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Laminin biology

THE LAMININ MOLECULELAMININS ARE KEY PROTEINS IN THE BASEMENT MEMBRANE

Laminins are a large family (at least 16 different isoforms ex­pressed in mammals) of conserved, multidomain glycopro­teins comprising the extracellular matrix. They are a major component of the basal lamina, a protein network that is the foundation for most cells and tissues. Laminins have an important biologically active role and are vital for the maintenance and survival of tissues and, importantly, most lamin­ins exhibit high cell-type specificity. With­out the right combination of laminin isoforms, cells and tissues become dysfunctional.

Each laminin isoform consists of three inter-coiled chains -an α, β, and γ chain – that exist in five, four, and three genetically distinct variants, respectively. The laminin isoforms are named according to their chain composition. For example, a combination of an α5 chain, a β2 chain, and a γ1 chain, forms laminin 5-2-1 (LN521). The trimeric proteins form a cross-like structure that can bind to other extracellular matrix molecules and various cell membrane receptors.

 

CELL-SPECIFIC CULTURE SUBSTRATES FOR IMPROVED CELL FUNCTIONALITY

In the body, cells reside in highly specialized, chemo-and mech­anosensitive microenvironments, or “niches”, which serve to protect and maintain the cells and to respond to the needs of the surrounding tissue. α5 chain laminins (511 and 521) are the key cell adhesion proteins of the natural Laminin expression in the blastocyststem cell niche, expressed and secreted by the embryonic stem cells of the embryo’s inner cell mass. The Biolaminin 521 cell culture substrate thus recapit­ulates the most biologically relevant milieu for hESCs and iPSCs cultured in vitro and is a critical autocrine and paracrine factor for regulating survival and self-renewal. Tissue-specific laminin iso­forms can also be used for robust differentiation of specialized cell types, such as hepatocytes, skeletal muscle cells, and various neural cells.

 

ONLY THE INTACT, FULL-LENGTH LAMININ MOLECULES CAN REPLICATE THE BIOLOGICAL RELEVANT CONDITIONS

There are many binding motifs on the full-length laminin molecule that can interact with cell membrane receptors. It has been suggested that the molecular mechanism underlying the laminin-mediated signaling involves the C-terminal region of laminins but integrins and other cellular receptors also interact with some of the N-terminal globular domains. Laminins are also capable of co-signaling with growth factors and efficiently buffer endogenously produced growth factors, thereby adding to the mechanistic complexity. Via binding to specific cellular receptors, laminins regulate cellular responses, such as cell anchorage, survival, proliferation, migration, organization and specialization, leading to improved cell functionality. 

 

 

 

 

 

THE EXTRACELLULAR MICROINVIRONMENT

Stem cells are influenced by the coordinated interaction of soluble factors, extracellular matrix (ECM) proteins, and signals from neighboring cells. This multifaceted cell-ECM communication takes place through both integrin and non-integrin membrane-bound receptors and induces complex intracellular signaling pathways with subsequent effects on survival, self-renewal, migration, morphogenesis, and differentiation.

 

 

BioLamina offers an expansive portfolio of defined, animal origin-free, recombinant laminin cell culture substrates, Biolaminins, for a variety of applications, including a reliable expansion of human pluripotent stem cells (hESC and iPSC) and differentiation and maintenance of different specialized cell types, such as hepatocytes, skeletal muscle cells, and different neural cells. The Biolaminin substrates allow you to imitate the natural cell-matrix interactions in vitro and the authentic cell culture environment gives more consistent and reliable cellular responses and improves cell functionality. BioLamina's Biolaminin substrates are the only original full length, recombinant laminins on the market. A fractionated or truncated laminin molecule or laminins isolated from tissue lack many of the laminin domains which are needed by the cells for the proper extracellular network to form and to for stimulation of correct cellular signal transductions. Hence, only the intact, full-length laminin can create a more authentic cell culture environment.

 

READ MORE ABOUT THE DIFFERENT BIOLAMININ CELL CULTURE APPLICATIONS

 

 


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