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Laminin α5/LAMA5 Antibody [P21J13]

Cat.No.: F3673

Application: Reactivity: Human

Usage Information

Dilution

Application
IF

Reactivity
Human

Source
Mouse 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

Datasheet & SDS

Biological Description

Specificity
Laminin α5/LAMA5 Antibody [P21J13] detects endogenous levels of total Laminin α5/LAMA5 protein.

Clone
P21J13

Synonym(s)
KIAA0533; KIAA1907; LAMA5; Laminin subunit alpha-5; Laminin-10 subunit alpha; Laminin-11 subunit alpha; Laminin-15 subunit alpha

Background
Laminin α5 (LAMA5), the largest α chain within laminin-511/521/523 heterotrimers that constitute epithelial and endothelial basement membranes, is characterized by an N-terminal LN domain that mediates end-on polymerization through β and γ chain interactions, and a C-terminal region containing five globular LG1–5 subdomains in the long cross-shaped arm. The LG4–5 tandem exposes integrin α3β1/α6β1 and α-dystroglycan binding sites via RGD-like motifs and specific carbohydrate moieties, as well as interfaces for syndecan and Lu-BCAM, while the central coiled-coil (LCC) region stabilizes the α5β1γ1 assembly. LAMA5 self-assembles into networks through LN domain-mediated, zipper-like intertrimer engagement under physiological pH and Ca²⁺, forming a scaffold that orchestrates epithelial-mesenchymal interactions: the LG1–3 tandem anchors integrin signaling, activating FAK/Src/PI3K/Akt pathways to promote cell proliferation and migration, while LG4–5 domains suppress apoptosis via dystroglycan–dystrophin linkage. The short-arm G domains modulate collagen IV and perlecan integration, contributing to filtration barrier formation, and the flexible long arms absorb tensile stress (~10–50 MPa). During organogenesis, LAMA5 patterns kidney glomeruli and the placental labyrinth by constraining epithelial branching, with VEGF-A coregulation facilitating endothelial sprouting. Genetic ablation in mice (Lama5 null) results in embryonic lethality at E10.5 due to defective chorioallantoic fusion and neural tube closure linked to impaired polarity signaling, whereas adult glomerular knockout causes proteinuria and fibrosis.

Background

Laminin α5 (LAMA5), the largest α chain within laminin-511/521/523 heterotrimers that constitute epithelial and endothelial basement membranes, is characterized by an N-terminal LN domain that mediates end-on polymerization through β and γ chain interactions, and a C-terminal region containing five globular LG1–5 subdomains in the long cross-shaped arm. The LG4–5 tandem exposes integrin α3β1/α6β1 and α-dystroglycan binding sites via RGD-like motifs and specific carbohydrate moieties, as well as interfaces for syndecan and Lu-BCAM, while the central coiled-coil (LCC) region stabilizes the α5β1γ1 assembly. LAMA5 self-assembles into networks through LN domain-mediated, zipper-like intertrimer engagement under physiological pH and Ca²⁺, forming a scaffold that orchestrates epithelial-mesenchymal interactions: the LG1–3 tandem anchors integrin signaling, activating FAK/Src/PI3K/Akt pathways to promote cell proliferation and migration, while LG4–5 domains suppress apoptosis via dystroglycan–dystrophin linkage. The short-arm G domains modulate collagen IV and perlecan integration, contributing to filtration barrier formation, and the flexible long arms absorb tensile stress (~10–50 MPa). During organogenesis, LAMA5 patterns kidney glomeruli and the placental labyrinth by constraining epithelial branching, with VEGF-A coregulation facilitating endothelial sprouting. Genetic ablation in mice (Lama5 null) results in embryonic lethality at E10.5 due to defective chorioallantoic fusion and neural tube closure linked to impaired polarity signaling, whereas adult glomerular knockout causes proteinuria and fibrosis.

References
https://pubmed.ncbi.nlm.nih.gov/26097310/ https://pubmed.ncbi.nlm.nih.gov/35625601/

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%