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Anti-Integrin αVβ3 Antibody, clone 27.1 (VNR-1) (Azide Free)

clone 27.1 (VNR-1), from mouse

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Integrin alpha-V, Integrin αVβ3, Vitronectin receptor subunit alpha, CD51, Integrin alpha-V heavy chain, Integrin alpha-V light chain, Integrin beta-3, Platelet membrane glycoprotein IIIa, GPIIIa, CD61

biological source


Quality Level

antibody form

purified antibody

antibody product type

primary antibodies


27.1 (VNR-1), monoclonal

species reactivity

human, rat


flow cytometry: suitable
immunohistochemistry: suitable (paraffin)



NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification


Gene Information

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This Item


Anti-Integrin beta-3 Antibody

biological source


biological source


biological source


biological source


Gene Information

human ... ITGAV(3685), ITGB3(3690)

Gene Information

human ... ITGAV(3685)

Gene Information

mouse ... Itga5(16402)

Gene Information

human ... ITGB3(3690)


27.1 (VNR-1), monoclonal


LM609, monoclonal


BMA5, monoclonal



species reactivity

human, rat

species reactivity

chicken, canine, monkey, rabbit, pig, human, avian, bovine

species reactivity


species reactivity

human, pig

UniProt accession no.

P05106, P06756

UniProt accession no.


UniProt accession no.

P09055, P11688

UniProt accession no.


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General description

Integrin alpha-V (UniProt P06756; CD51, Integrin alpha V, Vitronectin receptor subunit alpha) and Integrin beta-3 (UniProt P05106; CD61, GPIIIa, Platelet membrane glycoprotein IIIa, Vitronectin receptor subunit beta) are encoded by the ITGAV (MSK8, VNRA, VTNR; Gene ID 3685) and the ITGB3 (GP3A; Gene ID 3690) gene, respectively, in human. The integrin family of cell adhesion receptors consists of at least 16 membrane-associated heterodimers, composed of an alpha and beta subunit that associate in a non-covalent manner. The structure and functional diversity of the integrin family are based upon the pairing abilities of the individual alpha and beta subunits. Key to these molecular interactions between the integrin receptors and their respective ligands is the recognition of the Arg-Gly-Asp (RGD) sequence, known to be present in the extracellular matrix components fibronectin, vitronectin, collagen, fibrinogen, and von Willebrand factor. The involvement of integrins in vascular proliferation, adhesion, and wound repair has been well documented. The adhesion receptor alphaVbeta3 (also known as vitronectin receptor or VnR) appears to be selectively expressed on growing blood vessels and has been identified as a marker of angiogenic vascular tissue. Due to its involvement in angiogenesis, integrin alphaVbeta3 is among of the most studied integrin receptors.


Reacts with the human integrin alphaVbeta3. Shown to be specific for alphaVbeta3 by Loftus JC et al (1990) Science 249:915-918.


Epitope: Extracellular domain


Anti-Integrin αVβ3 Antibody, clone 27.1 (VNR-1) (Azide Free) is an antibody against Integrin αVβ3 for use in Immunohistochemistry (Paraffin), Flow Cytometry and Affects Function.
Flow Cytometry Analysis: A representative lot detected αvβ3 expression on SKOV3, OVCAR3, and IGROV1 human ovarian cancer cells. The surface expression was shown to be downregulated following treatment with SPARC (secreted protein acidic and rich in cysteine) from mouse parietal yolk sac (Said, N., et al. (2007). Am. J. Pathol. 170(3):1054–1063).
Flow Cytometry Analysis: A representative lot detected the surface expression of vitronection receptor (VnR) complex on CHO cells co-transfected with αv and either wild-type β3 or the Cam variant of Glanzmann′s thrombasthenia with the Asp119Tyr mutation (β3cam) (Loftus, J.C., et al. (1990). Science. 249(4971):915-918).
Affects Function: A representative lot blocked M21 human melanoma cells from adhering to fibrinogen (Fg), von Willebrand Factor (VWF), or fibronectin (FN) coated surface in a Integrin αvβ3-dependent manner (Pilch, J., et al. (2002). J. Biol. Chem. 277(24): 21930-21938).
Affects Function: A representative lot blocked metastatic human breast cancer cells from adhering to collagen I matrix (Felding-Habermann, B., et al. (2001). Proc. Natl. Acad. Sci. U. S. A. 98(4):1853-1858).
Research Category
Cell Structure
Research Sub Category
Adhesion (CAMs)


Evaluated by Immunohistochemistry in rat cerebral cortex tissue.

Immunohistochemistry Analysis: A 1:50 dilution of this antibody detected Integrin αVβ3 in rat cerebral cortex tissue.

Target description

116 kDa calculated

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgGκ antibody in buffer containing PBS, no 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.

Other Notes

Concentration: Please refer to lot specific datasheet.


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




Not applicable


Not applicable

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B Felding-Habermann et al.
Proceedings of the National Academy of Sciences of the United States of America, 98(4), 1853-1858 (2001-02-15)
Metastasis is the primary cause of death in human breast cancer. Metastasis to bone, lungs, liver, and brain involves dissemination of breast cancer cells via the bloodstream and requires adhesion within the vasculature. Blood cell adhesion within the vasculature depends
Jan Pilch et al.
The Journal of biological chemistry, 277(24), 21930-21938 (2002-04-06)
Shear-resistant arrest of circulating tumor cells is required for metastasis from the blood stream. Arrest during blood flow can be supported by tumor cell interaction with attached, activated platelets. This is mediated by tumor cell integrin alpha(v)beta3 and cross-linking plasma
J C Loftus et al.
Science (New York, N.Y.), 249(4971), 915-918 (1990-08-24)
The ligand-binding function of integrin adhesion receptors depends on divalent cations. A mutant alpha IIb beta 3 integrin (platelet gpIIb/IIIa) that lacks ligand recognition shows immunologic evidence of a perturbed interaction with divalent cations. This was found to be caused
Danielle Nader et al.
Viruses, 14(5) (2022-05-29)
The vascular barrier is heavily injured following SARS-CoV-2 infection and contributes enormously to life-threatening complications in COVID-19. This endothelial dysfunction is associated with the phlogistic phenomenon of cytokine storms, thrombotic complications, abnormal coagulation, hypoxemia, and multiple organ failure. The mechanisms
Neveen Said et al.
The American journal of pathology, 170(3), 1054-1063 (2007-02-27)
The matricellular glycoprotein SPARC (secreted protein acidic and rich in cysteine) has been accorded major roles in regulation of cell adhesion and proliferation, as well as tumorigenesis and metastasis. We have recently reported that in addition to its potent antiproliferative

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