Analytical Data
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Gene name
TMEM178
- Application
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Alternative Names
TMEM178A; TMEM178; PSEC0131; UNQ5926/PRO19820; Transmembrane Protein 178A
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NBL3
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Expression Region
1-297 aa
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AA Sequence
MEPRALVTALSLGLSLCSLGLLVTAIFTDHWYETDPRRHKESCERSRAGADPPDQKNRLMPLSHLPLRDSPPLGRRLLPGGPGRADPESWRSLLGLGGLDAECGRPVFATYSGLWRKCYFLGIDRDIDTLILKGIAQRCTAIKYHFSQPIRLRNIPFNLTKTIQQDEWHLLHLRRITAGFLGMAVAVLLCGCIVATVSFFWEESLTQHVAGLLFLMTGIFCTISLCTYAASISYDLNRLPKLIYSLPADVEHGYSWSIFCAWCSLGFIVAAGGLCIAYPFISRTKIAQLKSGRDSTV
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Molecular Weight
59.4 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
TMEM178, a member of the transmembrane protein family, has garnered attention in recent years due to its potential role in various biological processes, including cell signaling, immune response, and tumorigenesis. Research has suggested that TMEM178 may be implicated in the regulation of ion channels and has been linked to several diseases, making it a candidate for further study in recombinant protein applications. The ability to produce TMEM178 as a recombinant protein allows for detailed biophysical and biochemical characterizations, which are crucial for understanding its structure-function relationships. Furthermore, the study of TMEM178 can shed light on its interactions with other cellular components, providing insights into its mechanism of action in different physiological and pathological contexts. Given the protein’s potential involvement in multiple diseases, including cancer and autoimmune disorders, the exploration of TMEM178 through recombinant expression systems could facilitate the development of targeted therapeutic strategies and enhance our understanding of its biological significance.
