Recombinant Mouse L-Dopachrome Tautomerase (DCT) Protein (His-SUMO&Myc)

Beta LifeScience SKU/CAT #: BLC-03483P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse L-Dopachrome Tautomerase (DCT) Protein (His-SUMO&Myc)

Beta LifeScience SKU/CAT #: BLC-03483P
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Product Overview

Description Recombinant Mouse L-Dopachrome Tautomerase (DCT) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P29812
Target Symbol DCT
Synonyms Dct; Tyrp-2; Tyrp2; L-dopachrome tautomerase; DCT; DT; EC 5.3.3.12; DOPAchrome conversion factor; DOPAchrome isomerase; DOPAchrome oxidoreductase; L-dopachrome Delta-isomerase; SLATY locus protein; Tyrosinase-related protein 2; TRP-2; TRP2
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-10His-SUMO&C-Myc
Target Protein Sequence QFPRVCMTLDGVLNKECCPPLGPEATNICGFLEGRGQCAEVQTDTRPWSGPYILRNQDDREQWPRKFFNRTCKCTGNFAGYNCGGCKFGWTGPDCNRKKPAILRRNIHSLTAQEREQFLGALDLAKKSIHPDYVITTQHWLGLLGPNGTQPQIANCSVYDFFVWLHYYSVRDTLLGPGRPYKAIDFSHQGPAFVTWHRYHLLWLERELQRLTGNESFALPYWNFATGKNECDVCTDELLGAARQDDPTLISRNSRFSTWEIVCDSLDDYNRRVTLCNGTYEGLLRRNKVGRNNEKLPTLKNVQDCLSLQKFDSPPFFQNSTFSFRNALEGFDKADGTLDSQVMNLHNLAHSFLNGTNALPHSAANDPVFVVLHSFTDAIFDEWLKRNNPSTDAWPQELAPIGHNRMYNMVPFFPPVTNEELFLTAEQLGYNYAVDLSEEEAPVWSTTLS
Expression Range 24-472aa
Protein Length Partial
Mol. Weight 71.2kDa
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 Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA).
Subcellular Location Melanosome membrane; Single-pass type I membrane protein. Melanosome.
Protein Families Tyrosinase family
Database References
Associated Diseases The slaty mutation in Tyrp2 leads to a decrease of DT activity and a consequent change in the pigmentation of the mice to a dark gray/brown eumelanin. The slaty-2j mutation has a similar phenotype, the slaty-lt (light) mutation has a more severe effect and is semidominant; its phenotype may be a result of the failure of the enzyme to be correctly targeted to its normal location on the inner face of the melanosomal membrane.
Tissue Specificity Melanocytes and retinal pigmented epithelium (at protein level).

Gene Functions References

  1. soyasaponin Ag inhibited TRP2 expression in a dosedependent manner. Therefore, the depigmenting effect of soyasaponin Ag may be due to the inhibition of tyrosinase expression or the enhancement of tyrosinase degradation. PMID: 28713957
  2. the slaty mutant melanocytes seem to be more sensitive to ultraviolet rays and oxidative stress than black melanocytes. PMID: 26451690
  3. A novel murine model of vitiligo is established by sequential prime/boost immunizations into the hind footpad and tail dermis with tyrosinase-related protein 2 (TRP2)-180 (SVYDFFVWL) peptide. PMID: 23711243
  4. study indicates that tumor antigen (TRP2) expressed in MCMV induces a strong and long-lasting anti-melanoma effect through an antibody-dependent mechanism PMID: 23811402
  5. Vaccine formulations with synthetic long peptides for treating B16F10 skin melanoma fails to elicit strong CD8 T cell responses to self-differentiation antigens TRP-2 and gp100. PMID: 23203930
  6. level of gene targeting was not improved by the DSB induction, indicating a limited capacity of I-SceI to mediate homologous recombination at the Dct locus PMID: 22761925
  7. Recombinant dopachrome tautomerase was expressed and purified, without its carboxy-terminal transmembrane region. Analysis of dopachrome tautomerase tryptic peptides by MALDI-TOF/TOF determined N-glycosylation as a primary post-translational modification. PMID: 20386969
  8. Dopachrome tautomerase inactivation elevates the level of ROS, increases the numbers of sunburn cells and apoptotic cells, and decreases the amount of eumelanin in the epidermis upon exposure to chronic UVA radiation PMID: 20123016
  9. the TRP-2 polypeptide folds in the endoplasmic reticulum (ER) in the presence of calnexin, until it reaches a dithiothreitol-resistant conformation enabling its ER exit to the Golgi PMID: 12719423
  10. Results describe the generation of a knockout of the dopachrome tautomerase gene in mice with effects restricted to pigment production and coat color. PMID: 15060160
  11. We found that ionophore monensin (Mon) and the quaternary amine chloroquine (CQ) discriminate between the traffic routes of TRP-2 and TRP-1 PMID: 15707965
  12. The enzymatic activity of Dct may play a role in determining whether the eumelanin or pheomelanin pathway is preferred for pigment biosynthesis. PMID: 15960609
  13. These results suggest that the slaty mutation affects both eumelanin and pheomelanin synthesis in developmental stage-specific and skin site-specific manners. PMID: 16584806
  14. Slaty mutation blocks the melanosome maturation at stage III and affects the melanosome morphology (elliptical or spherical) in a developmental stage-specific manner. PMID: 17516460
  15. Eumelanin and pheomelanin may accumulate with difficulty in slaty-mutated melanocytes and be easily released from them during skin development. L-Tyr may stimulate this release. PMID: 17551240
  16. These results suggest that the slaty mutation inhibits the development of elliptical stage IV melanosomes and that L-Tyr restores the development of elliptical stage IV melanosomes PMID: 17867832
  17. Cytotoxicity toward targets loaded with a K(b)-restricted tyrosinase-related protein 2-derived peptide correlated with depigmentation in a mouse model of autoimmune vitiligo. PMID: 18337834
  18. mice lacking DCT displayed normal cardiac development but an increased susceptibility to atrial arrhythmias PMID: 19855129

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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.

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