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T0637

Sigma-Aldrich

Trypsin inhibitor

saline suspension

Sinónimos:

Trypsin Inhibitor Agarose

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About This Item

MDL number:
MFCD00165901
UNSPSC Code:
41106500
NACRES:
NA.56

product name

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

biological source

protein from Glycine max (soybean)

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

Categorías relacionadas

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.

Physical form

Suspension in 0.5 M NaCl containing preservative

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Liu-Ying Luo et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 12(3 Pt 1), 742-750 (2006-02-10)
Preliminary data suggest that hK11 is a novel serum biomarker for prostate and ovarian cancer. To examine the enzymatic characteristics of hK11, we purified and functionally characterized native hK11 from seminal plasma. hK11 was purified from seminal plasma by immunoaffinity
L J Marnett et al.
The Journal of biological chemistry, 263(32), 16532-16535 (1988-11-15)
Treatment of prostaglandin (PG)H synthase purified from ram seminal vesicle microsomes with trypsin cleaves the 70-kDa subunits into 33- and 38-kDa fragments (Chen, Y.-N. P., Bienkowski, M. J., and Marnett, L. J. (1987) J. Biol. Chem. 262, 16892-16899). In contrast
Y J Chuang et al.
The Journal of biological chemistry, 276(18), 14961-14971 (2001-03-30)
Heparin activates the primary serpin inhibitor of blood clotting proteinases, antithrombin, both by an allosteric conformational change mechanism that specifically enhances factor Xa inactivation and by a ternary complex bridging mechanism that promotes the inactivation of thrombin and other target
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
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
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