Radixin Antibody [C5B23] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

Lane 1: Hela, Lane 2: NIH/3T3, Lane 3: COS, Lane 4: C6

Usage Information

Dilution
WB1:1000

Application
WB

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
80 kDa

Datasheet & SDS

Biological Description

Specificity
Radixin Antibody [C5B23] detects endogenous levels of total Radixin protein.

Clone
C5B23

Synonym(s)
Radixin; RDX

Background
Radixin, a key member of the ERM (ezrin-radixin-moesin) protein family that links plasma membranes to the actin cytoskeleton, regulates cortical architecture, cell polarity, and motility through conformational activation at its C-terminal threonine residue. In its dormant state, intramolecular masking between the N-terminal FERM domain and C-terminal actin-binding tail maintains cytosolic sequestration, but phosphorylation at Thr564 by Rho-associated kinase or PKC disrupts this clamp, unmasking membrane-binding sites for CD44/ICAMs and F-actin tails to stabilize microvilli, lamellipodia, and tight junctions. Activated radixin scaffolds MRP-2 trafficking to apical canaliculi in polarized hepatocytes via ezrin/radixin/moesin phosphorylation cycling that responds to phosphatase inhibition or metabolic stress, while Gα13/RhoA signaling engages radixin's C-terminus to stimulate Rac1 and CaMKII, driving serum response element transcription and cytoskeletal remodeling. In colon epithelia, radixin overexpression hyperactivates Rac1-ERK cascades that boost MMP-7 secretion for basement membrane invasion, whereas Thr564 mutants reveal non-phosphorylatable forms that preserve polarity but abolish MRP-2 function, positioning radixin as the dominant ERM paralog for dissecting vectorial transport. Radixin maintains bile canalicular integrity and hepatocyte plate architecture, with conditional ablation disrupting Mrp-2 localization and organic anion efflux critical for xenobiotic clearance. Upregulation correlates with colorectal cancer progression through enhanced invadopodia while lung adenocarcinoma shows paradoxical downregulation suggesting context-dependent suppression; Akt2-mediated Thr564 phosphorylation links PI3K signaling to polarity loss.

Background

Radixin, a key member of the ERM (ezrin-radixin-moesin) protein family that links plasma membranes to the actin cytoskeleton, regulates cortical architecture, cell polarity, and motility through conformational activation at its C-terminal threonine residue. In its dormant state, intramolecular masking between the N-terminal FERM domain and C-terminal actin-binding tail maintains cytosolic sequestration, but phosphorylation at Thr564 by Rho-associated kinase or PKC disrupts this clamp, unmasking membrane-binding sites for CD44/ICAMs and F-actin tails to stabilize microvilli, lamellipodia, and tight junctions. Activated radixin scaffolds MRP-2 trafficking to apical canaliculi in polarized hepatocytes via ezrin/radixin/moesin phosphorylation cycling that responds to phosphatase inhibition or metabolic stress, while Gα13/RhoA signaling engages radixin's C-terminus to stimulate Rac1 and CaMKII, driving serum response element transcription and cytoskeletal remodeling. In colon epithelia, radixin overexpression hyperactivates Rac1-ERK cascades that boost MMP-7 secretion for basement membrane invasion, whereas Thr564 mutants reveal non-phosphorylatable forms that preserve polarity but abolish MRP-2 function, positioning radixin as the dominant ERM paralog for dissecting vectorial transport. Radixin maintains bile canalicular integrity and hepatocyte plate architecture, with conditional ablation disrupting Mrp-2 localization and organic anion efflux critical for xenobiotic clearance. Upregulation correlates with colorectal cancer progression through enhanced invadopodia while lung adenocarcinoma shows paradoxical downregulation suggesting context-dependent suppression; Akt2-mediated Thr564 phosphorylation links PI3K signaling to polarity loss.

References
https://pubmed.ncbi.nlm.nih.gov/25136657/ https://pubmed.ncbi.nlm.nih.gov/21160029/

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%