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SAB4200538

Sigma-Aldrich

Anti-Claudin-5 (C-terminal) 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

Quality Level

200

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
indirect immunofluorescence: 1-2 μg/mL using MCF7 cells
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 (CLDN5) is encoded by the gene mapped to human chromosome 22q11.21. The encoded protein a 23kDa, four-transmembrane protein. It is mainly expressed in endothelial cells forming part of the blood-brain barrier (BBB).

Immunogen

synthetic peptide corresponding to a sequence at the C-terminus of human claudin-5, conjugated to KLH. The corresponding sequence is highly conserved in mouse claudin-5 (single amino acid substitution) and in rat claudin-5 (89% identity).

Application

Anti-Claudin-5 (C-terminal) antibody has been used in I
  • immunoblotting
  • immunofluorescence
  • immunohistochemistry
  • immunolabelling
  • immunocytochemistry

Biochem/physiol Actions

Claudin-5 (CLDN5), as an essential component of blood-brain barrier (BBB), plays a vital role in regulating the homeostasis of the central nervous system. Mutation in the gene increases the risk of susceptibility to schizophrenia. Overexpression of the gene is associated with the progression of pancreatic ductal adenocarcinomas. Loss of CLDN5 in cardiomyocytes and endothelial cells is one of the main reason behind human heart failure. Hence, early usage of CLDN5 can be considered as a potential therapeutic target for heart failure.
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.

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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flash_point_c

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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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Expression of Iron-Related Proteins at the Neurovascular Unit Supports Reduction and Reoxidation of Iron for Transport Through the Blood-Brain Barrier
Burkhart A
Molecular Neurobiology (2015)
Claudin-5 levels are reduced from multiple cell types in human failing hearts and are associated with mislocalization of ephrin-B1
Swager SA, et.al.
Cardiovascular Pathology : the Official Journal of the Society For Cardiovascular Pathology, 24, 160-167 (2015)
Intracellular cytoskeleton and junction proteins of endothelial cells in the porcine iris microvasculature
Yang H, et al.
Experimental Eye Research, 140, 106-116 (2015)
Priscilla Ern Zhi Tan et al.
Experimental eye research, 172, 36-44 (2018-04-03)
We previously demonstrated endothelial phenotype heterogeneity in the vortex vein system. This study is to further determine whether regional differences are present in the cytoskeleton, junctional proteins and phosphorylated tyrosine labeling within the system. The vortex vein system of twenty
Expression of iron-related proteins at the neurovascular unit supports reduction and reoxidation of iron for transport through the blood-brain barrier
Burkhart A, et al.
Molecular Neurobiology, 53(10), 7237-7253 (2016)
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