Analytical Data
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Gene name
TMEM38B
- Application
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Alternative Names
TMEM38B; C9orf87; Trimeric intracellular cation channel type B; TRIC-B; TRICB; Transmembrane Protein 38B
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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
Q9NVV0
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Expression Region
1-291 aa
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AA Sequence
MDSPWDELALAFSRTSMFPFFDIAHYLVSVMAVKRQPGAAALAWKNPISSWFTAMLHCFGGGILSCLLLAEPPLKFLANHTNILLASSIWYITFFCPHDLVSQGYSYLPVQLLASGMKEVTRTWKIVGGVTHANSYYKNGWIVMIAIGWARGAGGTIITNFERLVKGDWKPEGDEWLKMSYPAKVTLLGSVIFTFQHTQHLAISKHNLMFLYTIFIVATKITMMTTQTSTMTFAPFEDTLSWMLFGWQQPFSSCEKKSEAKSPSNGVGSLASKPVDVASDNVKKKHTKKNE
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Molecular Weight
58.9 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
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Protein Description
TMEM38B, a member of the transmembrane protein family, has garnered significant interest due to its potential role in mediating calcium homeostasis in cells. Structurally, TMEM38B is an integral membrane protein thought to localize to the endoplasmic reticulum, where it may function as a calcium leak channel, thereby influencing intracellular calcium levels and various signaling pathways. Research has indicated that dysregulation of calcium signaling is implicated in a wide range of diseases, including neurodegenerative disorders and cancer. Consequently, understanding the functional mechanisms of TMEM38B is critical for elucidating its physiological roles and potential pathophysiological implications. Recombinant TMEM38B protein production allows researchers to study its properties in vitro, facilitating investigations into its structure-function relationships and interactions with other proteins. By utilizing techniques such as site-directed mutagenesis and electrophysiological assays, scientists can dissect the molecular mechanisms governing TMEM38B's activity, which may ultimately lead to novel therapeutic strategies targeting calcium signaling pathways in various diseases. As research progresses, insights gained from TMEM38B studies may provide significant contributions to the fields of cell biology and molecular medicine, underscoring the protein's emerging importance in health and disease.
