Analytical Data
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Gene name
TMPRSS11A
- Application
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Alternative Names
TMPRSS11A；ECRG1；HATL1；HESP；Transmembrane protease serine 11A
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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
Q6ZMR5
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Expression Region
40-421aa
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AA Sequence
HFLVFDQKKEYYHGSFKILDPQINNNFGQSNTYQLKDLRETTENLVSQVDEIFIDSAWKKNYIKNQVVRLTPEEDGVKVDVIMVFQFPSTEQRAVREKKIQSILNQKIRNLRALPINASSVQVNAMSSSTGELTVQASCGKRVVPLNVNRIASGVIAPKAAWPWQASLQYDNIHQCGATLISNTWLVTAAHCFQKYKNPHQWTVSFGTKINPPLMKRNVRRFIIHEKYRSAAREYDIAVVQVSSRVTFSDDIRRICLPEASASFQPNLTVHITGFGALYYGGESQNDLREARVKIISDDVCKQPQVYGNDIKPGMFCAGYMEGIYDACRGDSGGPLVTRDLKDTWYLIGIVSWGDNCGQKDKPGVYTQVTYYRNWIASKTGI
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Molecular Weight
44.3 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
TMPRSS11A, also known as Transmembrane Protease, Serine 11A, is a member of the type II transmembrane serine protease family, which plays a crucial role in various biological processes, including tissue remodeling, cell migration, and host-pathogen interactions. Research into TMPRSS11A has gained significance due to its potential involvement in viral entry pathways, particularly how it interacts with viral proteins to facilitate the infection of host cells. Understanding the structure and function of TMPRSS11A is critical for elucidating its role in disease mechanisms, especially in the context of respiratory viruses, where serine proteases are known to cleave viral envelope glycoproteins, thereby enabling the virus to penetrate the host cell membrane. Moreover, alterations in the expression or activity of TMPRSS11A have been implicated in various pathological conditions, including cancer and viral infections, making it a potential target for therapeutic intervention. Recent studies have aimed to characterize the biochemical properties, substrate specificity, and biological roles of TMPRSS11A, using recombinant protein techniques to produce and purify the enzyme. The insights gained from these investigations may pave the way for novel antiviral strategies and enhance our understanding of proteolytic regulation in health and disease.
