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AB117611

Anti-Integrin alpha V antibody

3

(1 Review)

|

(6 Publications)

Rabbit Polyclonal Integrin alpha V antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 6 publications. Immunogen corresponding to Synthetic Peptide within Human ITGAV conjugated to Keyhole Limpet Haemocyanin.

View Alternative Names

CD51, MSK8, VNRA, VTNR, ITGAV, Integrin alpha-V, Vitronectin receptor, Vitronectin receptor subunit alpha

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Integrin alpha V antibody (AB117611)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Integrin alpha V antibody (AB117611)

ab117611, at 5 µg/ml, staining Integrin alpha V in Formalin-fixed, Paraffin-embedded Human Placenta tissue by Immunohistochemistry.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Integrin alpha V antibody (AB117611)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Integrin alpha V antibody (AB117611)

ab117611, at 5 µg/ml, staining Integrin alpha V in Formalin-fixed, Paraffin-embedded Human Thyroid tissue by Immunohistochemistry.

Western blot - Anti-Integrin alpha V antibody (AB117611)
  • WB

Unknown

Western blot - Anti-Integrin alpha V antibody (AB117611)

All lanes:

Western blot - Anti-Integrin alpha V antibody (ab117611) at 1/500 dilution

Lane 1:

A549 cell extracts, treated with etoposide 25uM 1hr

Lane 2:

A549 cell extracts, treated with etoposide 25uM 1h with synthetic peptide

Predicted band size: 116 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Synthetic Peptide within Human ITGAV conjugated to Keyhole Limpet Haemocyanin. The exact immunogen used to generate this antibody is proprietary information.

P06756

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.88% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Integrin alpha V also known as integrin av CD51 and CD51/CD61 is a transmembrane protein with an approximate mass of 125 kDa. It functions mechanically by mediating cell adhesion and signaling through its interaction with the extracellular matrix and other cells. Integrin alpha V is widely expressed in a variety of tissues including endothelial and epithelial cells as well as some tumor cells. This protein forms heterodimers typically with beta subunits like CD61 which is also referred to as beta 3 integrin to execute its biological functions.
Biological function summary

Integrin alpha V plays a pivotal role in cellular processes such as migration proliferation and survival. It participates in the formation of multi-molecular complexes within cellular structures. The integrin av integrins particularly in conjunction with its CD51/CD61 form contribute to the regulation of angiogenesis immune response and wound healing. These functions arise from the integrin’s ability to act as a receptor for numerous ligands including fibrinogen fibronectin and vitronectin.

Pathways

Integrin alpha V is a critical component of the integrin signaling and focal adhesion pathways. These pathways involve a network of interactions that include proteins like focal adhesion kinase (FAK) and Src family kinases. Integrin alpha V’s interaction within these pathways assists in transmitting mechanical signals from the extracellular environment to the intracellular signaling cascades affecting cytoskeleton dynamics and gene expression. The pathway interactions with integrin av also coordinate complex signaling with other receptors and matrix proteins like laminins enhancing cellular communication and response to environmental changes.

Integrin alpha V’s dysregulation associates with conditions such as cancer and fibrosis. Overexpression or aberrant functioning of integrin av contributes to tumor progression and metastasis by promoting angiogenesis and cell migration. In fibrotic diseases the protein's interactions with the extracellular matrix components are altered leading to excessive tissue scarring and dysfunction. Furthermore integrin alpha V interplays with proteins such as matrix metalloproteinases (MMPs) in the tumor microenvironment facilitating tissue remodeling and cancer cell invasion.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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.
See full target information ITGAV

Publications (6)

Recent publications for all applications. Explore the full list and refine your search

The Journal of cell biology 224: PubMed40304687

2025

Extracellular vesicles adhere to cells primarily by interactions of integrins and GM1 with laminin.

Applications

Unspecified application

Species

Unspecified reactive species

Tatsuki Isogai,Koichiro M Hirosawa,Miki Kanno,Ayano Sho,Rinshi S Kasai,Naoko Komura,Hiromune Ando,Keiko Furukawa,Yuhsuke Ohmi,Koichi Furukawa,Yasunari Yokota,Kenichi G N Suzuki

Matrix biology : journal of the International Society for Matrix Biology 103-104:1-21 PubMed34537369

2021

EphA2 signaling within integrin adhesions regulates fibrillar adhesion elongation and fibronectin deposition.

Applications

Unspecified application

Species

Unspecified reactive species

Alexandra C Finney,Matthew L Scott,Kaylea A Reeves,Dongdong Wang,Mabruka Alfaidi,Jake C Schwartz,Connor M Chitmon,Christina H Acosta,James M Murphy,J Steven Alexander,Christopher B Pattillo,Ssang-Taek Lim,A Wayne Orr

Nature communications 11:1211 PubMed32139701

2020

Primary tumors release ITGBL1-rich extracellular vesicles to promote distal metastatic tumor growth through fibroblast-niche formation.

Applications

Unspecified application

Species

Unspecified reactive species

Qing Ji,Lihong Zhou,Hua Sui,Liu Yang,Xinnan Wu,Qing Song,Ru Jia,Ruixiao Li,Jian Sun,Ziyuan Wang,Ningning Liu,Yuanyuan Feng,Xiaoting Sun,Gang Cai,Yu Feng,Jianfeng Cai,Yihai Cao,Guoxiang Cai,Yan Wang,Qi Li

Journal of extracellular vesicles 7:1490144 PubMed30034643

2018

Molecular subtypes and differentiation programmes of glioma stem cells as determinants of extracellular vesicle profiles and endothelial cell-stimulating activities.

Applications

Unspecified application

Species

Unspecified reactive species

C Spinelli,L Montermini,B Meehan,A R Brisson,S Tan,D Choi,I Nakano,J Rak

Graefe's archive for clinical and experimental oph 256:1589-1597 PubMed29931427

2018

Premacular membranes in tissue culture.

Applications

Unspecified application

Species

Unspecified reactive species

Denise Vogt,Franziska Vielmuth,Christian Wertheimer,Felix Hagenau,Stefanie R Guenther,Armin Wolf,Volker Spindler,Siegfried G Priglinger,Ricarda G Schumann

Nature 527:329-35 PubMed26524530

2015

Tumour exosome integrins determine organotropic metastasis.

Applications

WB

Species

Human

Ayuko Hoshino,Bruno Costa-Silva,Tang-Long Shen,Goncalo Rodrigues,Ayako Hashimoto,Milica Tesic Mark,Henrik Molina,Shinji Kohsaka,Angela Di Giannatale,Sophia Ceder,Swarnima Singh,Caitlin Williams,Nadine Soplop,Kunihiro Uryu,Lindsay Pharmer,Tari King,Linda Bojmar,Alexander E Davies,Yonathan Ararso,Tuo Zhang,Haiying Zhang,Jonathan Hernandez,Joshua M Weiss,Vanessa D Dumont-Cole,Kimberly Kramer,Leonard H Wexler,Aru Narendran,Gary K Schwartz,John H Healey,Per Sandstrom,Knut Jørgen Labori,Elin H Kure,Paul M Grandgenett,Michael A Hollingsworth,Maria de Sousa,Sukhwinder Kaur,Maneesh Jain,Kavita Mallya,Surinder K Batra,William R Jarnagin,Mary S Brady,Oystein Fodstad,Volkmar Muller,Klaus Pantel,Andy J Minn,Mina J Bissell,Benjamin A Garcia,Yibin Kang,Vinagolu K Rajasekhar,Cyrus M Ghajar,Irina Matei,Hector Peinado,Jacqueline Bromberg,David Lyden
View all publications

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