Mouse Monoclonal Integrin alpha V antibody. Suitable for IP, Flow Cyt, Neut, IHC-Fr and reacts with Human samples. Cited in 8 publications. Immunogen corresponding to Cell preparation containing ITGAV protein.
Preservative: 0.02% Sodium azide
Constituents: 99.98% PBS
| IP | Flow Cyt | Neut | IHC-Fr | |
|---|---|---|---|---|
| Human | Expected | Expected | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info - | Notes ab170190 - Mouse monoclonal IgG1, is suitable for use as an isotype control with this antibody. |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info Use at an assay dependent concentration. | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Human | Dilution info - | Notes Samples should be acetone fixed. |
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The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (PubMed:28302677). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (PubMed:29030430). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 and ITGAV:ITGB6 act as receptors for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation (PubMed:15184403, PubMed:22278742, PubMed:28117447). ITGAV:ITGB3 acts as a receptor for CD40LG (PubMed:31331973). ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and migration to IBSP (PubMed:10640428). (Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor for Adenovirus type C. (Microbial infection) Integrin ITGAV:ITGB5 and ITGAV:ITGB3 act as receptors for Coxsackievirus A9 and B1. (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Herpes virus 8/HHV-8. (Microbial infection) Integrin ITGAV:ITGB6 acts as a receptor for herpes simplex 1/HHV-1. (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Human parechovirus 1. (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for West nile virus. (Microbial infection) In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.
CD51, MSK8, VNRA, VTNR, ITGAV, Integrin alpha-V, Vitronectin receptor, Vitronectin receptor subunit alpha
Mouse Monoclonal Integrin alpha V antibody. Suitable for IP, Flow Cyt, Neut, IHC-Fr and reacts with Human samples. Cited in 8 publications. Immunogen corresponding to Cell preparation containing ITGAV protein.
Preservative: 0.02% Sodium azide
Constituents: 99.98% PBS
Reacts with Integrin Alpha V Beta 3. 23C6 may be useful for bone resorption modulation, osteoclast identification, receptor purification, malignant melanoma identification and treatment.
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Integrin alpha V beta 3 also known as integrin αvβ3 or avb3 integrin is a transmembrane receptor with a molecular weight of about 140 kDa. This protein is composed of the alpha V (αv) and beta 3 (β3) subunits. Integrin αvβ3 is widely expressed in various cell types including endothelial cells osteoclasts and some tumor cells. Its function involves mechanical interaction with the extracellular matrix (ECM) allowing cells to adhere to ECM proteins such as vitronectin and fibronectin. This integrin plays an important role in cell adhesion migration and survival.
Integrin alpha V beta 3 engages in various cellular processes by serving as a part of integrin complexes. It mediates signal transduction from the ECM to the cell interior influencing cellular responses such as shape changes survival and proliferation. The receptor regulates angiogenesis which is the formation of new blood vessels and osteoclast-mediated bone resorption. These functions are essential for tissue remodeling and repair. The integrin can also modulate immune responses by interacting with immune cells affecting inflammation and wound healing processes.
Integrin alpha V beta 3 is an important component in signaling pathways such as the PI3K/AKT and MAPK pathways. These pathways facilitate the integrin's role in cell migration growth and survival. It interacts with proteins like focal adhesion kinase (FAK) and SRC kinase bridging signals from the ECM to intracellular signaling cascades. The integrin's ability to bind ligands and initiate these pathways makes it an important player in cellular responses to the extracellular environment influencing how cells align mechanically and biochemically.
Integrin alpha V beta 3 has significant associations with cancer progression and osteoporosis. In various cancers including melanoma and breast cancer overexpression of this integrin supports tumor angiogenesis and metastasis connecting its role with angiogenic growth factors and matrix metalloproteinases. In osteoporosis it collaborates with proteins like osteopontin promoting osteoclast attachment to the bone matrix thereby influencing bone degradation. Understanding its role in these disorders highlights potential therapeutic targets for inhibiting unwanted angiogenesis and excessive bone resorption.
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