Recommended Products
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
Related Categories
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
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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
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
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
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
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