Analytical Data
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Gene name
TMPRSS11D
- Application
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Alternative Names
TMPRSS11D; HAT; Transmembrane protease serine 11D; Airway trypsin-like protease
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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
O60235
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Expression Region
1-418 aa
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AA Sequence
MYRPARVTSTSRFLNPYVVCFIVVAGVVILAVTIALLVYFLAFDQKSYFYRSSFQLLNVEYNSQLNSPATQEYRTLSGRIESLITKTFKESNLRNQFIRAHVAKLRQDGSGVRADVVMKFQFTRNNNGASMKSRIESVLRQMLNNSGNLEINPSTEITSLTDQAAANWLINECGAGPDLITLSEQRILGGTEAEEGSWPWQVSLRLNNAHHCGGSLINNMWILTAAHCFRSNSNPRDWIATSGISTTFPKLRMRVRNILIHNNYKSATHENDIALVRLENSVTFTKDIHSVCLPAATQNIPPGSTAYVTGWGAQEYAGHTVPELRQGQVRIISNDVCNAPHSYNGAILSGMLCAGVPQGGVDACQGDSGGPLVQEDSRRLWFIVGIVSWGDQCGLPDKPGVYTRVTAYLDWIRQQTGI
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Molecular Weight
72.7 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
TMPRSS11D, a member of the transmembrane protease serine (TMPRSS) family, has garnered attention in recent years due to its potential roles in various physiological and pathological processes. This protein is primarily expressed in the epithelial tissues and has been implicated in the regulation of several biological functions, including cell signaling and tissue remodeling. Research indicates that TMPRSS11D may play a crucial role in viral entry mechanisms, particularly in the context of respiratory viruses. The understanding of its enzymatic activity and substrate specificity may provide insights into its involvement in diseases such as cancer and viral infections. Furthermore, the reconstitution of TMPRSS11D as a recombinant protein allows for detailed biochemical studies, potentially aiding in the identification of small-molecule inhibitors or therapeutic agents. By elucidating the function and mechanisms of action of TMPRSS11D, researchers aim to uncover novel strategies for targeting its activity in disease contexts, thus highlighting the importance of this protease in both basic research and clinical applications.











