Recombinant Rat D-Amino-Acid Oxidase (DAO) Protein (His&Myc)

Name: Recombinant Rat D-Amino-Acid Oxidase (DAO) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-03925P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Rat D-Amino-Acid Oxidase (DAO) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O35078
Target Symbol	DAO
Synonyms	Dao; Dao1D-amino-acid oxidase; DAAO; DAMOX; DAO; EC 1.4.3.3
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MRVAVIGAGVIGLSTALCIHERYHPAQPLHMKIYADRFTPFTTSDVAAGLWQPYLSDPSNPQEAEWNQQTFDHLQSCLHSPNAEKMGLALISGYNLFRDEVPDPFWKSTVLGFRKLTPSELDMFPDYSYGWFNTSLLLEGKSYLSWLTERLTERGVKFIHRKVASFEEVVRGGVDVIINCTGVWAGALQADASLQPGRGQIIQVEAPWIKHFILTHDPSLGIYNSPYIIPGSKTVTLGGVFQLGNWSELNSVHDHNTIWKSCCQLEPTLKNARIMGELTGFRPVRPQVRLERERLRFGSSSAEVIHNYGHGGYGLTIHWGCAMEAANLFGKILEEKNLSRMPPSHL
Expression Range	1-346aa
Protein Length	Full Length
Mol. Weight	45.8 kDa
Research Area	Metabolism
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	Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
Subcellular Location	Peroxisome.
Protein Families	DAMOX/DASOX family
Database References	KEGG: rno:114027 STRING: 10116.ENSRNOP00000000881 UniGene: Rn.81058

Gene Functions References

Plasma DAO activity decreases in response to severe intestinal mucosal injury after 5-FU treatment. PMID: 24005798
Its toxic effect on motor neurons can be mediated by expression in motor neurons and it promotes autophagy. PMID: 24138986
The study showed that the operation of renal ischemia resulted in a 45.49 +/- 8.30% (n = 8) decrease in the DAAO-induced consumption of substrate, indicating a sharp decrease in renal DAAO activity following this acute renal injury. PMID: 21110210
Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase PMID: 20368421
results suggest that an increase in DAO expression in parts of the brain is involved in aberrant D-amino acid metabolism, may be a potential therapeutic target for schizophrenia PMID: 19685198
This result clearly revealed that DAO was indispensable for the process of chiral inversion of d-leucine. PMID: 15026304
These results suggest that the TAA repeats are important for expression of the D-amino-acid oxidase gene. PMID: 18716858

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.