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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

Sinônimo(s):

Anti-Dihydrofolate reductase

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

reatividade de espécies

mouse, human, rat

concentração

~1.0 mg/mL

técnica(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

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

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

Descrição geral

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.

Especificidade

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.

Imunogênio

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

Aplicação

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

Ações bioquímicas/fisiológicas

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.

forma física

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificados de análise (COA)

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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)
Characterization and inhibition of AF10-mediated interaction
Hagen S, et al.
Journal of Peptide Science, 20(6), 385-397 (2014)
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)
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)
Alexandr Paci et al.
The Journal of biological chemistry, 291(22), 11761-11775 (2016-04-08)
Pih1 is a scaffold protein of the Rvb1-Rvb2-Tah1-Pih1 (R2TP) protein complex, which is conserved in fungi and animals. The chaperone-like activity of the R2TP complex has been implicated in the assembly of multiple protein complexes, such as the small nucleolar

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