Analytical Data
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Gene name
CLDN11
- Application
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Alternative Names
CLDN11；OSP；OTM；Claudin-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
O75508
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Expression Region
1-207aa
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AA Sequence
MVATCLQVVGFVTSFVGWIGVIVTTSTNDWVVTCGYTIPTCRKLDELGSKGLWADCVMATGLYHCKPLVDILILPGYVQACRALMIAASVLGLPAILLLLTVLPCIRMGQEPGVAKYRRAQLAGVLLILLALCALVATIWFPVCAHRETTIVSFGYSLYAGWIGAVLCLVGGCVILCCAGDAQAFGENRFYYTAGSSSPTHAKSAHV
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Molecular Weight
23.5 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
CLDN11, or Claudin 11, is a critical tight junction protein predominantly expressed in oligodendrocytes, the myelinating cells of the central nervous system. Its primary function involves regulating the paracellular permeability of ions and small molecules, contributing to the maintenance of the blood-brain barrier (BBB) and ensuring proper neuronal function. Research into CLDN11 has gained momentum due to its potential implications in neurological disorders, such as multiple sclerosis and other demyelinating diseases, where the integrity of the BBB is compromised. The study of CLDN11 recombinant proteins aims to elucidate its structural and functional properties, particularly how it forms tight junctions and interacts with other cellular components. By generating and characterizing recombinant CLDN11, researchers can investigate its role in cellular signaling pathways, its potential as a therapeutic target, and its involvement in disease mechanisms. Experimental approaches often include the use of cell cultures, in vivo models, and advanced imaging techniques to assess the physiological impact of CLDN11 modulation. Understanding the biophysical properties and regulation of CLDN11 is essential for developing strategies to enhance CNS repair and mitigate neuroinflammation, thereby paving the way for innovative treatments for related neurological conditions.
