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Merck
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T0637

Sigma-Aldrich

Trypsin inhibitor

saline suspension

Synonyme(s) :

Trypsin Inhibitor Agarose

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About This Item

Numéro MDL:
MFCD00165901
Code UNSPSC :
41106500
Nomenclature NACRES :
NA.56

product name

Trypsin inhibitor–Agarose, saline suspension, protein from Glycine max (soybean)

Source biologique

protein from Glycine max (soybean)

Forme

saline suspension

Matrice

cross-linked 4% beaded agarose

Activation de la matrice

cyanogen bromide

Fixation de matrice

amino

Espaceur de matrice

1 atom

Capacité

≥1 mg/mL binding capacity (trypsin)(with activity of 10,000 BAEE units per mg)

Température de stockage

2-8°C

Application

Trypsin inhibitor-Agarose has been used in affinity chromatography for the purification:

  • of shrimp chymotrypsin
  • of protease from Trichoderma reesei
  • of Ras-interacting protein 1(Rasip 1)
Trypsin inhibitor-agarose is used in protein chromatography, affinity chromatography, and specialty resins.

Forme physique

Suspension in 0.5 M NaCl containing preservative

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

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D Lu et al.
Journal of molecular biology, 292(2), 361-373 (1999-09-24)
Enteropeptidase is a membrane-bound serine protease that initiates the activation of pancreatic hydrolases by cleaving and activating trypsinogen. The enzyme is remarkably specific and cleaves after lysine residues of peptidyl substrates that resemble trypsinogen activation peptides such as Val-(Asp)4-Lys. To
J S Munger et al.
Molecular biology of the cell, 9(9), 2627-2638 (1998-09-03)
The multipotential cytokine transforming growth factor-beta (TGF-beta) is secreted in a latent form. Latency results from the noncovalent association of TGF-beta with its processed propeptide dimer, called the latency-associated peptide (LAP); the complex of the two proteins is termed the
S Lawler et al.
Current biology : CB, 8(25), 1387-1390 (1999-01-16)
Mitogen-activated protein kinases (MAPKs) mediate many of the cellular effects of growth factors, cytokines and stress stimuli. Their activation requires the phosphorylation of a threonine and a tyrosine residue located in a Thr-X-Tyr motif (where X is any amino acid)
Shuishu Wang et al.
Protein science : a publication of the Protein Society, 12(5), 1097-1108 (2003-04-30)
Pantothenate biosynthesis is essential for the virulence of Mycobacterium tuberculosis, and this pathway thus presents potential drug targets against tuberculosis. We determined the crystal structure of pantothenate synthetase (PS) from M. tuberculosis, and its complexes with AMPCPP, pantoate, and a
Christopher P Landowski et al.
Microbial cell factories, 15(1), 104-104 (2016-06-12)
The filamentous fungus Trichoderma reesei has tremendous capability to secrete over 100 g/L of proteins and therefore it would make an excellent host system for production of high levels of therapeutic proteins at low cost. We have developed T. reesei strains
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