Analytical Data
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Gene name
TMEM113
- Application
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Alternative Names
WD repeat-containing Protein 82
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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
Q6UXN9
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Expression Region
1-137 aa
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AA Sequence
MPSLPTTNCVHSLQMIPPLSPAPNQELVLGLCYMSYLAFLYMTFDFCCLYFSTVYAPSFKYICVHTDTHICVCVCIYLSSVVSKSSAEADGVLQPRRHPASLLIVFATSISESSLLIFSFQKTEAKLIVFAVSLAAK
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Molecular Weight
41.5 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
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Protein Description
TMEM113, a member of the transmembrane protein family, has garnered interest due to its potential roles in various biological processes, including cellular signaling, membrane dynamics, and cellular stress responses. Recent studies have suggested that TMEM113 may be implicated in important physiological functions such as cell proliferation, differentiation, and apoptosis, as well as in pathological conditions like cancer and neurodegenerative diseases. The exploration of TMEM113 recombinant proteins has become essential for elucidating its molecular mechanisms and interacting partners. By generating and studying these recombinant proteins, researchers aim to clarify TMEM113's functional roles in cellular environments, investigate its structural properties, and assess its potential as a therapeutic target. The ability to produce TMEM113 in a recombinant form allows for detailed biochemical characterization, enabling the identification of its interaction networks and influence on cellular pathways. This research not only contributes to a better understanding of TMEM113’s biological significance but also holds promise for future therapeutic applications, particularly in disease contexts where TMEM113's dysregulation is observed. Overall, the study of TMEM113 recombinant proteins represents a vital step toward unraveling the complexities of its functions in health and disease.
