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M0269

Sigma-Aldrich

Methotrexate−Agarose

saline suspension

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About This Item

Numero MDL:
MFCD00164466
Codice UNSPSC:
13111023
NACRES:
NA.56

Origine biologica

plant

Forma fisica

saline suspension

Grado di funzionalizzazione

2-7 mg per mL

tecniche

affinity chromatography: suitable

Matrice

cross-linked 4% beaded agarose

Attivazione matrice

cyanogen bromide

Gruppi immobilizzati alla matrice

carboxyl

Braccio spaziatore

8 atoms

Compatibilità

suitable for chromatography

Temperatura di conservazione

2-8°C

Applicazioni

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.

Stato fisico

Suspension in 1.0 M NaCl containing preservative

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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

Certificati d'analisi (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
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
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
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
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
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