Analytical Data
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Gene name
M1
- Application
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Alternative Names
M1；CLTNM；AP-1 complex subunit mu-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
Q9BXS5
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Expression Region
2-423aa
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AA Sequence
SASAVYVLD LKGKVLICRN YRGDVDMSEV EHFMPILMEK EEEGMLSPIL AHGGVRFMWI KHNNLYLVAT SKKNACVSLV FSFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR SEGIKYRKNE VFLDVIESVN LLVSANGNVL RSEIVGSIKM RVFLSGMPEL RLGLNDKVLF DNTGRGKSKS VELEDVKFHQ CVRLSRFEND RTISFIPPDG EFELMSYRLN THVKPLIWIE SVIEKHSHSR IEYMIKAKSQ FKRRSTANNV EIHIPVPNDA DSPKFKTTVG SVKWVPENSE IVWSIKSFPG GKEYLMRAHF GLPSVEAEDK EGKPPISVKF EIPYFTTSGI QVRYLKIIEK SGYQALPWVR YITQNGDYQL RTQ
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Molecular Weight
48.5 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
The study of M1 recombinant protein has gained significant attention in recent years due to its potential applications in vaccine development and therapeutic interventions. M1, a critical protein derived from various pathogens, notably viruses like influenza and other viral diseases, plays a vital role in viral replication and pathogenesis. Researchers have focused on M1 because of its ability to induce strong immune responses, making it a promising candidate for subunit vaccines. The recombinant production of M1 allows for a safer and more efficient manufacturing process compared to traditional methods, which often involve live pathogens. Additionally, the characterization of M1 protein's structure and function enhances our understanding of viral mechanisms, paving the way for innovative antiviral strategies. Recent advances in genetic engineering and protein expression techniques have further facilitated the optimization of M1 protein production, enabling large-scale applications. As the world faces emerging infectious diseases, the study of M1 recombinant protein not only contributes to fundamental virology but also holds promise for developing effective therapeutic solutions and vaccines, addressing urgent public health challenges.
