Recombinant Human LAMB3 Protein, N-His

Description of Recombinant Human LAMB3 Protein, N-His

The Structure of Recombinant Human LAMB3 Protein

Recombinant Human LAMB3 Protein, also known as Laminin subunit beta-3, is a protein that is encoded by the LAMB3 gene in humans. It is a member of the laminin family of glycoproteins, which are major components of the extracellular matrix. The extracellular matrix is a complex network of proteins and carbohydrates that provides structural support and regulates cellular behavior in tissues.

The LAMB3 gene is located on chromosome 1 and is composed of 33 exons, which can be alternatively spliced to produce different isoforms of the protein. The primary structure of the protein consists of 1,656 amino acids, with a predicted molecular weight of approximately 190 kDa. It is composed of a short cytoplasmic domain, a transmembrane domain, and a large extracellular domain.

The extracellular domain of Recombinant Human LAMB3 Protein is made up of five distinct domains: the N-terminal domain, the laminin G domain, the epidermal growth factor-like domain, the laminin IV type A domain, and the laminin IV type B domain. These domains are responsible for the binding of the protein to other molecules, such as other laminin subunits and integrins, and for its biological activity.

The Activity of Recombinant Human LAMB3 Protein

Recombinant Human LAMB3 Protein plays a crucial role in cell adhesion and migration, as well as in the maintenance of tissue structure and function. It is primarily expressed in the basal layer of epithelial cells, where it is involved in the formation and maintenance of the basement membrane, a specialized extracellular matrix that separates epithelial cells from underlying tissues.

One of the key functions of Recombinant Human LAMB3 Protein is its ability to interact with integrins, a family of cell surface receptors that mediate cell adhesion and signaling. Specifically, it binds to the α3β1 integrin, which is expressed on the surface of epithelial cells, and promotes the formation of stable adhesions between cells and the extracellular matrix. This interaction is essential for the proper organization and function of epithelial tissues, as well as for wound healing and tissue repair.

In addition to its role in cell adhesion, Recombinant Human LAMB3 Protein also has important signaling functions. It can activate intracellular signaling pathways, such as the PI3K-Akt and MAPK-ERK pathways, which regulate cell survival, proliferation, and differentiation. This signaling activity is mediated by the epidermal growth factor-like domain of the protein, which binds to the epidermal growth factor receptor (EGFR) and triggers downstream signaling events.

The Application of Recombinant Human LAMB3 Protein

Recombinant Human LAMB3 Protein has a wide range of applications in both research and clinical settings. Its ability to promote cell adhesion and signaling makes it a valuable tool for studying cell behavior and tissue development. It can be used in cell culture experiments to investigate the role of laminins in cell adhesion and migration, as well as in tissue engineering applications to promote the formation of functional tissues.

In the clinic, Recombinant Human LAMB3 Protein has been studied as a potential therapeutic agent for various diseases and conditions. Mutations in the LAMB3 gene have been linked to a rare genetic disorder called Herlitz junctional epidermolysis bullosa (H-JEB), which is characterized by severe blistering of the skin and mucous membranes. Recombinant Human LAMB3 Protein has been shown to improve the adhesion and survival of H-JEB keratinocytes in vitro, and clinical trials are currently underway to evaluate its potential as a treatment for this condition.

Furthermore, Recombinant Human LAMB3 Protein has been investigated as a potential target for cancer therapy. It is known to be overexpressed in various types of cancer, and its interaction with integrins has been implicated in tumor growth and metastasis. In preclinical studies, blocking the interaction between LAMB3