Angiomotin Antibody [M16G16] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Lane 1: 293T, Lane 2: OVCAR3, Lane 3: C2C12

Usage Information

Dilution
WB1:1000 IP1:100 IHC1:250-1:1000 IF1:200-1:400 FCM1:400-1:1600

Application
WB, IP, IHC, IF, FCM

Reactivity
Human, Mouse, Rat

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, 80 kDa

Datasheet & SDS

Biological Description

Specificity
Angiomotin Antibody [M16G16] detects endogenous levels of total Angiomotin protein.

Clone
M16G16

Synonym(s)
Angiomotin; AMOT; KIAA1071

Background
Angiomotin (AMOT) is a junction‑associated scaffold protein belonging to the Motin family, which includes AMOTL1 and AMOTL2, and is widely expressed in epithelial and endothelial tissues where it coordinates cell–cell adhesion, polarity, and migration. It exists primarily as two isoforms generated by alternative splicing, a full‑length p130 form and a shorter, amino‑terminally truncated p80 variant, both of which share conserved N‑terminal coiled‑coil and C‑terminal PDZ‑domain‑like motifs that mediate interactions with membrane‑associated and cytoskeletal proteins. AMOT directly binds the transcriptional co‑activators YAP and TAZ, sequestering them in the cytoplasm and limiting their nuclear entry and TEAD‑dependent transcription. This interaction can occur independently of canonical Hippo‑pathway phosphorylation. In endothelial cells, AMOT acts downstream of GPCR signaling and is a direct substrate of Lats1/2 kinases. Phosphorylation of conserved motifs in AMOT‑p130 disrupts its association with F‑actin and stress fibers, reduces focal adhesions, impairs migration, and attenuates angiogenesis. AMOT also interfaces with small‑GTPase networks by scaffolding components around junctional complexes, including interactions with Merlin and regulators of Rac1, and modulates actin organization and cytoskeletal dynamics that affect cell shape, collective migration, and barrier integrity. AMOT‑p130 differentially regulates Rho‑ and actin‑dependent cytoskeletal remodeling in epithelial and cancer contexts. In some breast cancer models, AMOT overexpression correlates with increased proliferation, invasion, and metastasis‑linked motility, while in other settings it correlates with reduced YAP‑driven growth. Angiomotin isoforms show differential expression, are subject to post‑translational modification by Lats1/2, and compete with other Motin‑family members.

Background

Angiomotin (AMOT) is a junction‑associated scaffold protein belonging to the Motin family, which includes AMOTL1 and AMOTL2, and is widely expressed in epithelial and endothelial tissues where it coordinates cell–cell adhesion, polarity, and migration. It exists primarily as two isoforms generated by alternative splicing, a full‑length p130 form and a shorter, amino‑terminally truncated p80 variant, both of which share conserved N‑terminal coiled‑coil and C‑terminal PDZ‑domain‑like motifs that mediate interactions with membrane‑associated and cytoskeletal proteins. AMOT directly binds the transcriptional co‑activators YAP and TAZ, sequestering them in the cytoplasm and limiting their nuclear entry and TEAD‑dependent transcription. This interaction can occur independently of canonical Hippo‑pathway phosphorylation. In endothelial cells, AMOT acts downstream of GPCR signaling and is a direct substrate of Lats1/2 kinases. Phosphorylation of conserved motifs in AMOT‑p130 disrupts its association with F‑actin and stress fibers, reduces focal adhesions, impairs migration, and attenuates angiogenesis. AMOT also interfaces with small‑GTPase networks by scaffolding components around junctional complexes, including interactions with Merlin and regulators of Rac1, and modulates actin organization and cytoskeletal dynamics that affect cell shape, collective migration, and barrier integrity. AMOT‑p130 differentially regulates Rho‑ and actin‑dependent cytoskeletal remodeling in epithelial and cancer contexts. In some breast cancer models, AMOT overexpression correlates with increased proliferation, invasion, and metastasis‑linked motility, while in other settings it correlates with reduced YAP‑driven growth. Angiomotin isoforms show differential expression, are subject to post‑translational modification by Lats1/2, and compete with other Motin‑family members.

References
https://pubmed.ncbi.nlm.nih.gov/28464980/ https://pubmed.ncbi.nlm.nih.gov/21205866/

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%