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SAB4200815

Sigma-Aldrich

Anti-VEGF165 antibody, Mouse monoclonal

clone VG-20, purified from hybridoma cell culture

Synonyme(s) :

VEGF-A, VPF, Vascular endothelial growth factor A, Vascular permeability factor

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Forme d'anticorps

purified from hybridoma cell culture

Type de produit anticorps

primary antibodies

Clone

VG-20, monoclonal

Espèces réactives

human

Conditionnement

antibody small pack of 25 μL

Concentration

~1 mg/mL

Technique(s)

immunoblotting: 1-2 μg/mL using recombinant human VEGFA protein expressed in HEK-293

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... VEGF165(7422)

Description générale

VEGFA - Vascular Endothelial Growth Factor A, also known as or Vascular permeability factor (VPF), is a major signaling growth factor member of the VEGF family, sub-group of the Platelet-Derived Growth Factor (PDFG) proteins, which is characterized by its conserved cystine-knot structure.1 VEGF expression is up regulated in hypoxia and in many types of cancers. Furthermore, VEGF receptors (VEGFR1 and VEGFR2) are also overexpressed in several tumors and studies have shown that high levels of VEGF correlates with poor prognosis.1-8 Inhibition of VEGF mediated angiogenesis signaling pathways have potential in angiogenesis-related disease therapy, this can be achieved by blocking either the circulating VEGF using Anti-VEGF antibodies such as Bevacizumab and Aflibercept5 or by VEGFR-2 inhibition using small molecules such as Gamabufotalin (CS-6) and Arenobufagin.6-8

Spécificité

Monoclonal Anti-VEGF165 specifically recognizes human VEGFA isoform VEGF165 and does not recognize VEGF121 isoform.

Immunogène

Recombinant VEGF165 protein

Application

The antibody is recommended to use in various immunological techniques, including Immunoblot (~21 kDa). Detection of the VEGF165 band by Immunoblotting is specifically inhibited by the immunogen.

Actions biochimiques/physiologiques

VEGF proteins are involved in angiogenesis and vasculogenesis, they predominantly activate proliferation and survival of endothelial cells and migration in non-endothelial cells.1VEGFA have several isoforms due to alternative splicing mainly at exons 6-8. The VEGF exon 8 splicing isoforms are divided into two groups, the “pro-angiogenic” VEGFxxxa isoforms considered to be activators of proliferation, survival and angiogenesis and the VEGFxxxb isoforms that are considered as “anti-angiogenic”.2

Forme physique

Supplied as a solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as a preservative.

Stockage et stabilité

For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Clause de non-responsabilité

Unless otherwise stated in our catalog 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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Flavia Plastino et al.
Experimental eye research, 206, 108518-108518 (2021-02-28)
Echinomycin (EKN), an inhibitor of hypoxia-inducible factor (HIF)-1 DNA-binding activity, has been implied as a possible therapeutic agent in ischemic diseases. Here, we assess EKN in hypoxia-driven responses in vitro using human primary adult retinal pigment epithelium cells (aRPE) and
Pooja Yadav et al.
iScience, 26(6), 106804-106804 (2023-05-26)
Alternative splicing of vascular endothelial growth factor A (VEGFA) generates numerous isoforms with unique roles in tumor angiogenesis, and investigating the underlying mechanism during hypoxia necessitates diligent pursuance. Our research systematically demonstrated that the splicing factor SRSF2 causes the inclusion

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