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Merck
CN

T8428

Trypsin Inhibitor−Celite®

powder, average diameter 1.8 μm, protein from Phaseolus limensis (lima bean)

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UNSPSC Code:
23151820
MDL number:
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biological source

protein from Phaseolus limensis (lima bean)

form

powder

extent of labeling

50-75 mg per g solid

matrix

powdered Celite

matrix spacer

8 atoms

pore size

1.8 μm average diameter

capacity

20-80 mg/mg, solid binding capacity (trypsin)(with an activity of 10,000 BAEE units per mg)

storage temp.

2-8°C

Application

Trypsin inhibitor Celite is used for protein chromatography, affinity chromatography and specialty resins. Trypsin inhibitor Celite has been used to determine that corn trypsin inhibitor decreases tissue-type plasminogen activator-mediated fibrinolysis of human plasma. Trypsin inhibitor celite has also been used in numerous studies assessing activtated coagulation time.

Legal Information

Celite is a registered trademark of Imerys Minerals California, Inc.

pictograms

Exclamation mark

signalword

Warning

Hazard Classifications

Acute Tox. 4 Inhalation - Eye Irrit. 2 - STOT SE 3

target_organs

Respiratory system

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves

法规信息

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分析证书(COA)

Lot/Batch Number

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Z Liu et al.
The Journal of pharmacology and experimental therapeutics, 284(2), 526-534 (1998-03-07)
S-Nitrosothiols are a group of potent, bioactive compounds that form through the reaction of nitric oxide (NO) with thiols in the presence of oxygen. These compounds are naturally occurring in vivo, stabilize NO and potentiate its biological effects. S-Nitrosoglutathione is
B R Hubbard et al.
Proceedings of the National Academy of Sciences of the United States of America, 86(18), 6893-6897 (1989-09-01)
The vitamin K-dependent carboxylase catalyzes the posttranslational modification of specific glutamic acid residues to form gamma-carboxyglutamic acid residues within the vitamin K-dependent proteins. This enzyme recognizes the gamma-carboxylation recognition site on the propeptide of the precursor forms of the vitamin
A Azzi et al.
Proceedings of the National Academy of Sciences of the United States of America, 79(8), 2447-2450 (1982-04-01)
An efficient affinity chromatography procedure for the isolation of mitochondrial cytochrome c oxidase and reductase is described. Saccharomyces cerevisiae cytochrome c was used as a ligand, bound to a thiol-Sepharose 4B gel through cysteine-107. In this way, the site of
D Y Min et al.
The Korean journal of parasitology, 36(4), 261-268 (1998-12-30)
The present study was undertaken to investigate the role of cysteine proteinase of Trichomonas vaginalis in escaping from host defense mechanism. A cysteine proteinase of T. vaginalis was purified by affinity chromatography and gel filtration. Optimum pH for the purified
R Li et al.
The Journal of cell biology, 143(6), 1523-1534 (1998-12-16)
In the presence of bound Mn2+, the three- dimensional structure of the ligand-binding A-domain from the integrin CR3 (CD11b/CD18) is shown to exist in the "open" conformation previously described only for a crystalline Mg2+ complex. The open conformation is distinguished

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