Analytical Data
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Gene name
MTR
- Application
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Alternative Names
MTR；Myotubularin-related Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99707
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Expression Region
1094-1203aa
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AA Sequence
RDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHE RVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLA DIEQSTGIRL
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Molecular Weight
38 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
MTR (methionine synthase reductase) is a crucial enzyme involved in the methionine cycle and plays a vital role in cellular metabolism and the regulation of homocysteine levels. Methionine is an essential amino acid that is critical for various biological processes, including protein synthesis and the production of S-adenosylmethionine, a key methyl donor in numerous methylation reactions. The MTR enzyme functions by catalyzing the conversion of homocysteine to methionine, using vitamin B12 as a cofactor, and is particularly important in the context of methylation processes that can influence gene expression and cellular function. Recent research on MTR protein has focused on understanding its structure, function, and regulation, particularly in the context of diseases associated with methionine metabolism, such as cardiovascular disorders and neurodegenerative diseases. Additionally, mutations in the MTR gene can lead to severe metabolic disorders, making the characterization of this protein critical for both basic biology and clinical applications. Advances in recombinant protein technology have facilitated the production of MTR in vitro, enabling researchers to investigate its properties and interactions in detail, thus contributing to our understanding of its role in health and disease. The study of MTR proteins holds significant promise for the development of therapeutic strategies aimed at modulating methionine metabolism and addressing related metabolic diseases.
