More Proteins

Extracellular Matrix (ECM) proteins are important supplements for cell culturing applications. They facilitate the attachment and cytoplasmic spreading of all types of anchorage-dependent cells. This include using to attach cells to substrates in 3-D cultures that enable an assay with more in vivo like properties.

ECM proteins facilitate cell growth, differentiation and migration enable adherence and give cultures tissue like tensile strength. 

Galectins (also known as galaptins or S-lectin) are a family of lectins which bind beta-galactoside. The family is defined by having at least one characteristic carbohydrate recognition domain (CRD) with an affinity for beta-galactosides and sharing certain sequence elements. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide, galectins can also be secreted by one or more unidentified, non-classical, secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications.

Matrix Metalloproteinases (MMPs) are a family of zinc metalloendopeptidases secreted by cells, and are responsible for much of the turnover of matrix components. They are produced as zymogens, with a signal sequence and propeptide segment that must be removed during activation. In general, This signal sequence and propeptide plus a catalytic domain (containing the highly conserved zinc binding site) characterizes the structure of the MMPs.

MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.

Recombinant viral antigens contain part of viral sequence meaning that the recombinant antigen contains a region which can be recognized by different antibodies produced by different individuals. This reduces the risk of false negatives which can occur with synthetic peptides, which contain only a small portion of the entire protein. If an individual infected with a viral antigen makes antibodies to a part of the protein not included in the synthetic peptides, a false negative results.

Recombinant viral protein usually contains a fusion protein/partner which produces superior attachment to assay surfaces such as wells. For this reason, smaller amounts of recombinant protein will produce the same results as larger amounts of unfused protein. The choice of fusion partner prevents false positives, allowing superior adhesion without incorrect results.

Applications include ELISA.  The ability to use these proteins ensure ELISAs are safe, specific and rapid. Even when a virus cannot be cultured, provided a gene sequence is available, it is possible to rapidly respond to emerging viruses and new viral strains of existing pathogens.