Analytical Data
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Gene name
DNAH11
- Application
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Alternative Names
DNAH11；Dynein axonemal heavy chain 11
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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
Q96DT5
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Expression Region
全长
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AA Sequence
full
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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
DNAH11 is a member of the dynein family of motor proteins, specifically known for its role in the functioning of cilia and flagella. It plays a critical role in the proper movement of cilia, which are essential for various physiological processes, including the movement of mucus in the respiratory tract and the proper functioning of the reproductive system. Mutations in the DNAH11 gene have been associated with primary ciliary dyskinesia (PCD), a genetic disorder characterized by impaired ciliary function, leading to respiratory issues, infertility, and other complications. The investigation of DNAH11 recombinant protein has garnered significant interest as it helps to elucidate the protein's structure, function, and interactions within the cellular context. By expressing and purifying recombinant DNAH11, researchers aim to explore its biochemical properties, analyze its role in ciliary movement, and understand how specific mutations affect its function. This research is vital for developing potential therapeutic strategies to address conditions linked to abnormal ciliary function and advancing our understanding of dynein-mediated motility in various biological systems. Understanding the mechanisms involving DNAH11 could also provide insights into broader implications for diseases associated with ciliary dysfunction, thereby impacting both clinical and therapeutic approaches in the field of genetics and molecular biology.
