Anti-Laminin α1/β1 Antibody, clone AL-4

Control
Laminin purified protein

Evaluated by Western Blot in Laminin purified protein.

Western Blot Analysis: 0.25 µg/mL of this antibody detected Laminin α1/β1 in 10 µg of Laminin purified protein.

Anti-Laminin α1/β1 Antibody, clone AL-4 is an antibody against Laminin α1/β1 for use in Western Blotting, ICC.

Research Category
Cell Structure

Research Sub Category
ECM Proteins

As originally characterized, clone AL-4 reacts with EHS mouse laminin, A chain (laminin α1). The epitope is mapped to the carboxy terminal globular domain on the A chain. Recent work by Scheele, et al. (2006) has further demonstrated that clone AL-4, under reducing conditions, recognized both the 200 kDa β1/γ1 band and the 400 kDa α1 band of mouse EHS laminin. However the affinity for the 400 kDa band was very low. AL-4 also demonstrated strong binding the Laminin β1. By ELISA the epitope for the AL-4 seemed to be located on the Laminin β1 chain, however the clone also recognizes the laminin α1 chain in immunoblots, thus AL-4 seems to show mixed cross reactivity to laminins α1 and β1, with the β1 reactivity being more prominent.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Laminins are secreted glycoproteins, and are an important structural component of the extracellular matrix. The family of laminins is comprised of multiple isoforms, each formed from the oligomerization of various alpha, beta, and gamma chains. Laminin isoforms are expressed in a tissue-specific pattern, and contain multiple domains, which may include laminin EGF-like domains; laminin G-domains; laminin IV type A domains; and a laminin N-terminal domain. Laminins are capable of self-assembly to form a structural scaffold; they also bind to cell-surface molecules such as dystroglycan and mediate attachment of these molecules to the extracellular matrix. Laminins may also participate in intracellular signaling processes by binding to various integrin receptors. They are involved in cell adhesion, migration, differentiation, neurite outgrowth, and metastasis.

~170 kDa observed

Laminin isolated from mouse EHS tumor

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Replaces: MAB1905

Format: Purified

Protein G Purified

Purified rat monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.