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MABT129

Sigma-Aldrich

Anti-VE-Cadherin Antibody (CD144), clone BV9

clone BV9, from mouse

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Synonym(s):
Cadherin-5, 7B4 antigen, Vascular endothelial cadherin, VE-cadherin, CD144
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

BV9, monoclonal

species reactivity

human

technique(s)

activity assay: suitable
immunocytochemistry: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... CDH5(1003)

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V1514SAB1306131SAB4504676
Gene Information

human ... CDH5(1003)

Gene Information

human ... CDH5(1003)

Gene Information

human ... CDH5(1003)

Gene Information

human ... CDH5(1003)

biological source

mouse

biological source

rabbit

biological source

rabbit

biological source

rabbit

species reactivity

human

species reactivity

human

species reactivity

human

species reactivity

human, rat, mouse

antibody form

purified antibody

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

isotype

IgG2aκ

isotype

-

isotype

-

isotype

-

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General description

Also known as CD144, human Vascular Endothelial (VE)-cadherin is a calcium-dependent adhesion molecule strictly located at cell to cell junctions. VE-cadherin is present in all types of endothelium (veins, arteries, capillary and large vessels). Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cadherins are reported to play an important role in angiogeneis and in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha catenin forming a link to the cytoskeleton.

Specificity

This antibody recognizes the extracellular domain of VE-Cadherin.

Immunogen

Epitope: Extracellular domain.
Recombinant protein corresponding to the extracellular domain of human VE-Cadherin.

Application

Activity Assay Analysis: A representative lot from an independent laboratory increased endothelial permeability, inhibited the organization of vasclular-like structures, and prevented the protective effect of VEGF against apoptosis in endothelial cells.
Research Category
Cell Structure
Research Sub Category
Adhesion (CAMs)
This VE-Cadherin antibody is validated for use in ICC & Enzyme Assay for the detection of the VE-Cadherin protein.

Quality

Evalutated by Immunocytochemistry in HUVEC cells.

Immunocytochemistry Analysis: 1 µg/mL of this antibody detected VE-Cadherin in HUVEC cells.

Target description

88 kDa calculated

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG2aκ in buffer containing PBS without 0.05% sodium azide.

Storage and Stability

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Analysis Note

Control
HUVEC cells

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.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Justyna Lisowska et al.
Journal of cell science, 131(15) (2018-07-22)
Endothelial integrity relies on a mechanical crosstalk between intercellular and cell-matrix interactions. This crosstalk is compromised in hemorrhagic vascular lesions of patients carrying loss-of-function mutations in cerebral cavernous malformation (CCM) genes. RhoA/ROCK-dependent cytoskeletal remodeling is central to the disease, as
Cécile Otten et al.
EMBO molecular medicine, 10(10) (2018-09-06)
Cerebral cavernous malformations (CCMs) are vascular lesions in the central nervous system causing strokes and seizures which currently can only be treated through neurosurgery. The disease arises through changes in the regulatory networks of endothelial cells that must be comprehensively
Matthew J Stebbins et al.
Biotechnology journal, 13(2) (2017-09-30)
The blood-brain barrier (BBB) is critical to central nervous system (CNS) health. Brain microvascular endothelial cells (BMECs) are often used as in vitro BBB models for studying BBB dysfunction and therapeutic screening applications. Human pluripotent stem cells (hPSCs) can be
Ilse S Pienaar et al.
Neurobiology of disease, 74, 392-405 (2014-12-24)
Deep brain stimulation (DBS) of the subthalamic nucleus (STN) has become an accepted treatment for motor symptoms in a subset of Parkinson's disease (PD) patients. The mechanisms why DBS is effective are incompletely understood, but previous studies show that DBS

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