Analytical Data
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Gene name
OCLN
- Application
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Alternative Names
OCLN；Occludin
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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
Q16625
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Expression Region
1-522aa
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AA Sequence
MSSRPLESPPPYRPDEFKPNHYAPSNDIYGGEMHVRPMLSQPAYSFYPED EILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTSLLGG SVGYPYGGSGFGSYGSGYGYGYGYGYGYGGYTDPRAAKGFMLAMAAFCFI AALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPT AQSSGSLYGSQIYALCNQFYTPAATGLYVDQYSYHYCVVDPQEAIAIVLG FMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKN VSAGTQDVPSPPSDYVERVDSPMAYSSNGKVNDKRFYPESSYKSTPVPEV VQELPLTSPVDDFRQPRYSSGGNFETPSKRAPAKGRAGRSKRTEQDHYET DYTTGGESCDELEEDWIREYPPITSDQQRQLYKRNFDTGLQEYKSLQSEL DEINKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNHC KQLKSKLSHIKKMVGDYDRQKT
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Molecular Weight
84 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
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Protein Description
OCLN, or Occludin, is a prominent integral membrane protein that plays a crucial role in the formation and maintenance of tight junctions between epithelial cells, which are essential for maintaining barrier integrity and regulating paracellular transport. Understanding the structure and function of OCLN is significant due to its implications in various physiological processes and pathophysiological conditions, including inflammation, cancer progression, and bacterial infections. Recent studies have highlighted the involvement of OCLN in cellular signaling pathways, indicating its potential role in modulating cell behavior and tissue homeostasis. Moreover, alterations in OCLN expression and localization have been linked to the disruption of tight junctions, contributing to increased permeability and the pathogenesis of diseases such as inflammatory bowel disease and cancer metastasis. The recombination of OCLN protein has thus emerged as a critical area of research, aiming to elucidate its functional mechanisms and interactions at the molecular level. This research aims to enhance our understanding of tight junction dynamics and develop therapeutic strategies targeting OCLN for disease intervention. By investigating the recombinant form of the OCLN protein, researchers hope to gain insights into its structural properties, interaction networks, and regulatory roles, providing a foundation for novel approaches to restore epithelial barrier function and address related health issues.
