Recombinant Human Dihydrofolate Reductase (DHFR) Protein (His-SUMO)

Name: Recombinant Human Dihydrofolate Reductase (DHFR) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10137P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Dihydrofolate Reductase (DHFR) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P00374
Target Symbol	DHFR
Synonyms	DHFR; DHFRP1; Dihydrofolate reductase; DYR; DYR_HUMAN; EC 1.5.1.3
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	VGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND
Expression Range	2-187aa
Protein Length	partial
Mol. Weight	37.3kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.
Subcellular Location	Mitochondrion. Cytoplasm.
Protein Families	Dihydrofolate reductase family
Database References	HGNC: 2861 OMIM: 126060 KEGG: hsa:1719 STRING: 9606.ENSP00000396308 UniGene: PMID: 28887233 Dihydrofolate reductase and thymidylate synthase form a complex in vitro and co-localize in normal and cancer cells. PMID: 27187663 Single nucleotide polymorphism in DHFR gene is associated with Systemic lupus erythematosus. PMID: 28943344 study concludes polymorphism 63/91 in DHFR gene promoter can modulate the onset of methotrexate-related adverse effects in rheumatoid arthritis patients PMID: 27636122 our findings suggest that the identification of DHFR polymorphisms in the promoter region of the gene may be helpful in tailoring MTX doses for ALL pediatric patients on maintenance therapy. PMID: 28719513 The abundance of dihydrofolate reductase was statistically significantly increased in rheumatoid arthritis (RA)-patient biopsies compared with controls and correlated with the administered dosage of methotrexate (MTX), the most frequently prescribed immunosuppressive drug for RA. PMID: 27627584 The present study demonstrated that ADAR1 positively regulates the expression of DHFR by editing the miR-25-3p and miR-125a-3p binding sites in the 3'-UTR of DHFR, enhancing cellular proliferation and resistance to methotrexate in MCF-7 cells. PMID: 28188287 In conclusion, the finding suggests that folate nutrition and 19bp del-DHFR [Dihydrofolate reductase] variation may interact to modify adenomatous polyp [colorectal cancer] risk. PMID: 26875486 the highest expression of GGH and EGFR was noted in the left-sided colon; the highest expression of DHFR, FPGS, TOP1 and ERCC1 was noted in the rectosigmoid, whereas TYMP expression was approximately equivalent in the right-sided colon and rectum PMID: 26676887 Overexpression of miR-192 inhibited cellular proliferation by binding DHFR. miR-192 decreased cellular anchoring via the repression of ITGAV, ITGB1, ITGB3, and CD47 PMID: 26506238 Data suggest that DHFR exhibits intrinsic activity kinetics that are temperature-independent; additional mass (i.e., incorporation of H, C, and N isotopes) has no effect on intrinsic activity kinetics or protein conformation/stability of DHFR. PMID: 26813442 patients homozygous for the G allele of rs1053129 in the DHFR gene were more likely to have a metastasis (45%, P= 0.005), and the methylenetetetrahydrofolate reductase (MTHFR) 677C allele was associated with higher degree of liver toxicity PMID: 25778468 the association between cognitive outcomes with the 19-bp deletion DHFR polymorphism, folate status, and their interaction with high or normal plasma folate PMID: 26354538 S-nitrosylation of DHFR at cysteine 7 by eNOS-derived NO is crucial for DHFR stability. PMID: 26381869 genetic association studies in cohort of healthy young adults in Ireland: Data suggest that a 19 bp deletion/insertion polymorphism within intron 1 of DHFR (rs70991108) is not associated with folate nutritional status in the population studied. PMID: 26269242 Dihydrofolate Reductase and Thymidylate Synthase Transgenes Resistant to Methotrexate Interact to Permit Novel Transgene Regulation. PMID: 26242737 results for the first time suggested the DHFR 19-bp D/D genotype may confer a reduced risk of NS-CL/P and might act as a protective factor against NS-CL/P in the Iranian subjects. PMID: 26221921 Triple mutant haplotypes AIRNI (N51I+C59R+S108N) of the dhfr gene associated with pyrimethamine resistance were prevalent in Chirang district of Assam. PMID: 25511211 The human dihydrofolate reductase is relatively less stable than its E.coli counterpart. PMID: 26349210 subpicosecond protein motion is dynamically coupled to hydride transfer catalyzed by hsDHFR but not ecDHFR PMID: 25369552 MTHFR, DHFR and ATIC genetic variants can be considered as pharmacogenetic markers of outcome in RA patients under MTX monotherapy. PMID: 25084201 Genome-wide association studies identify 10 novel genetic loci as risk factors for methotrexate response in rheumatoid arthritis patients additionally to polymorphism in DHFR, FPGS and TYMS. PMID: 24583629 Genetic association between DHFR single nucleotide polymorphisms and nonsyndromic cleft lip with or without cleft palate. PMID: 24361572 The hDHFR requires minimal backbone conformational rearrangement as it proceeds through its enzymatic cycle, but that ligand flux is brokered by more subtle conformational changes that depend on the side chain motions of critical residues. PMID: 24498949 berberine suppresses the growth of cDDP-resistant cells more than the sensitive counterparts, by interfering with the expression of folate cycle enzymes, dihydrofolate reductase (DHFR) and thymidylate synthase (TS). PMID: 23903781 Data suggest that methylenetetrahydrofolate reductase (NAD(P)H), dihydrofolate reductase, thymidylate synthetase and SLC19A1 genes present increased expression after the highest dose of methotrexate in laryngeal cancer cell line. PMID: 23838799 Despite structural similarity, Escherichia coli and human DHFRs use different dynamic mechanisms to perform the same function, and human DHFR cannot complement DHFR-deficient E. coli cells. PMID: 24077226 Interactions between the ligands and Asn 64, Phe 31, and Phe 34 are important for increased affinity for DHFR. PMID: 24053334 We conclude that low activity of endothelial DHFR is an important factor limiting the benefits of BH4 therapies, which may be further aggravated by folate supplements. PMID: 23707606 There is an association between DHFR DD/SHMT TT and DHFR II/SHMT TT combined genotypes and folate and MMA concentrations in individuals with Down syndrome. PMID: 23421317 High DHFR immunoexpression correlated with nodal status and primary nasopharyngeal carcinoma. PMID: 23726796 The data presented here provide a glimpse into the evolutionary trajectory of functional DHFR through its protein sequence space that lead to the diverged binding and catalytic properties of the E. coli and human enzymes. PMID: 23733948 Inhibits cell growth through a mechanism involving downregulation of DHFR protein. PMID: 22954684 Genotyping of DHFR 829C>T and GGH -401C>T was performed using a polymerase chain reaction. PMID: 22994778 Led to accelerated degradation of DHFR and to inhibition of cancer cell growth. PMID: 23197646 The present study was aimed to investigate the possible association between 19-base pair (bp) deletion polymorphism of the DHFR gene (rs70991108), null genotype of UGT2B17 as well as the expression level of NGX6 with the risk of breast cancer. PMID: 23053953 Rheumatoid arthritis patients with DHFR-317AA genotype had less favourable response to methotrexate. PMID: 22324981 human dihydrofolate reductase is bound to NADP. PMID: 22024482 Constituents of the folate cycle could be involved in the etiology of idiopathic intellectual disability. PMID: 22005284 This report has clearly shown that the population rate of change of resistant dhfr and dhps alleles is contingent to the sulfadoxine-pyrimethamine usage in the population in the Morogor-Mvomero district PMID: 21857842 The 19-bp deletion polymorphism of DHFR gene was not a maternal risk factor for Down syndrome and was not related to variations in the concentrations of serum folate and plasma homocysteine and methylmalonic acid in the study population. PMID: 21120433 The 19-base pair deletion polymorphism of DHFR was studied in Japanese. The genotype distribution was wild/wild, 11.9%; wild/deletion, 40.1%; deletion/deletion, 48.0%. Frequencies of wild type and deletion alleles were 0.32 and 0.68, respectively. PMID: 20834190 Dihydrofolate reductase deficiency is associated with inborn error of metabolism. PMID: 21310276 Dihydrofolate reductase deficiency due to a homozygous DHFR mutation causes megaloblastic anemia and cerebral folate deficiency leading to severe neurologic disease. PMID: 21310277 the first kinetic parameters for DHFR from pjDHFR and pcDHFR with methotrexate (MTX), trimethoprim (TMP), and its potent analogue, PY957, is reported. PMID: 19196009 DNA variants have a role in predisposition to disease-free survival in childhood acute lymphoblastic leukemia PMID: 19861437 protein folding of dihydrofolate reductases (DHFR) from human, Escherichia coli, and Lactobacillus casei were elucidated and compared using intrinsic Trp fluorescence and fluorescence-detected ANS binding PMID: 11779239 studied differences between the regulation of Plasmodium and human dihydrofolate reductases PMID: 11964483 Computer modeling studies of the structural role of NADPH binding to active site mutants of human dihydrofolate reductase in complex with piritrexim PMID: 11996001 Molecular mechanisms that govern translational regulation of DHFR in response to MTX. Review. PMID: 12084458

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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