Recombinant Human DHFR Protein

重组人DHFR蛋白 | 重组人二氢叶酸还原酶

DHFR | DHFRP1 | Dihydrofolate Reductase | DYR | EC 1.5.1.3

rp188305-10μg

10μg

无载体

≥95%(SDS-PAGE)

Dihydrofolate Reductase (DHFR) is an approximately 21 kDa enzyme that catalyzes the NADPH-dependent reduction of dihydrofolate to tetrahydrofolate, which is crucial for the synthesis of purines, thymidylate, and certain amino acids. Structurally, DHFR consists of an eight-stranded beta -sheet and four alpha -helices. Human DHFR shares 90% amino acid identity with mouse and rat DHFR. In addition to acting as a cofactor, NADPH protects DHFR from degradation in vitro and in a cellular context. DHFR protein binds to its own mRNA to self-regulate translation. The enzymatic activity and subcellular localization of DHFR are at least partially regulated by post-translational modification. Mono-ubiquitination of DHFR by MDM2 reduces the activity of DHFR. DHFR is primarily cytoplasmic, but it has been shown to translocate to the nucleus in a SUMO-dependent manner. Due to its role in nucleotide biosynthesis, DHFR has long been a therapeutic target for the treatment of various cancers and infectious diseases.

1. Measured by the reduction of dihydrofolic acid (DHF). The specific activity is >5,500 pmol/min/μg, as measured under the described conditions. 2. Immobilized Recombinant Human DHFR Protein (rp188305) at 1.0 μg/mL can bind Recombinant Dihydrofolate reductase/DHFR Antibody (Ab099867) with the EC50 of 4.9 ng/mL.

重组表达

22.2 kDa

C-His

23.5 kDa, under reducing conditions; 23.5 kDa, under non-reducing conditions.

E. coli Accession #: P00374 | E. coli

<1.0 EU/μg

人(Human)

1-187 aa

MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKNDHHHHHH

No

Yes