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This Anti-Integrin αVβ3 Antibody, clone LM609, Alexa Fluor®488 conjugated is validated for use in FC, IF for the detection of Integrin αVβ3.
More>>This Anti-Integrin αVβ3 Antibody, clone LM609, Alexa Fluor®488 conjugated is validated for use in FC, IF for the detection of Integrin αVβ3. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
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 (Cheresh, 1991). The involvement of integrins in vascular proliferation, adhesion, and wound repair has been well documented. The adhesion receptor, integrin alphaVbeta3, appears to be selectively expressed on growing blood vessels and has been identified as a marker of angiogenic vascular tissue (Brooks, 1994). Due to its involvement in angiogenesis, integrin alphaVbeta3 is one of the most intensely studied of the integrin receptors.
References
Product Information
Format
AlexaFluor®488
HS Code
3002 15 90
Control
POSITIVE CONTROL: Human myeloma cell lines M21 and MoalphaV (Chen, 1995).
NEGATIVE CONTROL: Mo cells (this cell line was derived from M21 but does not express integrin alphaV
Chen, 1995).
Presentation
Purified immunoglobulin from Protein A Sepharose™ chromatography, conjugated to Alexa Fluor® 488. Final formulation in PBS 0.01M, SODIUM AZIDE 0.1%, PH7.1, 15mg/mL BSA.
This Anti-Integrin αVβ3 Antibody, clone LM609, Alexa Fluor®488 conjugated is validated for use in FC, IF for the detection of Integrin αVβ3.
Key Applications
Flow Cytometry
Immunofluorescence
Application Notes
Flow Cytometry: 1-3 μg LM609 per 0.5 x 10e6 cells in 100μL (Smith, 1996).Immunoprecipitation: Specifically immunoprecipitates the integrin alphaVbeta3 complex which, when resolved by SDS-PAGE under reducing conditions, results in an approximately 130 kDa band corresponding to the alphaV subunit and a 105 kDa band corresponding to the beta3 subunit (Cheresh, 1987).
Immunofluorescence: 5-10 μg/mL for staining of bFGF-treated 6 mm cryosections of chick chorioallantoic membrane fixed with acetone (Brooks, 1994). LM609 is also effective on 4% paraformaldehyde fixed, frozen tissues and cells. However it is not effective for immunohistochemical staining of paraffin-embedded tissue sections.
Inhibits adhesion of cells to vitronectin coated surfaces at 10-25 μg/mL.
Optimal working dilutions must be determined by the end user.
Biological Information
Immunogen
Purified adhesion receptor from the human melanoma cell line M21 (Cheresh, 1987).
Clone
LM609
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Mouse
Specificity
Reacts with the vitronectin receptor alphaVbeta3 complex, an RGD-directed adhesion receptor. LM609 has been demonstrated to block adhesion of a human melanoma cell line (M21) to vitronectin, fibrinogen and von Willebrand factor, as well as to a synthetic RGD containing peptide (Cheresh, 1987). In chick chorioallentoic membranes, LM609 was shown to block angiogenesis induced by bFGF and TNFalpha but had no effect on pre-existing vessels (Brooks, 1994). While LM609 does block cell attachment to RGD containing ligands, it does not interact directly with the RGD binding site. Instead, LM609 appears to be an allosteric inhibitor of integrin alphaVbeta3, which binds to a conformational epitope resulting from the post-translational association of the alphaV and beta3 subunits.
ITAGV encodes integrin alpha chain V. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. The I-domain containing integrin alpha V undergoes post-translational cleavage to yield disulfide-linked heavy and light chains, that combine with multiple integrin beta chains to form different integrins. Among the known associating beta chains (beta chains 1,3,5,6, and 8; 'ITGB1', 'ITGB3', 'ITGB5', 'ITGB6', and 'ITGB8'), each can interact with extracellular matrix ligands; the alpha V beta 3 integrin, perhaps the most studied of these, is referred to as the Vitronectin receptor (VNR). In addition to adhesion, many integrins are known to facilitate signal transduction.
FUNCTION: SwissProt: P06756 # The alpha-V integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willebrand factor. They recognize the sequence R-G-D in a wide array of ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. SIZE: 1048 amino acids; 116038 Da SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of an heavy and a light chain linked by a disulfide bond. Alpha-V associates with either beta-1, beta-3, beta-5, beta-6 or beta-8 subunit. Interacts with HIV-1 Tat. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: SwissProt: P06756 ## Belongs to the integrin alpha chain family. & Contains 7 FG-GAP repeats.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Alexa Fluor® is a registered trademark of Molecular Probes, Inc.
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 and Shipping Information
Storage Conditions
Maintain for 1 year at 2–8°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
The multifunctional mannose 6-phosphate/insulin-like growth factor 2 receptor (M6P/IGF2R) is considered a tumor suppressor. We report here that RNA interference with M6P/IGF2R expression in urokinase-type plasminogen activator (uPA)/urokinase-type plasminogen activator receptor (uPAR) expressing human cancer and endothelial cells resulted in increased pericellular plasminogen activation, cell adhesion, and higher invasive potential through matrigel. M6P/IGF2R silencing led also to the cell surface accumulation of urokinase and plasminogen and enhanced expression of alphaV integrins. Genetic rescue experiments and inhibitor studies revealed that the enhanced plasminogen activation was due to a direct effect of M6P/IGF2R on uPAR, whereas increased cell adhesion to vitronectin was dependent on alphaV integrin expression and not uPAR. Increased cell invasion of M6P/IGF2R knockdown cells was rescued by cosilencing both uPAR and alphaV integrin. Furthermore, we found that M6P/IGF2R expression accelerates the cleavage of uPAR. M6P/IGF2R silencing resulted in an increased ratio of full-length uPAR to the truncated D2D3 fragment, incapable of binding most uPAR ligands. We conclude that M6P/IGF2R controls cell invasion by regulating alphaV integrin expression and by accelerating uPAR cleavage, leading to the loss of the urokinase/vitronectin/integrin-binding site on uPAR.
Insulin-like growth factor-I promotes migration in human androgen-independent prostate cancer cells via the alphavbeta3 integrin and PI3-K/Akt signaling Marelli, M. et al. Int J Oncol., 28:723-730 (2006)
2005
Overexpression of alpha(v)beta6 integrin in serous epithelial ovarian cancer regulates extracellular matrix degradation via the plasminogen activation cascade. Ahmed, N, et al. Carcinogenesis, 23: 237-44 (2002)
2002
Recent evidence suggests that integrins are involved in the multi-step process of tumour metastasis. The biological relevance of alpha(v) integrins and associated beta-subunits in ovarian cancer metastasis was examined by analysing the expression of these cell surface receptors in nine ovarian cancer cell lines and also in the primary human ovarian surface epithelial cell line (HOSE). beta1, beta3 and beta5 subunits were present in all ten ovarian cell lines. beta6 subunit was present at varying levels in eight out of nine cancer cell lines but was absent in the HOSE cell line. Immunohistochemical staining showed that beta6 was present in both non-invasive (borderline) and high-grade ovarian cancer tissues but was absent in benign and normal ovarian tissue. High alpha(v)beta6 integrin expressing ovarian cancer cell lines had high cell surface expression of uPA and uPAR. Ovarian cancer cell lines expressing high to moderate level of alpha(v)beta6 integrin demonstrated ligand-independent enhanced levels of high molecular weight (HMW)-uPA and pro-matrix metalloproteinase 2 and 9 (pro-MMP-2 and pro-MMP-9) expression in the tumour-conditioned medium. High and moderate expression of alpha(v)beta6 integrin correlated with increased plasminogen-dependent degradation of extracellular matrix which could be inhibited by inhibitors of plasmin, uPA and MMPs or by monoclonal antibody against uPA, MMP-9 or alpha(v)beta6 integrin. These results suggest that endogenous de novo expression of alpha(v)beta6 integrin in ovarian cancer cells may contribute to their invasive potential, and that alpha(v)beta6 expression may play a role in ovarian cancer progression and metastasis.
On the mechanism of thrombin-induced angiogenesis: involvement of alphavbeta3-integrin. Tsopanoglou, Nikos E, et al. Am. J. Physiol., Cell Physiol., 283: C1501-10 (2002)
2002
Thrombin has been reported to be a potent angiogenic factor both in vitro and in vivo, and many of the cellular effects of thrombin may contribute to activation of angiogenesis. In this report we show that thrombin-treatment of human endothelial cells increases mRNA and protein levels of alphavbeta3-integrin. This thrombin-mediated effect is specific, dose dependent, and requires the catalytic site of thrombin. In addition, thrombin interacts with alphavbeta3 as demonstrated by direct binding of alphavbeta3 protein to immobilized thrombin. This interaction of thrombin with alphavbeta3-integrin, which is an angiogenic marker in vascular tissue, is of functional significance. Immobilized thrombin promotes endothelial cells attachment, migration, and survival. Antibody to alphavbeta3 or a specific peptide antagonist to alphavbeta3 can abolish all these alphavbeta3-mediated effects. Furthermore, in the chick chorioallantoic membrane system, the antagonist peptide to alphavbeta3 diminishes both basal and the thrombin-induced angiogenesis. These results support the pivotal role of thrombin in activation of endothelial cells and angiogenesis and may be related to the clinical observation of neovascularization within thrombi.
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