Recombinant Mouse Tyrosinase (TYR) Protein (His)

Name: Recombinant Mouse Tyrosinase (TYR) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07921P
Price: 3112.8 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Tyrosinase (TYR) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P11344
Target Symbol	TYR
Synonyms	(Albino locus protein)(Monophenol monooxygenase)
Species	Mus musculus (Mouse)
Expression System	in vitro E.coli expression system
Tag	N-10His
Target Protein Sequence	HFPRACASSKNLLAKECCPPWMGDGSPCGQLSGRGSCQDILLSSAPSGPQFPFKGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFGGPNCTEKRVLIRRNIFDLSVSEKNKFFSYLTLAKHTISSVYVIPTGTYGQMNNGSTPMFNDINIYDLFVWMHYYVSRDTLLGGSEIWRDIDFAHEAPGFLPWHRLFLLLWEQEIRELTGDENFTVPYWDWRDAENCDICTDEYLGGRHPENPNLLSPASFFSSWQIICSRSEEYNSHQVLCDGTPEGPLLRNPGNHDKAKTPRLPSSADVEFCLSLTQYESGSMDRTANFSFRNTLEGFASPLTGIADPSQSSMHNALHIFMNGTMSQVQGSANDPIFLLHHAFVDSIFEQWLRRHRPLLEVYPEANAPIGHNRDSYMVPFIPLYRNGDFFITSKDLGYDYSYLQESDPGFYRNYIEPYLEQASRIWPWLLGAALVGAVIAAALSGLSSRLCLQKKKKKKQPQEERQPLLMDKDDYHSLLYQSHL
Expression Range	19-533aa
Protein Length	Full Length of Mature Protein
Mol. Weight	61.3 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	This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine. In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone.
Subcellular Location	Melanosome membrane; Single-pass type I membrane protein. Melanosome.
Protein Families	Tyrosinase family
Database References	KEGG: mmu:22173 STRING: 10090.ENSMUSP00000004770 UniGene: Mm.238127
Associated Diseases	Defects in Tyr result in various forms of albinism. Himalayan strain tyrosinase is temperature-sensitive.
Tissue Specificity	Expressed in the skin.

Gene Functions References

This study demonstrates the utility of CRISPR-Cas9 system in generating domain-specific in-frame deletions and helps gain further insights into structure-function of Tyr gene. PMID: 27224051
These results suggest that the tyrosinase-induced metabolism of rhodendrol causes melanocyte toxicity. PMID: 25713930
Data indicate that both ephedrannins A and B were competitive inhibitors of mushroom tyrosinase. PMID: 25857772
STAP-2 colocalized with tyrosinase in lysosomes and protected tyrosinase from protein degradation in B16F10 melanoma cells. PMID: 26023234
Docosahexaenoic acid inhibits melanogenesis in B16F10 cells in vitro through increased tyrosinase degradation. PMID: 24562306
Studied upregulation by Kaliziri extract of tyrosinase, TRP-1, TRP-2 and MITF expression in murine B16 melanoma cells. PMID: 24884952
The albino mutation of tyrosinase alters ocular angiogenic responsiveness. PMID: 23423728
Tyrosinase is mutated in the albino dorsal lateral geniculate nucleus, arising from retinal ganglion cell misspecification together with potential perturbations of early activity patterns in the albino retina. PMID: 22492037
activated by ascorbic acid in B16 melanoma via p38 MAPK signaling and upregulation of melanogenic regulatory factors PMID: 21667118
Effect of zibuganshenfang on the expression and activity of tyrosinase on B16 cells PMID: 22256768
the schisis phenotype caused by the Rs1 mutation is rescued by a Tyr mutation in the C57BL/6J genetic background, strongly suggesting that Tyr is the Mor1 gene. PMID: 20876567
Data suggest that accumulation of tyrosinase in the endoplasmic reticulum of melanocytes leads to ER stress and activation of the unfolded protein response. PMID: 20444203
Data show that interfering with p38 MAPK expression stimulates melanogenesis and tyrosinase family protein expression. PMID: 20053998
role of P protein and tyrosinase in oculocutaneous albinism PMID: 12028586
processing is controlled by pink-eyed dilution protein PMID: 12058062
identified the tyrosinase gene (Tyr) as a modifier of the drainage structure phenotype in developmental glaucoma PMID: 12624268
Tyrosinase maturation and oligomerization in the endoplasmic reticulum require a melanocyte-specific factor PMID: 12724309
investigation of the boundary activity of locus control regions in transgenic animals and cells PMID: 14576318
tyrosinase has a role in fatty acid regulation of pigmentation PMID: 14739285
Interactions between N-linked glycans and lectin chaperones help to minimize tyrosinase aggregation and also target non-native substrates for retro-translocation and subsequent degradation PMID: 15161941
Tyrosinase is a subject to post-Golgi quality control. PMID: 15760341
tyrosinase has roles in the development of the visual system, as shown in a transgenic mouse model [review] PMID: 16146766
tyrosinase and related proteins as physiological substrates of presenilins and link gamma-secretase activity with intracellular protein transport PMID: 16384915
These results therefore suggest that proteasomes, particularly p27 subunit, are directly involved in the regulation of melanin biosynthesis in mouse melanoma cells. PMID: 16879986
a 186 kb BAC containing the tyrosinase gene provides transgene expression in both RPE and melanocytes indicating the presence of regulatory sequences required for expression in the RPE PMID: 17196956
Gallic acid effectively suppressed Tyr activity. PMID: 17541153
The inhibitory effect of 4-hydroxybenzyl alcohol on melanogenesis is due to the direct inhibition of melanosomal Tyr activity, rather than to the suppression of Tyr gene. PMID: 17541167
analysis of the mammalian tyrosinase active site with loss of function mutations PMID: 17850513
these data demonstrate that Tyrp1 interacts directly with Tyrosinase in vivo, which may regulate the stability and trafficking of melanogenic enzymes and thus pigment synthesis. PMID: 18042623
Results describe the molecular detection of circulating melanoma cells by reverse transcription-polymerase chain reaction (RT-PCR) in human blood samples and in a xenograft mouse model. PMID: 18425346
the pigment-cell-specific cuproenzyme tyrosinase acquires copper only transiently and inefficiently within the trans-Golgi network of mouse melanocytes PMID: 18650808
tyrosinase as a beta1,6 branch containing glycoprotein: substrate of GnT-V PMID: 18655794
Data suggest that the tyrosinase promoter may be transiently active around E10 in subsets of precursor cells in the neural crest and intestines. PMID: 19220779

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.