Analytical Data
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Gene name
TM
- Application
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Alternative Names
TM；Transmembrane Protein 127
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75204
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Expression Region
1-238aa
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AA Sequence
MYAPGGAGLPGGRRRRSPGGSALPKQPERSLASALPGALSITALCTALAEPAWLHIHGGTCSRQELGVSDVLGYVHPDLLKDFCMNPQTVLLLRVIAAFCFLGILCSLSAFLLDVFGPKHPALKITRRYAFAHILTVLQCATVIGFSYWASELILAQQQQHKKYHGSQVYVTFAVSFYLVAGAGGASILATAANLLRHYPTEEEEQALELLSEMEENEPYPAEYEVINQFQPPPAYTP
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Molecular Weight
25.8 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
TM recombinant proteins, derived from tandem repeat modules, have emerged as pivotal tools in molecular biology and biotechnology due to their unique structural and functional characteristics. These proteins are engineered by fusing repeating units, which allows for the customization of their properties, such as stability, solubility, and binding affinity. The research into TM recombinant proteins is driven by their diverse applications, ranging from use in vaccine development and targeted drug delivery systems to their role in fundamental biological studies. For instance, the repetitive nature of these proteins can facilitate the presentation of multiple epitopes, enhancing immune responses in vaccine formulations. Moreover, their modular architecture often enables the development of biosensors and diagnostic tools, as they can be designed to interact specifically with various biomolecules. Advances in genetic engineering and protein expression systems have further fueled the exploration of TM recombinant proteins, allowing scientists to produce these complex molecules at scale. The ongoing research aims to optimize their performance, elucidate their mechanisms of action, and explore new therapeutic avenues. Overall, the study of TM recombinant proteins represents a promising frontier in biotechnology, with the potential to significantly impact medicine, environmental science, and industrial applications.
