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Merck

V4758

Sigma-Aldrich

Monoclonal Anti-Vascular Endothelial Growth Factor antibody produced in mouse

clone 26503, purified immunoglobulin, lyophilized powder

Synonym(e):

Anti-VEGF

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About This Item

MDL-Nummer:
UNSPSC-Code:
51111800
NACRES:
NA.41

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

26503, monoclonal

Form

lyophilized powder

Speziesreaktivität

primate, human

Methode(n)

capture ELISA: 2-8 μg/mL
neutralization: suitable
western blot: 1-2 μg/mL

Isotyp

IgG2b

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

Allgemeine Beschreibung

The antibody will neutralize the biological activity of recombinant human VEGF165. It also recognizes VEGF121.

Immunogen

purified recombinant Sf21-derived human VEGF (165 aa isoform).

Anwendung

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Monoclonal Anti-Vascular Endothelial Growth Factor antibody produced in mouse was used to block the interaction between VEGF and kinase domain receptor in Calf Pulmonary Aortic Endothelial (CPAE) cells.

Biochem./physiol. Wirkung

The vascular endothelial growth factor family consists of five members, VEGF-A to VEGF-E. They play important roles in important role in embryonic vasculogenesis, angiogenesis and homeostasis. The interaction between VEGFs and their respective receptors results in the activation of MAPK, PI3K, PKC, FAK and Src kinase pathways.

Physikalische Form

Lyophilized from a 0.2 μm solution in phosphate buffered saline containing carbohydrates.

Haftungsausschluss

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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Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Esther Grueso et al.
Journal of virology, 93(19) (2019-07-19)
As many tumor cells synthetize vascular endothelial growth factors (VEGF) that promote neo-vascularization and metastasis, frontline cancer therapies often administer anti-VEGF (α-VEGF) antibodies. To target the oncolytic parvovirus minute virus of mice (MVM) to the tumor vasculature, we studied the
Tali Lange et al.
The Journal of biological chemistry, 278(19), 17164-17169 (2003-02-25)
The splice forms of vascular endothelial growth factor (VEGF) differ in biological properties such as the receptor types that they recognize and their interaction with heparan sulfate proteoglycans. We have identified a new VEGF mRNA splice form encoding a VEGF
Giuseppa Gennaro et al.
Circulation, 107(2), 230-233 (2003-01-23)
The mechanisms responsible for the association between advanced age and atherosclerotic diseases are not clear. Because atherosclerosis develops in response to local endothelial injuries, we investigated the effect of aging on vascular healing and reendothelialization. Endothelium denudation was performed by
Dong-Kwon Lim et al.
Biomaterials, 77, 130-138 (2015-11-21)
Vascular endothelial growth factor 165 (VEGF165) is an important extracellular protein involved in pathological angiogenesis in diseases such as cancer, wet age-related macular degeneration (wet-AMD) and retinitis pigmentosa. VEGF165 exists in two different isoforms: the angiogenic VEGF165a, and the anti-angiogenic
R Binétruy-Tournaire et al.
The EMBO journal, 19(7), 1525-1533 (2000-04-04)
Vascular endothelial growth factor (VEGF) binding to the kinase domain receptor (KDR/FLK1 or VEGFR-2) mediates vascularization and tumor-induced angiogenesis. Since there is evidence that KDR plays an important role in tumor angiogenesis, we sought to identify peptides able to block

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