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M0269

Sigma-Aldrich

Methotrexate−Agarose

saline suspension

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About This Item

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

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

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Certificados de análisis (COA)

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T Endo et al.
The EMBO journal, 7(4), 1153-1158 (1988-04-01)
We have purified milligram amounts of an importable mitochondrial precursor protein [the presequence of yeast cytochrome oxidase subunit IV fused to mouse dihydrofolate reductase (DHFR)]. This has made it possible, for the first time, to perform detailed studies on the
H J Chung et al.
Biochimica et biophysica acta, 1524(2-3), 183-188 (2000-12-13)
Tetrahydrobiopterin (BH4)-glucoside was identified from Synechococcus sp. PCC 7942 by HPLC analysis and the enzymatic activity of a glycosyltransferase producing the compound from UDP-glucose and BH4. The novel enzyme, named UDP-glucose:BH4 glucosyltransferase, has been purified 846-fold from the cytosolic fraction
C Ahn et al.
The Journal of biological chemistry, 272(24), 15323-15328 (1997-06-13)
Dihydroneopterin triphosphate (H2NTP) 2'-epimerase from Escherichia coli catalyzes the epimerization of H2NTP to dihydromonapterin triphosphate (H2MTP). The enzyme was purified 954-fold to apparent homogeneity by a combination of ammonium sulfate fractionation and column chromatography of Cibacron blue 3GA dye ligand
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
V Wilquet et al.
European journal of biochemistry, 255(3), 628-637 (1998-09-17)
We have overexpressed the gene for dihydrofolate reductase (DHFR) from Thermotoga maritima in Escherichia coli and characterized the biochemical properties of the recombinant protein. This enzyme is involved in the de novo synthesis of deoxythymidine 5'-phosphate and is critical for
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