Integrin αV Antibody [P12L6] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

Lane 1: A549, Lane 2: MCF7, Lane 3: Jurkat, Lane 4: RL-7

Usage Information

Dilution
WB1:1000 IF1:50

Application
WB, IF

Reactivity
Human, Mouse, Rat, Monkey

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
140 kDa, 135 kDa

Positive Control	A2780 cells; A549 cells; MCF7cells; Jurkat cells; RL-7cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Integrin αV Antibody [P12L6] detects endogenous levels of total Integrin αV protein.

Clone
P12L6

Synonym(s)
Integrin alpha-V; Vitronectin receptor; Vitronectin receptor subunit alpha; Integrin alpha-V heavy chain; Integrin alpha-V light chain; CD51

Background
Integrin αV, encoded by the ITGAV gene, is a versatile integrin alpha subunit that forms heterodimers with β1, β3, β5, β6, or β8 subunits, mediating cell-extracellular matrix (ECM) adhesion by recognizing RGD motifs in ligands such as vitronectin, fibronectin, and osteopontin, and playing key roles in cell migration, signaling, and tissue remodeling. The type I transmembrane glycoprotein features a large extracellular domain with a seven-bladed β-propeller head (lacking an I-domain), thigh, and two calf domains organized in a bent, low-affinity resting conformation that transitions to an extended, high-affinity state upon inside-out activation via talin/kindlin binding to its short cytoplasmic tail. The ligand-binding pocket is formed at the αV propeller-βI domain interface and is stabilized by metal ion sites (MIDAS, ADMIDAS, SyMBS on β; Ca²⁺ sites on αV genu/propeller). αV integrins regulate proliferation, survival, and migration through outside-in signaling via FAK/Src, PI3K/Akt, and MAPK/ERK pathways, with specific heterodimers mediating angiogenesis (αVβ3/β5 in endothelium), TGF-β activation (αVβ6/β8 in fibrosis and immunity), and osteoclast-mediated bone resorption (αVβ3). Dysregulation of αV integrins drives tumor progression, metastasis, and therapeutic resistance in cancers (pancreatic, glioblastoma, breast), contributes to pulmonary fibrosis and osteoporosis, and facilitates viral entry (adenovirus, SARS-CoV-2), establishing αV as a validated therapeutic target for antibodies and RGD mimetics in oncology and antifibrotic treatments.

Background

Integrin αV, encoded by the ITGAV gene, is a versatile integrin alpha subunit that forms heterodimers with β1, β3, β5, β6, or β8 subunits, mediating cell-extracellular matrix (ECM) adhesion by recognizing RGD motifs in ligands such as vitronectin, fibronectin, and osteopontin, and playing key roles in cell migration, signaling, and tissue remodeling. The type I transmembrane glycoprotein features a large extracellular domain with a seven-bladed β-propeller head (lacking an I-domain), thigh, and two calf domains organized in a bent, low-affinity resting conformation that transitions to an extended, high-affinity state upon inside-out activation via talin/kindlin binding to its short cytoplasmic tail. The ligand-binding pocket is formed at the αV propeller-βI domain interface and is stabilized by metal ion sites (MIDAS, ADMIDAS, SyMBS on β; Ca²⁺ sites on αV genu/propeller). αV integrins regulate proliferation, survival, and migration through outside-in signaling via FAK/Src, PI3K/Akt, and MAPK/ERK pathways, with specific heterodimers mediating angiogenesis (αVβ3/β5 in endothelium), TGF-β activation (αVβ6/β8 in fibrosis and immunity), and osteoclast-mediated bone resorption (αVβ3). Dysregulation of αV integrins drives tumor progression, metastasis, and therapeutic resistance in cancers (pancreatic, glioblastoma, breast), contributes to pulmonary fibrosis and osteoporosis, and facilitates viral entry (adenovirus, SARS-CoV-2), establishing αV as a validated therapeutic target for antibodies and RGD mimetics in oncology and antifibrotic treatments.

References
https://pubmed.ncbi.nlm.nih.gov/23106217/ https://pubmed.ncbi.nlm.nih.gov/36588107/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%