Analytical Data
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Gene name
CLEC11A
- Application
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Alternative Names
CLEC11A；CLECSF3；LSLCL；SCGF；C-type lectin domain family 11 member A
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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
Q9Y240
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Expression Region
22-323aa
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AA Sequence
MASMTGGQQMGRGHHHHHHENLYFQGGEFARGAEREWEGGWGGAQEEERE REALMLKHLQEALGLPAGRGDENPAGTVEGKEDWEMEEDQGEEEEEEATP TPSSGPSPSPTPEDIVTYILGRLAGLDAGLHQLHVRLHALDTRVVELTQG LRQLRNAAGDTRDAVQALQEAQGRAEREHGRLEGCLKGLRLGHKCFLLSR DFEAQAAAQARCTARGGSLAQPADRQQMEALTRYLRAALAPYNWPVWLGV HDRRAEGLYLFENGQRVSFFAWHRSPRPELGAQPSASPHPLSPDQPNGGT LENCVAQASDDGSWWDHDCQRRLYYVCEFPF
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Molecular Weight
37 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
CLEC11A, a member of the C-type lectin superfamily, has garnered attention due to its involvement in various biological processes, including immune response and tissue regeneration. Initially identified as a protein expressed in the bone marrow, CLEC11A is now recognized for its essential role in hematopoiesis and its potential implications in diseases such as cancer and inflammation. Recent studies have highlighted its significance in the regulation of mesenchymal stem cell proliferation and differentiation, suggesting that CLEC11A may play a critical role in tissue repair and regenerative medicine. Researchers are increasingly focusing on the recombinant form of CLEC11A to elucidate its functional roles and mechanisms of action. These investigations are facilitating the exploration of its therapeutic potential, particularly in enhancing stem cell therapies and improving outcomes in regenerative medicine. The ongoing research aims to provide a deeper understanding of CLEC11A’s signaling pathways and interactions with other cellular components, which could lead to novel strategies for treating various degenerative and inflammatory disorders. As the landscape of regenerative therapies evolves, the characterization of CLEC11A as a functional biomolecule holds promise for innovative applications in cell-based therapies and tissue engineering.
