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AB114189

Recombinant Human Occludin protein (GST tag N-Terminus)

Recombinant Human Occludin protein (GST tag N-Terminus)

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(1 Publication)

Recombinant Human Occludin protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 522 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

別名を表示する

Occludin, OCLN

1 Images
SDS-PAGE - Recombinant Human Occludin protein (GST tag N-Terminus) (AB114189)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Occludin protein (GST tag N-Terminus) (AB114189)

ab114189 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.

Key facts

発現系

Wheat germ

タグ

GST tag N-Terminus

アプリケーション

ELISA, WB, SDS-PAGE

applications

生物活性

No

アクセッション番号

Q16625

アニマルフリー

No

キャリアフリー

No

Human

バッファー組成

pH: 8 Constituents: 0.79% Tris HCl, 0.3% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

配列情報

[{"sequence":"MSSRPLESPPPYRPDEFKPNHYAPSNDIYGGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTSLLGGSVGYPYGGSGFGSYGSGYGYGYGYGYGYGGYTDPRAAKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSLYGSQIYALCNQFYTPAATGLYVDQYSYHYCVVDPQEAIAIVLGFMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKNVSAGTQDVPSPPSDYVERVDSPMAYSSNGKVNDKRFYPESSYKSTPVPEVVQELPLTSPVDDFRQPRYSSGGNFETPSKRAPAKGRAGRSKRTEQDHYETDYTTGGESCDELEEDWIREYPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT","proteinLength":"Full Length","predictedMolecularWeight":"83.53 kDa","actualMolecularWeight":null,"aminoAcidEnd":522,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q16625","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

出荷温度及び保存条件

出荷温度
Dry Ice
短期保存温度
-80°C
長期保存温度
-80°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Occludin is a protein that plays an important mechanical role in forming tight junctions which are specialized connections between neighboring cell membranes. Alternative names for this target include occludin-1. The occludin protein has a molecular weight of approximately 65 kDa. It is expressed in a variety of tissues but levels tend to be high in epithelial and endothelial cells where tight junctions are essential for barrier functions. Occludin acts as integral membrane protein contributing to the complex structures that seal spaces between cells.
Biological function summary

Occludin serves as an important component in maintaining cell-to-cell adhesion within tight junction complexes. It interacts with other tight junction proteins such as claudins and junctional adhesion molecules to regulate paracellular permeability. These interactions help maintain selective barrier properties of epithelial and endothelial layers preventing the passage of large molecules and pathogens while allowing passage of ions and small molecules. Occludin stabilizes the tight junctions by interacting with the cytoskeleton and signaling proteins that are important for tight junction assembly and maintenance.

Pathways

Occludin functions prominently in the regulation of tight junction integrity and barrier function. It participates in pathways such as the tight junction signaling pathway and the paracellular transport pathway. Occludin interacts with ZO-1 a scaffolding protein bridging its interaction with the actin cytoskeleton which supports the structural organization and function of tight junctions. This connectivity allows for regulation of the permeability and transport across the epithelial barrier.

Disruptions in occludin function are connected to conditions such as inflammatory bowel disease (IBD) and some cancers. In IBD abnormal occludin expression can compromise intestinal barrier function leading to increased intestinal permeability and an inflammatory response. In certain cancers loss of occludin expression is linked to increased invasiveness and metastasis due to weakened cell adhesion. The dysfunction of proteins like ZO-1 which interact with occludin in these pathways also contributes to these pathological states highlighting the importance of occludin's regulatory roles in maintaining cellular barrier integrity.

製品の性状

製品の状態

Liquid

一般的な情報

機能

May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions.. (Microbial infection) Acts as a coreceptor for hepatitis C virus (HCV) in hepatocytes.

配列の類似性

Belongs to the ELL/occludin family.

翻訳後修飾

Dephosphorylated by PTPRJ. The tyrosine phosphorylation on Tyr-398 and Tyr-402 reduces its ability to interact with TJP1. Phosphorylation at Ser-490 also attenuates the interaction with TJP1.. (Microbial infection) Cleaved by S.pyogenes SpeB protease; leading to its degradation (PubMed:23532847). Degradation by SpeB promotes bacterial translocation across the host epithelial barrier (PubMed:23532847).

製品プロトコール

ターゲットの情報

May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions.. (Microbial infection) Acts as a coreceptor for hepatitis C virus (HCV) in hepatocytes.
See full target information OCLN

文献 (1)

Recent publications for all applications. Explore the full list and refine your search

Virulence 9:879-894 PubMed29726306

2018

Secreted Giardia intestinalis cysteine proteases disrupt intestinal epithelial cell junctional complexes and degrade chemokines.

Applications

Unspecified application

Species

Unspecified reactive species

Jingyi Liu,Showgy Ma'ayeh,Dimitra Peirasmaki,Britta Lundström-Stadelmann,Lars Hellman,Staffan G Svärd
View all publications

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