Dihydrofolate Reductase Active Protein | DHFR active protein
Recombinant Human Dihydrofolate Reductase
Gene Names
DHFR; DYR; DHFRP1
Purity
Greater than 95.0% as determined by SDS-PAGE.
Synonyms
Dihydrofolate Reductase; N/A; Recombinant Human Dihydrofolate Reductase; DHFR Human; Dihydrofolate Reductase Human Recombinant; Dihydrofolate reductase; DHFR; DHFRP1; DHFR active protein
Host
Escherichia Coli
Purity/Purification
Greater than 95.0% as determined by SDS-PAGE.
Form/Format
The DHFR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M Nacl 2mM DTT, and 30% glycerol.
Concentration
1 mg/ml (varies by lot)
Sequence
MGSSHHHHHH SSGLVPRGSH MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND.
Sequence Length
187
Physical Appearance
Sterile Filtered colorless solution.
Biological Activity
Specific activity is >3500 pmol/min/ug is defined as the amount of enzyme that converts 1.0 pmole of dihydrofolic acid to tetrahydrofolic acid per minute at pH 6.5 at 25C.
Preparation and Storage
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Related Product Information for DHFR active protein
Description: DHFR Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.6kDa.The DHFR is purified by proprietary chromatographic techniques.
Introduction: Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes. DHFR deficiency is associated with megaloblastic anemia.DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid.DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.
Introduction: Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes. DHFR deficiency is associated with megaloblastic anemia.DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid.DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
NCBI Official Full Name
dihydrofolate reductase isoform 1
NCBI Official Synonym Full Names
dihydrofolate reductase
NCBI Official Symbol
DHFR
NCBI Official Synonym Symbols
DYR; DHFRP1
NCBI Protein Information
dihydrofolate reductase
UniProt Protein Name
Dihydrofolate reductase
UniProt Gene Name
DHFR
UniProt Entry Name
DYR_HUMAN
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Product Notes
The DHFR dhfr (Catalog #AAA38726) is an Active Protein produced from Escherichia Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: MGSSHHHHHH SSGLVPRGSH MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND. It is sometimes possible for the material contained within the vial of "Dihydrofolate Reductase, Active Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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