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SAB4200537

Sigma-Aldrich

Anti-Claudin-5 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

Anti-AWAL, Anti-BEC1, Anti-CLDN5, Anti-CPETRL1, Anti-TMVCF

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~23 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunohistochemistry: 20 μg/mL using formalin-fixed, paraffin-embedded human heart
western blot: 1-2 μg/mL using extracts of OVCAR-3 cells

UniProt accession no.

O00501

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CLDN5(7122)

General description

Claudin-5 is a member of claudin family. It is also known as CLDN5, beclin 1, TMVCF and CPETRL1 and is highly expressed in endothelial cells (ECs), including the blood-brain barrier.
Claudin-5 is encoded by the gene mapped to human chromosome 22q11.21.

Specificity

Anti-Claudin-5specifically recognizes human Claudin-5.

Immunogen

synthetic peptide corresponding to an internal sequence of human claudin-5, conjugated to KLH. The corresponding sequence is highly conserved (single amino acid substitution) in mouse and rat claudin-5.

Application

Anti-Claudin-5 antibody produced in rabbit has been used in immunofluorescence staining.
Anti-Claudin-5 antibody produced in rabbit may be used in several immunochemical techniques including immunoblotting (~23 kDa) and immunohistochemistry.

Biochem/physiol Actions

Claudin-5 gene is a downstream target of ETS-related gene (ERG), a transcription factor that regulates endothelial cell-restricted genes and is markedly repressed in response to inflammatory stimuli. Knockout of claudin-5 in mice is lethal, resulting in disruption of in the blood-brain barrier. Claudin-5 has been shown to be overexpressed in various tumors including lung adenocarcinomas but undetectable in squamous cells cell carcinomas.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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ETS-related gene (ERG) controls endothelial cell permeability via transcriptional regulation of the claudin 5 (CLDN5) gene
Yuan L, et al.
Test, 287(9), 6582-6591 (2012)
Marta Justyna Kozieł et al.
Cancers, 12(3) (2020-03-22)
Claudins are major integral proteins of tight junctions (TJs), the apical cell-cell adhesions that enable maintaining polarity of epithelial cells, their differentiation, and cell signaling. A number of studies have indicated that claudins might play a crucial role in both
Claudin-1 and claudin-5 expression patterns differentiate lung squamous cell carcinomas from adenocarcinomas
Paschoud S, et al.
Modern Pathology, 20(9), 947-947 (2007)
Janyerkye Tulyeu et al.
Microorganisms, 7(10) (2019-10-19)
Increased intestinal permeability is thought to underlie the pathogenesis of food allergy. We explore the mechanism responsible for changes in the morphology and function of the intestinal barrier using a rat model of food allergy, focusing on the contribution of

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