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M0269

Sigma-Aldrich

Methotrexate−Agarose

saline suspension

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10 ML
$334.00
25 ML
$631.00

$334.00

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10 ML
$334.00
25 ML
$631.00

About This Item

MDL number:
UNSPSC Code:
13111023
NACRES:
NA.56

$334.00

PRICE WITHOUT NATIONAL TAXES

Check Cart for Availability

biological source

plant

form

saline suspension

extent of labeling

2-7 mg per mL

technique(s)

affinity chromatography: suitable

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

carboxyl

matrix spacer

8 atoms

suitability

suitable for chromatography

storage temp.

2-8°C

Application

Methotrexate-agarose is used in protein chromatography, affinity chromatography, metabolic pathways and specialty resins. Methotrexate-agarose has been used to investigate the toxicity mechanism of mortality in adult buffalo flies caused by ingestion of folate analogues. Methotrexate-agarose has also been used to study the purification, cloning, and functional expression of dihydroneopterin triphosphate 2′-epimerase from Escherichia coli.

Physical form

Suspension in 1.0 M NaCl containing preservative

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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C J Thomson et al.
Journal of general microbiology, 136(4), 673-677 (1990-04-01)
The type IIIb dihydrofolate reductase, a novel plasmid-encoded enzyme recently identified in Shigella sonnei, has been shown to have some similar biochemical properties to the type IIIa dihydrofolate reductase which was first identified in New Zealand in 1979. However, the
K Braig et al.
Proceedings of the National Academy of Sciences of the United States of America, 90(9), 3978-3982 (1993-05-01)
Chaperonins are oligomeric protein complexes that play an essential role in the cell, mediating ATP-dependent polypeptide chain folding in a variety of cellular compartments. They appear to bind early folding intermediates, preventing their aggregation; in the presence of MgATP and
Munehito Arai et al.
Journal of molecular biology, 329(4), 779-791 (2003-06-06)
The unfolded state of a protein is an ensemble of a large number of conformations ranging from fully extended to compact structures. To investigate the effects of the difference in the unfolded-state ensemble on protein folding, we have studied the
M Tehei et al.
Biophysical journal, 90(3), 1090-1097 (2005-11-01)
The internal dynamics of native and immobilized Escherichia coli dihydrofolate reductase (DHFR) have been examined using incoherent quasielastic neutron scattering. These results reveal no difference between the high frequency vibration mean-square displacement of the native and the immobilized E. coli
T Endo et al.
Journal of biochemistry, 118(4), 753-759 (1995-10-01)
We have designed a fusion gene encoding a chimeric mitochondrial precursor protein (avidin fusion protein) that consists of the mitochondrial presequence followed by mouse dihydrofolate reductase, a spacer segment, and streptavidin. The avidin fusion protein synthesized in vitro formed a

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