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Merck
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Principaux documents

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

Nom du produit

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

Source biologique

protein from Glycine max (soybean)

Niveau de qualité

200

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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Certificats d'analyse (COA)

Lot/Batch Number
0000301237
SLCP2688
SLCM2320
SLCJ9939
SLCG2836

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Consulter la Bibliothèque de documents

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
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
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
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)
D P Goldenberg et al.
Proceedings of the National Academy of Sciences of the United States of America, 89(11), 5083-5087 (1992-06-01)
In a previous study, a genetic screening procedure was used to identify variants of bovine pancreatic trypsin inhibitor that can fold to an active conformation but that are inactivated much more rapidly than the wild-type protein in the presence of
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