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Trypsin from bovine pancreas (High Activity)

$195.00

Catalog Number: B2010249 (50 mg)
Trypsin from bovine pancreas is a high quality research product used as high purity, high specific activity, trypsin (≥10,000 BAEE units/mg protein) from bovine pancreas. Trypsin cleaves proteins and peptides at the C-terminus of lysine (K) and arginine (R) residues. Custom bulk orders of this product are available upon request.

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SKU: B2010249 Categories: ,

Description

Trypsin from Bovine pancreas
Catalog number: B2010249
Lot number: Batch Dependent
Expiration Date: Batch dependent
Volume/Weight: 50 mg
pH: na
Supplied as: Reconstitute before use
Appearance: Lyophilized Powder
Applications: high purity, high specific activity, trypsin (≥10,000 BAEE units/mg protein) from bovine pancreas. Trypsin cleaves proteins and peptides at the C-terminus of lysine (K) and arginine (R) residues.
Storage: -20C
Keywords: tryptic enzyme
Grade: Biotechnology grade. All components are highly pure (minimum 99%). All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered on a 0.22 um.

References:
1: Schilling O, Biniossek ML, Mayer B, Elsässer B, Brandstetter H, Goettig P,
Stenman UH, Koistinen H. Specificity profiling of human trypsin-isoenzymes. Biol
Chem. 2018 Sep 25;399(9):997-1007.

2: Perera E, Rodríguez-Viera L, Perdomo-Morales R, Montero-Alejo V, Moyano FJ,
Martínez-Rodríguez G, Mancera JM. Trypsin isozymes in the lobster Panulirus
argus (Latreille, 1804): from molecules to physiology. J Comp Physiol B. 2015
Jan;185(1):17-35.

3: Tabish TA, Pranjol MZI, Karadag I, Horsell DW, Whatmore JL, Zhang S.
Influence of luminescent graphene quantum dots on trypsin activity. Int J
Nanomedicine. 2018 Mar 15;13:1525-1538.

4: Stefansson B, Sandholt GB, Gudmundsdottir Á. Elucidation of different cold-
adapted Atlantic cod (Gadus morhua) trypsin X isoenzymes. Biochim Biophys Acta
Proteins Proteom. 2017 Jan;1865(1):11-19.

5: Wu F, Zhao M, Zhang Y, Su N, Xiong Z, Xu P. Recombinant acetylated trypsin
demonstrates superior stability and higher activity than commercial products in
quantitative proteomics studies. Rapid Commun Mass Spectrom. 2016 Apr
30;30(8):1059-66.

6: Kanno G, Klomklao S, Kumagai Y, Kishimura H. A thermostable trypsin from
freshwater fish Japanese dace (Tribolodon hakonensis): a comparison of the
primary structures among fish trypsins. Fish Physiol Biochem. 2019
Apr;45(2):561-571.

7: Klomklao S, Benjakul S. Two trypsin isoforms from albacore tuna (Thunnus
alalunga) liver: Purification and physicochemical and biochemical
characterization. Int J Biol Macromol. 2018 Feb;107(Pt B):1864-1870.

8: Pilon FM, Silva CDR, Visôtto LE, Barros RA, da Silva Júnior NR, Campos WG, de
Almeida Oliveira MG. Purification and characterization of trypsin produced by
gut bacteria from Anticarsia gemmatalis. Arch Insect Biochem Physiol. 2017
Oct;96(2).

9: Yu H, Cai S, Gao J, Wang C, Qiao X, Wang H, Feng L, Wang Y. Express Sequence
Tag Analysis – Identification of Anseriformes Trypsin Genes from Full-Length
cDNA Library of the Duck (Anas platyrhynchos) and Characterization of Their
Structure and Function. Biochemistry (Mosc). 2016 Feb;81(2):152-62.

10: Rühl M, Schönborn S, Karas M. Detergent-assisted sample preparation for
MALDI-MS: Investigation of octylglucoside and docecylmaltoside for matrix
crystallization, on-plate digestion, and trypsin activity. J MAs Spect. 2018
Aug;53(8):675-679.

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