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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 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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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
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
Ying Xu et al.
Journal of bacteriology, 185(18), 5519-5526 (2003-09-02)
Adapting metabolic enzymes of microorganisms to low temperature environments may require a difficult compromise between velocity and affinity. We have investigated catalytic efficiency in a key metabolic enzyme (dihydrofolate reductase) of Moritella profunda sp. nov., a strictly psychrophilic bacterium with
M Iwakura et al.
Protein engineering, 5(8), 791-796 (1992-12-01)
A single polypeptide chain containing two dihydrofolate reductase (DHFR) sequences from Escherichia coli was constructed to determine if a repeat sequence fusion protein could be expressed in an active form. The possibility that intersequence interactions could play a significant role
S Shallom et al.
The Journal of biological chemistry, 274(53), 37781-37786 (1999-12-23)
In Plasmodium falciparum, dihydrofolate reductase and thymidylate synthase activities are conferred by a single 70-kDa bifunctional polypeptide (DHFR-TS, dihydrofolate reductase-thymidylate synthase) which assembles into a functional 140-kDa homodimer. In mammals, the two enzymes are smaller distinct molecules encoded on different
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