Laminin Antibody (Mouse mAb) [E12M18]

Application: Reactivity: Feline, Human, Porcine

Usage Information

Dilution
IHC1:25

Application
IHC, IF, ELISA

Reactivity
Feline, Human, Porcine

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

Predicted MW
337 kDa

Positive Control	Murine sarcoma basement membrane; Human tongue
Negative Control

Datasheet & SDS

Biological Description

Specificity
Laminin Antibody (Mouse mAb) [E12M18] detects endogenous levels of total Laminin protein.

Clone
E12M18

Synonym(s)
Laminin subunit alpha-1, Laminin A chain, Laminin-1 subunit alpha, Laminin-3 subunit alpha, S-laminin subunit alpha (S-LAM alpha), LAMA1, LAMA

Background
Laminins are heterotrimeric extracellular matrix glycoproteins assembled from α, β, and γ chains that associate through a coiled-coil domain into a cross-shaped molecule, with short arms mediating self-polymerization and a long arm bearing LG domains that engage cell-surface receptors. Laminin polymerization is initiated through interactions among the three short arms of separate trimers, driven primarily by the α-chain LN domain, generating a nascent two-dimensional lattice that becomes anchored to the cell surface. This cell-surface anchorage requires binding through the laminin LG domains to two principal receptor classes, integrins and dystroglycan, which act in a partially compensatory manner: either receptor alone can support laminin recruitment and basement membrane formation, but efficiency and downstream cell polarization are maximized when both receptors are engaged together, and loss of both abolishes laminin accumulation entirely and triggers apoptosis in affected cells. Once anchored, the nascent laminin scaffold recruits nidogen, type IV collagen, and heparan sulfate proteoglycans including perlecan and agrin, with nidogen forming a bridging link between laminin and the independently self-assembling type IV collagen network, and the two polymer systems together constituting the structural core of the mature basement membrane. Integrin and dystroglycan engagement additionally couples the assembled matrix to the underlying actin and keratin cytoskeletons, transmitting mechanical and signaling information bidirectionally across the cell surface and influencing cell shape, polarity, adhesion, and differentiation. Laminin isoform composition varies by tissue and developmental stage, with distinct α, β, and γ chain combinations defining basement membranes across epithelial, vascular, neural, and muscle tissue. Mutations affecting the α2 laminin chain or its dystroglycan and integrin receptor interactions disrupt sarcolemmal lattice organization in skeletal muscle and are a recognized cause of congenital muscular dystrophy.

Background

Laminins are heterotrimeric extracellular matrix glycoproteins assembled from α, β, and γ chains that associate through a coiled-coil domain into a cross-shaped molecule, with short arms mediating self-polymerization and a long arm bearing LG domains that engage cell-surface receptors. Laminin polymerization is initiated through interactions among the three short arms of separate trimers, driven primarily by the α-chain LN domain, generating a nascent two-dimensional lattice that becomes anchored to the cell surface. This cell-surface anchorage requires binding through the laminin LG domains to two principal receptor classes, integrins and dystroglycan, which act in a partially compensatory manner: either receptor alone can support laminin recruitment and basement membrane formation, but efficiency and downstream cell polarization are maximized when both receptors are engaged together, and loss of both abolishes laminin accumulation entirely and triggers apoptosis in affected cells. Once anchored, the nascent laminin scaffold recruits nidogen, type IV collagen, and heparan sulfate proteoglycans including perlecan and agrin, with nidogen forming a bridging link between laminin and the independently self-assembling type IV collagen network, and the two polymer systems together constituting the structural core of the mature basement membrane. Integrin and dystroglycan engagement additionally couples the assembled matrix to the underlying actin and keratin cytoskeletons, transmitting mechanical and signaling information bidirectionally across the cell surface and influencing cell shape, polarity, adhesion, and differentiation. Laminin isoform composition varies by tissue and developmental stage, with distinct α, β, and γ chain combinations defining basement membranes across epithelial, vascular, neural, and muscle tissue. Mutations affecting the α2 laminin chain or its dystroglycan and integrin receptor interactions disrupt sarcolemmal lattice organization in skeletal muscle and are a recognized cause of congenital muscular dystrophy.

References
https://pubmed.ncbi.nlm.nih.gov/23076216/ https://pubmed.ncbi.nlm.nih.gov/19355968/

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%