T0637
Trypsin inhibitor–Agarose
saline suspension, protein from Glycine max (soybean)
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biological source
protein from Glycine max (soybean)
Quality Level
form
saline suspension
matrix
cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
amino
matrix spacer
1 atom
capacity
≥1 mg/mL binding capacity (trypsin)(with activity of 10,000 BAEE units per mg)
storage temp.
2-8°C
Related Categories
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)
Physical form
Suspension in 0.5 M NaCl containing preservative
WGK
WGK 3
Regulatory Information
动植物源性产品
Certificates of Analysis (COA)
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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)
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
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
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
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
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