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M0269

Sigma-Aldrich

Methotrexate−Agarose

saline suspension

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About This Item

MDL number:
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 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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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