P cadherin Antibody [B17B8] | Primary Antibodies

Application: Reactivity: Human

Lane 1: A431, Lane 2: PC-3, Lane 3: BxPC-3

Usage Information

Dilution
WB1:1000 IHC1:250 IF1:50

Application
WB, IHC, IF

Reactivity
Human

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 Observed MW
91 kDa 120 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human breast cancer tissue; Human breast tissue; BxPC-3 cells; A431 cells; PC-3 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
P cadherin Antibody [B17B8] detects endogenous levels of total P cadherin protein.

Clone
B17B8

Synonym(s)
CDHP, CDH3, Cadherin-3, Placental cadherin, P-cadherin

Background
P-cadherin (CDH3) is a classical calcium-dependent transmembrane glycoprotein of the cadherin superfamily that mediates homophilic cell-cell adhesion, playing essential roles in placental trophoblast invasion, mammary gland development, and maintenance of epithelial integrity. Its extracellular domain is composed of five tandem EC repeats with calcium-binding linkers that rigidify the ectodomain, facilitating trans strand-swap dimerization at the EC1 domain via a conserved Trp2 interface. Anchored by a single transmembrane helix, P-cadherin’s cytoplasmic tail contains binding sites for β-catenin, α-catenin, and p120-catenin, establishing a complex that links adherens junctions to the actin cytoskeleton for junctional stability and efficient force transmission. P-cadherin localizes to basolateral adherens junctions and works in concert with E-cadherin to suppress invasive behavior by sequestering β-catenin and inhibiting canonical Wnt signaling. However, during epithelial-mesenchymal transition (EMT), selective upregulation of P-cadherin, often accompanied by E-cadherin loss, promotes collective cell migration and branching morphogenesis through RhoA/ROCK-driven actomyosin contractility and matrix metalloproteinase (MMP) activation. P-cadherin overexpression is associated with poor prognosis in breast, ovarian, and gastric cancers, enhancing tumor cell motility, invasiveness, and metastasis, in part via PI3K/Akt-mediated survival signaling that operates independently of catenin binding.

Background

P-cadherin (CDH3) is a classical calcium-dependent transmembrane glycoprotein of the cadherin superfamily that mediates homophilic cell-cell adhesion, playing essential roles in placental trophoblast invasion, mammary gland development, and maintenance of epithelial integrity. Its extracellular domain is composed of five tandem EC repeats with calcium-binding linkers that rigidify the ectodomain, facilitating trans strand-swap dimerization at the EC1 domain via a conserved Trp2 interface. Anchored by a single transmembrane helix, P-cadherin’s cytoplasmic tail contains binding sites for β-catenin, α-catenin, and p120-catenin, establishing a complex that links adherens junctions to the actin cytoskeleton for junctional stability and efficient force transmission. P-cadherin localizes to basolateral adherens junctions and works in concert with E-cadherin to suppress invasive behavior by sequestering β-catenin and inhibiting canonical Wnt signaling. However, during epithelial-mesenchymal transition (EMT), selective upregulation of P-cadherin, often accompanied by E-cadherin loss, promotes collective cell migration and branching morphogenesis through RhoA/ROCK-driven actomyosin contractility and matrix metalloproteinase (MMP) activation. P-cadherin overexpression is associated with poor prognosis in breast, ovarian, and gastric cancers, enhancing tumor cell motility, invasiveness, and metastasis, in part via PI3K/Akt-mediated survival signaling that operates independently of catenin binding.

References
https://pubmed.ncbi.nlm.nih.gov/18001487/ https://pubmed.ncbi.nlm.nih.gov/25849494/

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%