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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(e):

Porcine Trypsin, Trypsin for Mass Spectropetry

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Über diesen Artikel

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

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Produktname

Trypsin aus Schweinepankreas, Proteomics Grade, BioReagent, Dimethylated

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

Quality Level

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Dieser Artikel
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

solubility

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

solubility

-

solubility

-

solubility

-

shipped in

wet ice

shipped in

ambient

shipped in

-

shipped in

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

product line

BioReagent

product line

BioReagent

product line

-

product line

-

General description

Trypsin ist eine Serinprotease, die in der Regel als wichtiges Enzymreagens in der Biochemie und Biologie eingesetzt wird.[1] Dieses Verfahren erzeugt ein hochgradig aufgereinigtes Trypsinprodukt, das sich für die Proteomikforschung eignet. Die Proteomik-Qualität eignet sich ideal zur Verwendung beim Trypsinabbau in sowohl Lösung als auch Gel. Trypsin, eine Serinprotease, kommt im Verdauungssystem verschiedener Wirbeltiere vor.[2]

Application

Trypsin aus dem Schweinepankreas wird für folgende Anwendungen eingesetzt:
  • In-Gel-Proteinverdau und Analysen mittels MALDI-TOF-Massenspektrometrie[3]
  • Analyse mittels Elektrospray-Ionisations-Massenspektrometrie (ESI-MS)[4]
  • Proteom-Oberflächenprofilierung von L. plantarum[5]
  • Gelfiltration, Ultrazentrifugation und rotierende Elektronenmikroskopie mit Abschattung[6]
  • Massenspektrometrie[7][8]

Biochem/physiol Actions

Trypsin wird aufgrund seiner hochspezifischen Spaltung, die zu einer begrenzten Anzahl tryptischer Peptide führt, regelmäßig in der Proteomikforschung für Peptid-Mapping und Proteinsequenzarbeit eingesetzt. Es hydrolysiert Peptidbindungen an der Carboxylseite von Arginin- und Lysinresten[2] spezifisch. Das Enzym weist außerdem Esterase- und Amidaseaktivitäten auf.[9] Trypsin dient als Zellkultur-Tool. Es wird für die Hydrolyse von allergenen Proteinen eingesetzt, um hypoallergene Milch in der Industrie herzustellen.[1]

Ähnliches Produkt

Produkt-Nr.
Beschreibung
Preisangaben

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Lagerklasse

11 - Combustible Solids

ppe

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


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Die Dokumentenbibliothek aufrufen

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)
Masayuki Shimoda et al.
Cell transplantation, 21(2-3), 465-471 (2012-07-17)
Porcine islets are considered to be a promising resource for xenotransplantation. However, it is difficult to isolate porcine islets because of the marked fragility and rapid dissociation. Endogenous trypsin is one of the main factors to damage islets during the
Biomarkers of acute and chronic pancreatitis
Kaphalia BS
Biomarkers in Toxicology, 279-289 (2014)
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

Artikel

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

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

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.

Protokolle

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

Questions

1–6 of 6 Questions  
  1. 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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  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.

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  3. 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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  4. 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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  5. 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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  6. 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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