Analytical Data
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Gene name
TMEM150
- Application
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Alternative Names
Transmembrane Protein 150A. Transmembrane Protein 150
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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
Q86TG1
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Expression Region
1-271 aa
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AA Sequence
MTAWILLPVSLSAFSITGIWTVYAMAVMNHHVCPVENWSYNESCPPDPAEQGGPKTCCTLDDVPLISKCGSYPPESCLFSLIGNMGAFMVALICLLRYGQLLEQSRHSWVNTTALITGCTNAAGLLVVGNFQVDHARSLHYVGAGVAFPAGLLFVCLHCALSYQGATAPLDLAVAYLRSVLAVIAFITLVLSGVFFVHESSQLQHGAALCEWVCVIDILIFYGTFSYEFGAVSSDTLVAALQPTPGRACKSSGSSSTSTHLNCAPESIAMI
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Molecular Weight
55.2 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
TMEM150, a member of the transmembrane protein family, has garnered attention due to its potential role in various physiological and pathological processes. This protein is believed to be involved in regulating ion channels and has implications in cellular signaling pathways, making it integral to the study of neurobiology and cardiovascular health. The investigation into TMEM150 recombinant proteins has emerged from the need to understand its structure-function relationship, particularly in the context of ion homeostasis and neuronal excitability. Recent research has indicated that aberrations in TMEM150 expression could be linked to conditions such as neuropathic pain and cardiovascular diseases. By generating and characterizing recombinant TMEM150, researchers aim to elucidate its biological functions, interactions with other cellular components, and its influence on disease mechanisms. Understanding the molecular properties of TMEM150 not only contributes to the fundamental knowledge of transmembrane proteins but also opens avenues for developing therapeutic strategies targeting diseases associated with its dysregulation.
