of serine peptidases.
N D Rawlings et al.
Methods in enzymology, 244, 19-61 (1994-01-01)
Shaoming Mao et al.
Molecular bioSystems, 7(5), 1660-1677 (2011-03-09)
The solventogenic bacterium Clostridium acetobutylicum is the most important species of Clostridium used in the fermentation industry. However, the intolerance to butanol hampers the efficient production of solvents. Butanol toxicity has been attributed to the chaotropic effect on the cell
Fredrick Van Goor et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(46), 18843-18848 (2011-10-07)
Cystic fibrosis (CF) is caused by mutations in the CF transmembrane conductance regulator (CFTR) gene that impair the function of CFTR, an epithelial chloride channel required for proper function of the lung, pancreas, and other organs. Most patients with CF
Adam W Barb et al.
Biochemistry, 48(14), 3068-3077 (2009-03-05)
The UDP-3-O-(R-3-hydroxyacyl)-N-acetylglucosamine deacetylase LpxC catalyzes the committed reaction of lipid A (endotoxin) biosynthesis in Gram-negative bacteria and is a validated antibiotic target. Although several previously described compounds bind to the unique acyl chain binding passage of LpxC with high affinity

Articles

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

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

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

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

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

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.

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  2. 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.

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  3. 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.

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  4. 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?

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

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

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  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.

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