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AB114389

Recombinant Human Claudin 4 protein (GST tag N-Terminus)

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(1 Publication)

Recombinant Human Claudin 4 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 209 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

CPER, CPETR1, WBSCR8, CLDN4, Claudin-4, Clostridium perfringens enterotoxin receptor, Williams-Beuren syndrome chromosomal region 8 protein, CPE-R, CPE-receptor

1 Images
SDS-PAGE - Recombinant Human Claudin 4 protein (GST tag N-Terminus) (AB114389)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Claudin 4 protein (GST tag N-Terminus) (AB114389)

ab114389 analysed on a 12.5% SDS-PAGE Stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB, SDS-PAGE

applications

Biologically active

No

Accession

O14493

Animal free

No

Carrier free

No

Species

Human

Storage buffer

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>" } } }

Sequence info

[{"sequence":"MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV","proteinLength":"Full Length","predictedMolecularWeight":"48.73 kDa","actualMolecularWeight":null,"aminoAcidEnd":209,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"O14493","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

Claudin-4 also known as CLDN4 is a protein essential for tight junctions which are critical in maintaining the permeability barrier of epithelial cells. The protein has a molecular mass of approximately 22 kDa. Claudin-4 expresses notably in epithelial cells of various tissues including the kidney lung and gastrointestinal tract. In addition to its presence in normal tissues claudin-4 can also exhibit heightened expression in certain cancerous tissues making it a subject of interest in oncology research.
Biological function summary

Claudin-4 plays a significant role in paracellular transport and cell polarity. By assembling into complexes with other claudins and tight junction proteins claudin-4 regulates the selective permeability and homeostasis across cell layers. It functions as a component of tight junction strands contributing to their barrier properties. Interaction with proteins such as occludin and ZO-1 further defines its role in tight junction structure and function.

Pathways

Claudin-4 participates in critical biological processes such as epithelial cell signaling and apoptosis regulation. It interfaces with the epithelial-to-mesenchymal transition (EMT) pathway where claudin-4 expression influences cellular adhesion and motility. Claudin-4 also interacts with related claudin proteins in these pathways contributing to structural arrangement and pathway signaling precision.

Claudin-4 has associations with several types of cancers including pancreatic and ovarian cancer. Its consistent overexpression in these conditions suggests its involvement in tumorigenesis and metastasis. In the context of ovarian cancer claudin-4 may interact with proteins such as mesothelin which plays a role in cell adhesion and tumor progression. Investigating claudin-4's involvement in cancer can provide insights into potential therapeutic targets and diagnostic markers.

Specifications

Form

Liquid

General info

Function

Can associate with other claudins to regulate tight junction structural and functional strand dynamics (PubMed : 35773259, PubMed : 36008380). May coassemble with CLDN8 into tight junction strands containing anion-selective channels that convey paracellular chloride permeability in renal collecting ducts (By similarity) (PubMed : 36008380). May integrate into CLDN3 strands to modulate localized tight junction barrier properties (PubMed : 35773259, PubMed : 36008380). May disrupt strand assembly of channel-forming CLDN2 and CLDN15 and inhibit cation conductance (PubMed : 35773259, PubMed : 36008380). Cannot form tight junction strands on its own (PubMed : 35773259, PubMed : 36008380).

Sequence similarities

Belongs to the claudin family.

Post-translational modifications

Phosphorylated. Phosphorylation by EPHA2 is stimulated by EFNA1 and alters interaction with TJP1.

Product protocols

Target data

Can associate with other claudins to regulate tight junction structural and functional strand dynamics (PubMed : 35773259, PubMed : 36008380). May coassemble with CLDN8 into tight junction strands containing anion-selective channels that convey paracellular chloride permeability in renal collecting ducts (By similarity) (PubMed : 36008380). May integrate into CLDN3 strands to modulate localized tight junction barrier properties (PubMed : 35773259, PubMed : 36008380). May disrupt strand assembly of channel-forming CLDN2 and CLDN15 and inhibit cation conductance (PubMed : 35773259, PubMed : 36008380). Cannot form tight junction strands on its own (PubMed : 35773259, PubMed : 36008380).
See full target information CLDN4

Publications (1)

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

Oncotarget 10:2189-2202 PubMed31040910

2019

Targeting claudin-4 enhances CDDP-chemosensitivity in gastric cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Yukiko Nishiguchi,Rina Fujiwara-Tani,Takamitsu Sasaki,Yi Luo,Hitoshi Ohmori,Shingo Kishi,Shiori Mori,Kei Goto,Wataru Yasui,Masayuki Sho,Hiroki Kuniyasu
View all publications

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