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Cytoskeletal and ECM Antibodies

The extracellular matrix (ECM) is the non-cellular component that provides structural scaffolding to surrounding cells. The ECM also provides critical biochemical support that is required for intracellular communication, differentiation, and homeostasis.

The cytoskeleton is the microscopic network of protein filaments and tubules in the cytoplasm of cells that helps them maintain their shape and internal organization. It provides mechanical support that enables cells to carry out essential functions like division and movement. For over three decades SouthernBiotech has supplied ECM antibodies, as well as cytoskeletal antibodies, to help advance your matrix biology research forward. Our antibodies are produced and validated in-house, for your immunohistochemistry, western blot, and ELISA assays.

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Frequently Asked Questions

The ECM is a dynamic, three-dimensional (3D) meshwork of proteins, carbohydrates, and other biomolecules that is found in virtually all multicellular organisms. It serves as a scaffold for surrounding cells, providing tissues and organs with structural integrity and the mechanical properties essential for their function. In addition, the ECM can influence cellular behaviors such as proliferation, differentiation, and migration, giving it a central role in processes including stem cell niche formation, angiogenesis, and wound healing. Abnormal ECM composition and structure has been implicated in the pathogenesis of diseases including osteoarthritis, fibrosis, and cancer. Also, mutations in genes coding for specific ECM proteins have been linked to conditions such as osteogenesis imperfecta, Marfan syndrome, and junctional epidermolysis bullosa.

The ECM is known to contain over 300 different proteins, including the following:

  • Collagens are the most abundant ECM components. They comprise a superfamily of 28 proteins, each consisting of three polypeptide α chains, which is divided into seven subtypes based on homology and function. Well-known collagen subtypes include the fibril-forming collagens, such as collagen type I, which is found in most connective tissues, and the network-forming collagens, such as collagen type IV, the major constituent of basement membranes.
  • Fibronectin contains binding sites for a broad range of molecules and is critical for cellular attachment and migration. It is synthesized by almost all mammalian cells as a monomer with a molecular weight of ~250 kDa, which dimerizes intracellularly via disulfide bond formation before being secreted. Following its secretion, fibronectin associates with other ECM components to form an interconnected network of fibers.
  • Laminins are heterotrimeric proteins consisting of one α, one β, and one γ chain. To date, 16 different laminin combinations have been identified in vivo, with molecular weights ranging from 400–800 kDa. Laminins are major components of basement membranes, where they are closely interwoven with the type IV collagen network, and serve to bind to various cellular receptors.
  • Elastin is found in tissues that undergo repeated stretching, such as the lung, vascular vessels, skin, elastic cartilage, and ligaments. In mammals, it is secreted as a ~60 kDa tropoelastin monomer by elastogenic cells including smooth muscle cells, fibroblasts, and endothelial cells, before associating with fibrillin microfibrils to form elastic fibers.
  • Proteoglycans consist of a core protein onto which multiple glycosaminoglycan (GAG) side chains are attached. They are grouped into families based on homology and localization, and interact with biomolecules including other ECM components, growth factors, cytokines, cell surface receptors, and enzymes to exert a wide range of biological functions.

The ECM is fundamental to countless biological processes, spanning everything from embryonic development through to tissue remodeling following injury. By studying the ECM, researchers can determine which components are required for normal physiological function and learn how their dysregulation contributes to the pathogenesis of disease. Such insights are key to developing novel treatments for conditions including cancer, autoimmune disease, and neurodegenerative disorders, as well as can drive advances in regenerative medicine and tissue engineering.

The ECM must undergo continuous remodeling to control tissue homeostasis. This is achieved through the controlled degradation, reassembly and modification of its various constituents. Because collagens are the main structural components of the ECM, they have a pivotal role in the remodeling process. The metzincin superfamily of enzymes, which includes the matrix metalloproteinases (MMPs), the adamalysins, and the astacins, represents a major participant in both physiological and pathological collagen degradation. Many metzincin enzymes have been investigated as potential therapeutic targets for preventing tumorigenesis and metastasis.

Our polyclonal goat anti-collagen antibodies are widely used for ECM-based research. Targeting collagens I – VI, they have broad species reactivity, are validated for use in multiple applications, and are available as various conjugates.

The cytoskeleton is an intracellular network of protein fibers that performs many different functions. These include maintaining or changing the shape of a cell, enabling the transport of intracellular vesicles, securing organelles in position, and enabling cell movement in response to various stimuli. The three main types of protein fibers that make up the cytoskeleton are as follows:

  • Microfilaments are composed of globular actin subunits that polymerize and intertwine as filament pairs, producing structures with a diameter of approximately 7 nm. Each actin filament has two distinct ends: a barbed end, to which actin monomers are added, and a pointed end, from which actin monomers are removed, giving it polarity. Microfilaments serve as tracks for myosins, making them important for processes that involve movement, such as muscle contraction, cell motility, cytokinesis, and vesicle/organelle transport. They also have an essential role in preserving cell structure.
  • Intermediate filaments are formed from a diverse family of proteins, which includes the keratins, nuclear lamins, and vimentin, as well as desmin, glial fibrillary acidic protein (GFAP), and nestin. Each intermediate filament consists of several intertwined protein strands, giving it a diameter of around 10 nm, and has a predominantly structural function.
  • Microtubules are assembled from heterodimers of α- and β-tubulin, which polymerize to form a hollow tube with a diameter of approximately 25 nm. Like microfilaments, microtubules have polarity, with the α- and β-tubulin subunits respectively being exposed at the minus and plus ends. In mesenchymal cells, microtubules are typically nucleated from γ-tubulin at the centrosome, which anchors the minus ends while the plus ends extend towards the edges of the cell. In epithelial cells, microtubules are instead oriented along the apical-basal axis, with the plus ends facing the basal side. Microtubules provide tracks for kinesins and dyneins to allow for vesicle transport. They also help cells to resist compression, are key structural components of flagella and cilia, and serve to separate replicated chromosomes.

With roles that include giving cells shape, supporting cell division, enabling molecular transport, and many others, cytoskeletal proteins are central to almost every cellular process. Cytoskeletal protein abnormalities have been linked to conditions including cardiovascular disease, neurodegeneration, and cancer, as well as pulmonary fibrosis, liver cirrhosis, and autoimmune skin blistering, highlighting the critical importance of understanding how these biomolecules work and how their behaviors might be manipulated for therapeutic purposes.

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