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D1067

Sigma-Aldrich

Anti-DHFR, N-terminal antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Dihydrofolate reductase

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

mouse, human, rat

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): 0.5-1.0 μg using 100-200 ng of purified DHFR
western blot (chemiluminescent): 0.5-1.0 μg/mL using 100 ng of purified recombinant DHFR

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DHFR(1719)
mouse ... Dhfr(13361)
rat ... Dhfr(24312)

Related Categories

General description

Dihydrofolate reductase has 187 amino acids and corresponds to molecular weight of 18-20 kDa. It is mapped to chromosome 5q22 region. DHFR contains substrate binding site and coenzyme binding domain.

Specificity

Anti-DHFR, N-terminal antibody is specific for the epitope residing within amino acids of mouse DHFR. The antibody interacts with DHFR and DHFR fusion proteins. The product is specific for DHFR in humans, mice and rats. Staining of the DHFR band by immunoblotting is inhibited by the immunizing peptide.

Immunogen

The immunizing sequence is conserved in mouse, human and rat.

Application

Anti-DHFR, N-terminal antibody produced in rabbit has been used in immunoprecipitation and western blotting.

Biochem/physiol Actions

Dihydrofolate reductase (DHFR) inhibitors, such as methotrexate, are folate analogs which can bind to the active site and deactivate the enzyme. From another angle, structural and enzymatic properties of DHFR led to development of a variety of screenings, in which DHFR can function in a fashion that resembles reporter genes. The screenings are based on the fact that DHFR can be dissected into two halves that can reassemble to form an active enzyme. Thus, each of the two halves of DHFR can be expressed as two fusion proteins that when interacting with each other can restore the DHFR enzymatic activity. The readout of this protein-protein interaction and consequent enzymatic activity, can be either restoration of growth in bacterial, yeast and plant, or receptor activation. The approach was proved to be useful for receptor-ligand, antigen-antibody and other interactions.
Dihydrofolate reductase (DHFR) is an NADPH dependent enzyme that reduces dihydrofolate and regenerates tetrahydrofolate. DHFR is involved in the biosynthesis of thymidylate and purines, and thereby regulates DNA synthesis and cell survival. Alterations in DHFR have been associated with impaired nucleic acid synthesis and cell death. Thus, this enzyme has important therapeutic implications in cell proliferative disorders such as cancer.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Certificates of Analysis (COA)

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A study on dihydrofolate reductase and its inhibitors: a review
Rao, AS and Tapale, SR
International Journal of Pharmaceutical Sciences and Research, 4(7), 2535-2535 (2013)
Characterization and inhibition of AF10-mediated interaction
Hagen S, et al.
Journal of Peptide Science, 20(6), 385-397 (2014)
The dihydrofolate reductase protein-fragment complementation assay: A survival-selection assay for large-scale analysis of protein-protein interactions
Michnick SW, et al.
Cold Spring Harbor Protocols, 2016(11), pdb-prot090027 (2016)
The proteasome subunit Rpn8 interacts with the small nucleolar RNA Protein (snoRNP) assembly protein Pih1 and mediates its ubiquitin-independent degradation in Saccharomyces cerevisiae
Paci A, et al.
The Journal of Biological Chemistry, 291(22), 11761-11775 (2016)
Nan Xin et al.
The Journal of cell biology, 221(7) (2022-05-25)
The mitochondrial unfolded protein response (UPRmt) is dedicated to promoting mitochondrial proteostasis and is linked to extreme longevity. The key regulator of this process is the transcription factor ATFS-1, which, upon UPRmt activation, is excluded from the mitochondria and enters

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