Analytical Data
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Gene name
MITF
- Application
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Alternative Names
MITF；BHLHE32；Microphthalmia-associated transcription factor
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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
O75030
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Expression Region
1-520aa
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AA Sequence
MLEMLEYNHYQVQTHLENPTKYHIQQAQRQQVKQYLSTTLANKHANQVLSLPCPNQPGDH VMPPVPGSSAPNSPMAMLTLNSNCEKEGFYKFEEQNRAESECPGMNTHSRASCMQMDDVI DDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYGNQGLPPPGLTISNSCPANLPN IKRELTESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTI LKASVDYIRKLQREQQRAKELENRQKKLEHANRHLLLRIQELEMQARAHGLSLIPSTGLC SPDLVNRIIKQEPVLENCSQDLLQHHADLTCTTTLDLTDGTITFNNNLGTGTEANQAYSV PTKMGSKLEDILMDDTLSPVGVTDPLLSSVSPGASKTSSRRSSMSMEETEHTC
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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
MITF (Microphthalmia-associated transcription factor) is a critical transcription factor involved in various biological processes, including melanocyte development, pigmentation, and the maintenance of neural crest-derived cells. Its role in melanoma, a type of skin cancer, has garnered significant attention, as MITF is frequently found to be dysregulated in this disease. Research on MITF has revealed that it functions in a complex regulatory network, influencing cell differentiation and survival. The manipulation of MITF expression and activity offers potential therapeutic avenues for treating melanoma and other conditions linked to pigmentation anomalies. Recombination technologies used to generate MITF fusion proteins have provided essential insights into its functional domains and interactions with other cellular proteins. These studies are crucial for understanding the mechanisms underlying MITF-related diseases and for the development of targeted therapies. Furthermore, the exploration of MITF's role in cellular signaling pathways can shed light on its involvement in cancer progression and resistance to treatment. Overall, MITF and its recombinant protein studies represent a vital area of research that bridges basic science with potential clinical applications, offering hope for innovative strategies in cancer treatment and regenerative medicine.
