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N-Cadherin Antibody [G6B2]

Cat.No.: F0147

Application: Reactivity: Human, Mouse

Usage Information

Dilution
WB1:1000 IP1:150 IHC1:50 - 1:200 IF1:400 - 1:1600

Application
WB, IP, IHC, IF

Reactivity
Human, Mouse

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

Datasheet & SDS

Biological Description

Specificity
N-Cadherin Antibody [G6B2] detects endogenous levels of total N-Cadherin protein.

Clone
G6B2

Synonym(s)
CDH2; Cadherin-2; CDw325; Neural cadherin (N-cadherin); CD325; CDHN; NCAD

Background
N-Cadherin (CDH2) is a calcium-dependent transmembrane glycoprotein essential for homotypic cell-cell adhesion in mesenchymal, neuronal, and endothelial cells, orchestrating tissue morphogenesis, neuronal migration, synaptic plasticity, and vascular integrity through coordinated extracellular and intracellular interactions. Its extracellular region features five tandem EC domains (EC1–EC5), each about 110 residues, containing conserved Ca²⁺-binding motifs (DXNDNEPXXF) that rigidify interdomain linkers and facilitate both cis and trans adhesive interfaces; the EC1 domain utilizes Trp2 to insert into the hydrophobic pocket of an opposing EC1 in a trans His-Ala-Val motif-dependent manner, while EC5 supports cis dimerization. A single-pass transmembrane helix anchors N-cadherin in the membrane, and its conserved cytoplasmic tail (~150 residues) includes p120-catenin and β-catenin binding sites in the juxtamembrane domain (JMD), linking to α-catenin and F-actin for cytoskeletal attachment. N-cadherin can form ternary complexes with FGFR, activating Src/FAK signaling and upregulating MMP-9/2 expression to promote invadopodia formation, ECM remodeling, and collective cell migration. In adherens junctions, juxtamembrane phosphorylation by Src or EGFR recruits Hakai for endocytosis, while PKA-mediated phosphorylation of Ser/Thr residues stabilizes β-catenin/Akt signaling and suppresses apoptosis, supporting EMT via Snail1 and RhoA. During neuronal development, N-cadherin interacts with δ-catenin to regulate dendritic spine morphogenesis and NMDA receptor clustering through PSD-95, and in endothelial cells, crosstalk with VE-cadherin modulates VEGF-induced permeability via Rac1 and actin cytoskeletal barriers. In cancer, the cadherin switch, characterized by N-cadherin upregulation with E-cadherin loss, drives metastasis in breast, prostate, and melanoma by enhancing motility and survival signaling, while mutations affecting EC1 cis-binding or cytoplasmic p120-catenin docking are associated with neurodevelopmental disorders and cardiomyopathy.

Background

N-Cadherin (CDH2) is a calcium-dependent transmembrane glycoprotein essential for homotypic cell-cell adhesion in mesenchymal, neuronal, and endothelial cells, orchestrating tissue morphogenesis, neuronal migration, synaptic plasticity, and vascular integrity through coordinated extracellular and intracellular interactions. Its extracellular region features five tandem EC domains (EC1–EC5), each about 110 residues, containing conserved Ca²⁺-binding motifs (DXNDNEPXXF) that rigidify interdomain linkers and facilitate both cis and trans adhesive interfaces; the EC1 domain utilizes Trp2 to insert into the hydrophobic pocket of an opposing EC1 in a trans His-Ala-Val motif-dependent manner, while EC5 supports cis dimerization. A single-pass transmembrane helix anchors N-cadherin in the membrane, and its conserved cytoplasmic tail (~150 residues) includes p120-catenin and β-catenin binding sites in the juxtamembrane domain (JMD), linking to α-catenin and F-actin for cytoskeletal attachment. N-cadherin can form ternary complexes with FGFR, activating Src/FAK signaling and upregulating MMP-9/2 expression to promote invadopodia formation, ECM remodeling, and collective cell migration. In adherens junctions, juxtamembrane phosphorylation by Src or EGFR recruits Hakai for endocytosis, while PKA-mediated phosphorylation of Ser/Thr residues stabilizes β-catenin/Akt signaling and suppresses apoptosis, supporting EMT via Snail1 and RhoA. During neuronal development, N-cadherin interacts with δ-catenin to regulate dendritic spine morphogenesis and NMDA receptor clustering through PSD-95, and in endothelial cells, crosstalk with VE-cadherin modulates VEGF-induced permeability via Rac1 and actin cytoskeletal barriers. In cancer, the cadherin switch, characterized by N-cadherin upregulation with E-cadherin loss, drives metastasis in breast, prostate, and melanoma by enhancing motility and survival signaling, while mutations affecting EC1 cis-binding or cytoplasmic p120-catenin docking are associated with neurodevelopmental disorders and cardiomyopathy.

References
https://pubmed.ncbi.nlm.nih.gov/20066110/ https://pubmed.ncbi.nlm.nih.gov/22171007/

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%