Analytical Data
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Gene name
TMEM158
- Application
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Alternative Names
(40 kDa BINP-binding protein)(p40BBP)(Ras-induced senescence protein 1)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WZ71
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Expression Region
21-300aa
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Molecular Weight
29.9 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
TMEM158 (Transmembrane protein 158) is a recently identified protein that has garnered attention in the fields of molecular biology and biochemistry due to its potential role in various cellular processes. Initially associated with certain diseases, including cancers and neurological disorders, TMEM158 is believed to influence cell proliferation, apoptosis, and signal transduction pathways. The study of TMEM158 recombinant proteins is crucial in elucidating its function and mechanisms within cells, as well as understanding its interactions with other proteins. Recombinant protein technologies allow for the overexpression and purification of TMEM158, facilitating detailed structural and functional analyses. Researchers aim to characterize the biochemical properties of TMEM158, examine its expression patterns, and explore its relevance in disease models. Additionally, understanding TMEM158's role could provide insights into novel therapeutic strategies and biomarker development. Given its potential implications in health and disease, TMEM158 stands as an intriguing target for ongoing research, highlighting the importance of recombinant protein studies in advancing our understanding of complex biological systems.
