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Merck
CN

M0269

Methotrexate−Agarose

saline suspension

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About This Item

UNSPSC Code:
13111023
NACRES:
NA.56
MDL number:
MFCD00164466

Key Documents

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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

Quality Level

200

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

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter

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Certificates of Analysis (COA)

Lot/Batch Number
0000362898
0000313030
0000313030
0000362898
0000341705

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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
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
S Rospert et al.
The EMBO journal, 15(4), 764-774 (1996-02-15)
Proteins that are imported from the cytosol into mitochondria cross the mitochondrial membranes in an unfolded conformation and then fold in the matrix. Some of these proteins require the chaperonin hsp60 for folding. To test whether hsp60 is required for
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
P Loetscher et al.
The Journal of biological chemistry, 266(17), 11213-11220 (1991-06-15)
Several years ago, we proposed that polypeptide regions rich in proline (P), glutamic acid (E), serine (S), and threonine (T) (PEST) target intracellular proteins for destruction (Rogers, S., Wells, R., and Rechsteiner, M. (1986) Science 234, 364-368). To test the
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