Biotinylated Recombinant E.Coli Dihydrofolate Reductase (FOLA) Protein (MBP&His-Avi)

Name: Biotinylated Recombinant E.Coli Dihydrofolate Reductase (FOLA) Protein (MBP&His-Avi)
Brand: Beta LifeScience
SKU: BLC-00588P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Avi-tagged proteins, Biotinylated proteins, Featured biotinylated protein molecules, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Biotinylated Recombinant E.Coli Dihydrofolate Reductase (FOLA) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P0ABQ4
Target Symbol	FOLA
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-MBP&C-6His-Avi
Target Protein Sequence	MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
Expression Range	1-159aa
Protein Length	Full Length
Mol. Weight	65.8 kDa
Research Area	Others
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. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
Protein Families	Dihydrofolate reductase family
Database References	KEGG: ecj:JW0047 STRING: 316385.ECDH10B_0049

Gene Functions References

NADP+ not only binds to the native form but also a partially unfolded form of dihydrofolate reductase. PMID: 25367157
Quantum mechanics/molecular dynamics simulations reveal that the M20 loop conformational dynamics of dihydrofolate reductase (DHFR) is severely restricted at the transition state of the hydride transfer as a result of the M42W/G121V double mutation. PMID: 23297871
Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle PMID: 23614825
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
Present a general kinetic framework that can be used to study conformation changes, apply this framework to E. coli DHFR and find the conformational change occurs predominantly prior to unbinding. PMID: 22641560
Protein interface remodeling in a chemically induced protein dimer. PMID: 22733548
Dihydrofolate reductase is bound to endogenous tetrahydrofolate PMID: 22024482
[review] A general mechanism is presented for folA catalysis that includes multiple intermediates and a complex, multidimensional standard free energy surface. PMID: 22029278
Only a single peptide from DHFR is found to be substantially more flexible than the Bacillus stearothermophilus-DHFR at 25 degrees C in a region located within the protein interior at the intersection of the cofactor and substrate-binding sites. PMID: 21859100
Taken together with previous studies in the millisecond time range, a hierarchical assembly of DHFR--in which each subdomain independently folds, subsequently docks, and then anneals into the native conformation after an initial global collapse--emerges. PMID: 21554889
Thermodynamics and solvent effects on substrate and cofactor binding in Escherichia coli chromosomal dihydrofolate reductase PMID: 21462996
mutant DHFR that abrogates millisecond-time-scale fluctuation in active site without perturbing structural and electrostatic preorganization; found link between conformational fluctuations on millisecond time scale and chemical step of enzymatic reaction PMID: 21474759
Fcused on residues 52, 67, 121, and 145 in the four distinct loops of DHFR. All the single-residue deletion mutants showed marked reduction in stability, except for Delta52 in an alphaC-betaC loop. PMID: 20045086
resulting triple mutants, DM-N18C, DM-R52C, DM-D87C and DM-D132C dihydrofolate reductase, were alkylated with glucose, N-acetylglucosamine, lactose and maltotriose iodoacetamides. PMID: 20412060
Data show that the M42W mutation alters the dynamics of DHFR and are consistent with theoretical analysis that suggests this mutation disrupts motion that promotes catalysis. PMID: 20073522
results suggest that dynamics in dihydrofolate reductase are exquisitely "tuned" for every intermediate in the catalytic cycle; structural fluctuations efficiently channel the enzyme through functionally relevant conformational space. PMID: 20080605
These results suggest that through electrostatic interactions Arg44 plays a functional role in retaining the cofactor binding affinity at the cost of the Escherichia coli dihydrofolate reductase stability. PMID: 20043879
Lys-32 residues have a role in the ionic interaction in R67 dihydrofolate reductase PMID: 15333636
the hydroxyl group of Tyr-69 of DFHR is important for interactions with NADPH, whereas both the hydroxyl group and hydrophobic ring atoms of the Tyr-69 residues are necessary for proper interactions with dihydrofolate PMID: 15333637
structural and functional alterations induced by peroxynitrite may play a direct role in compromising DHFR function in multiple pathological conditions PMID: 15639221
biophysical analysis of immobilized and native Escherichia coli dihydrofolate reductase PMID: 16258053
Results show that mutant dihydrofolate reductase has reduced catalytic activity. PMID: 16363797
characterization of higher energy conformational substates of dihydrofolate reductase using using nuclear magnetic resonance relaxation dispersion PMID: 16973882
DHFR structure from neutron diffraction studies provides insights into dynamics, active-site protonation states, and solvation pattern of the E. coli enzyme. PMID: 17130456
The folding trajectory of this alpha/beta-type protein (DHFR) is located between those of alpha-helical and beta-sheet proteins, suggesting that native structure determines the folding landscape. PMID: 17331539
Several mutations were found to grant resistance to trimethoprim, both by reducing the binding affinity of the enzyme for the drug, and by increasing the activity of the enzyme. PMID: 17451440

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.