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Rabbit Anti-ITGAV Recombinant Antibody (BA0158) (CBMAB-0405CQ)

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Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat
Clone
BA0158
Antibody Isotype
IgG
Application
IHC-P, WB

Basic Information

Immunogen
Human Integrin beta 1 aa 1-250
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Integrin Subunit Alpha V
Introduction
Integrins serve as major receptors for extracellular matrix (ECM)-mediated cell adhesion and migration, cytoskeletal organization, cell proliferation, survival, and differentiation. Alpha-V integrins comprise a subset sharing a common alpha-V subunit combined with 1 of 5 beta subunits. Integrins are heterodimeric integral membrane proteins composed of an alpha subunit and a beta subunit that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha V subunit. The gene contains 30 exons and spans over 93 kb of genomic DNA. The heterodimer consisting of alpha V and beta 3 subunits is also known as the vitronectin receptor. This integrin may regulate angiogenesis and cancer progression. Alternative splicing results in multiple transcript variants. Note that the integrin alpha 5 and integrin alpha V subunits are encoded by distinct genes.
Entrez Gene ID
Human3685
Mouse16410
Rat296456
UniProt ID
HumanP06756
MouseP43406
RatF1LZX9
Alternative Names
CD51; MSK8; VNRA; VTNR
Function
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 a receptor 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 act as a receptor for CD40LG (PubMed:31331973).
(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.
Biological Process
AngiogenesisManual Assertion Based On ExperimentIEP:UniProtKB
Apolipoprotein A-I-mediated signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Apoptotic cell clearanceManual Assertion Based On ExperimentIGI:BHF-UCL
Calcium ion transmembrane transportManual Assertion Based On ExperimentIDA:UniProtKB
Cell adhesionManual Assertion Based On ExperimentIDA:BHF-UCL
Cell adhesion mediated by integrinManual Assertion Based On ExperimentIDA:UniProtKB
Cell migrationManual Assertion Based On ExperimentIMP:BHF-UCL
Cell-matrix adhesionManual Assertion Based On ExperimentIMP:UniProtKB
Cell-substrate adhesionManual Assertion Based On ExperimentIMP:UniProtKB
Endodermal cell differentiationManual Assertion Based On ExperimentIMP:UniProtKB
Entry into host cell by a symbiont-containing vacuole1 PublicationNAS:BHF-UCL
ERK1 and ERK2 cascadeISS:BHF-UCL
Extrinsic apoptotic signaling pathway in absence of ligandISS:BHF-UCL
Heterotypic cell-cell adhesionManual Assertion Based On ExperimentIMP:UniProtKB
Integrin-mediated signaling pathwayManual Assertion Based On ExperimentIDA:ComplexPortal
Negative chemotaxisManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of entry of bacterium into host cellManual Assertion Based On ExperimentIDA:BHF-UCL
Negative regulation of extrinsic apoptotic signaling pathwayManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of lipid storageManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of lipid transportManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of lipoprotein metabolic processManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of low-density lipoprotein receptor activityManual Assertion Based On ExperimentIMP:BHF-UCL
Negative regulation of macrophage derived foam cell differentiationManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of cell adhesionManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of cell migrationIEA:Ensembl
Positive regulation of cell population proliferationManual Assertion Based On ExperimentIDA:BHF-UCL
Positive regulation of cytosolic calcium ion concentrationIEA:Ensembl
Positive regulation of intracellular signal transductionManual Assertion Based On ExperimentIMP:BHF-UCL
Positive regulation of osteoblast proliferationIEA:Ensembl
Positive regulation of small GTPase mediated signal transductionManual Assertion Based On ExperimentIMP:BHF-UCL
Regulation of phagocytosisManual Assertion Based On ExperimentIDA:BHF-UCL
Regulation of transforming growth factor beta activationManual Assertion Based On ExperimentIDA:UniProtKB
Substrate adhesion-dependent cell spreadingManual Assertion Based On ExperimentIDA:UniProtKB
Transforming growth factor beta productionIEA:Ensembl
VasculogenesisIEA:Ensembl
Viral entry into host cellManual Assertion Based On ExperimentIMP:UniProtKB
Cellular Location
Cell membrane; Cell junction, focal adhesion
Topology
Extracellular: 31-992
Helical: 993-1016
Cytoplasmic: 1017-1048
More Infomation

Huang, S. W., Luo, J. Y., Qin, L. T., Huang, S. N., Huang, Z. G., Dang, Y. W., ... & Chen, G. (2022). Upregulation of ITGAV and the underlying mechanisms in nasopharyngeal carcinoma. Electronic Journal of Biotechnology, 60, 43-57.

Sato, N., Sakai, N., Furukawa, K., Takayashiki, T., Kuboki, S., Takano, S., ... & Ohtsuka, M. (2022). Yin Yang 1 regulates ITGAV and ITGB1, contributing to improved prognosis of colorectal cancer. Oncology Reports, 47(5), 1-20.

Huang, J. M., Pang, Z. Y., Qi, G. B., Wang, Z., & Lv, Z. T. (2020). Association of ITGAV polymorphisms and risk of rheumatoid arthritis: evidence from a meta-analysis. Expert Review of Clinical Immunology, 16(6), 631-639.

Weiler, S. M., Lutz, T., Bissinger, M., Sticht, C., Knaub, M., Gretz, N., ... & Breuhahn, K. (2020). TAZ target gene ITGAV regulates invasion and feeds back positively on YAP and TAZ in liver cancer cells. Cancer Letters, 473, 164-175.

Cheuk, I. W. Y., Siu, M. T., Ho, J. C. W., Chen, J., Shin, V. Y., & Kwong, A. (2020). ITGAV targeting as a therapeutic approach for treatment of metastatic breast cancer. American journal of cancer research, 10(1), 211.

Loeser, H., Scholz, M., Fuchs, H., Essakly, A., Damanakis, A. I., Zander, T., ... & Gebauer, F. (2020). Integrin alpha V (ITGAV) expression in esophageal adenocarcinoma is associated with shortened overall-survival. Scientific Reports, 10(1), 18411.

Kang, C. L., Qi, B., Cai, Q. Q., Fu, L. S., Yang, Y., Tang, C., ... & Wu, X. Z. (2019). LncRNA AY promotes hepatocellular carcinoma metastasis by stimulating ITGAV transcription. Theranostics, 9(15), 4421.

Lee, Y. S., Kim, K. C., Mongre, R. K., Kim, J. Y., Kim, Y. R., Choi, D. Y., ... & Hong, J. T. (2019). IL-32γ suppresses lung cancer stem cell growth via inhibition of ITGAV-mediated STAT5 pathway. Cell Death & Disease, 10(7), 506.

Lee, Y. S., Lee, C. H., Bae, J. T., Nam, K. T., Moon, D. B., Hwang, O. K., ... & Hong, J. T. (2018). Inhibition of skin carcinogenesis by suppression of NF-κB dependent ITGAV and TIMP-1 expression in IL-32γ overexpressed condition. Journal of Experimental & Clinical Cancer Research, 37, 1-16.

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For research use only. Not intended for any clinical use.

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