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Extracellular Matrix

Extracellular matrix (ECM) has both structural and regulatory roles. Biological regulation by ECM is emerging as a major research area, driven by several new directions. As a crucial modulator of cell behavior, ECM has exceptionally strong relevance and translational implications for human disease, opening novel opportunities for mechanistic understanding of disease pathogenesis as well as treatment. Formation of the extracellular matrix (ECM) requires cells to secrete ECM proteins. Assembly is achieved by following a strict hierarchical assembly pattern which begins with the deposition of fibronectin filaments on the cell surface, a process known as fibrillogenesis. Cells continue to remodel the ECM by degradation and reassembly mechanisms, the dynamic nature of the ECM being particularly apparent during development, wound healing, and certain disease states. It is estimated that there are over 300 proteins comprising the mammalian ECM or “core matrisome” and this does not include the large number of ECM-associated proteins. Cells interact with the ECM through receptors such as integrins and syndecans, resulting in the transduction of multiple signals to regulate key cellular processes such as differentiation, proliferation, survival, and motility of cells. The ECM has also been shown to bind growth factors such as VEGF, HGF and BMPs which are thought to create growth factor gradients that regulate pattern formation during development. Many of the ECM-regulated cell processes operate via reorganization of the actin and microtubule cytoskeletons.

Here you will find a list of important antibodies, reagents, kits, and other tools you need for your research in the field of ECM, and additional resources on the topic.

Mechanisms of ECM function

Mechanisms of ECM function - antibodies-online.com

The versatile functions of the ECM depend on its diverse physical, biochemical, and biomechanical properties. Anchorage to the basement membrane is essential for various biological processes, including asymmetric cell division in stem cell biology and maintenance of tissue polarity (stage 1). Depending on contexts, the ECM may serve to block or facilitate cell migration (stages 2 and 3). In addition, by binding to growth factor signaling molecules and preventing their otherwise free diffusion, the ECM acts as a sink for these signals and helps shape a concentration gradient (stage 4). Certain ECM components, including heparan sulfate proteoglycans and the hyaluronic acid receptor CD44, can selectively bind to different growth factors and function as a signal coreceptor (stage 5) or a presenter (stage 6) and help determine the direction of cell–cell communication (Lu et al., 2011). The ECM also direct signals to the cell by using its endogenous growth factor domains (not depicted) or functional fragment derivatives after being processed by proteases such as MMPs (stage 7). Finally, cells directly sense the biomechanical properties of the ECM, including its stiffness, and change a wide variety of behaviors accordingly (stage 8).

ECM Biomarkers

Serum Markers of collagen synthesis:

Serum Markers of collagen degradation:

Serum Markers of inhibition of degradation:

Type 1 Collagen Antibodies

Collagen is the most abundant fibrous protein within the interstitial ECM and constitutes up to 30% of the total protein mass of a multicellular animal.

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Cow, Human, Mammalian, Mouse, Rat
Clonality Polyclonal
Application WB, ELISA, IHC, IP
Cat. No. ABIN5596819
Quantity 100 μg
Datasheet Datasheet
Reactivity Cow, Human, Mammalian, Mouse, Rat
Clonality Polyclonal
Application WB, ELISA, IHC, IP
Cat. No. ABIN5596823
Quantity 50 μg
Datasheet Datasheet

Type 2 Collagen Antibodies

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Cow, Human, Mammalian, Mouse, Rat, Sheep
Clonality Polyclonal
Application WB, ELISA, IHC, IP
Cat. No. ABIN5596824
Quantity 100 μg
Datasheet Datasheet
Reactivity Human
Clonality Polyclonal
Application ELISA
Cat. No. ABIN135048
Quantity 0.2 mg
Datasheet Datasheet
Reactivity Human, Mouse, Rat
Clonality Polyclonal
Application WB, ELISA, IHC, IF
Cat. No. ABIN1533237
Quantity 100 μg
Datasheet Datasheet
Reactivity Cow, Human, Mammalian
Clonality Polyclonal
Application WB, ELISA, IHC, IP
Cat. No. ABIN5596826
Quantity 100 μg
Datasheet Datasheet

Type 3 Collagen Antibodies

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Human
Clonality Monoclonal
Application WB, IF, IP
Cat. No. ABIN7266459
Quantity 100 μL
Datasheet Datasheet
Reactivity Human
Clonality Polyclonal
Application ELISA
Cat. No. ABIN135050
Quantity 0.2 mg
Datasheet Datasheet
Reactivity Human, Mouse, Rat
Clonality Polyclonal
Application ELISA, IHC, IF
Cat. No. ABIN1533238
Quantity 100 μg
Datasheet Datasheet

Type 4 Collagen Antibodies

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Cow, Human, Mammalian
Clonality Polyclonal
Application ELISA, WB, IHC, IP
Cat. No. ABIN5596835
Quantity 100 μg
Datasheet Datasheet
Reactivity Human, Mouse, Pig, Rat
Clonality Polyclonal
Application ELISA, WB, IHC (p), IHC (fro), FACS, IF (p), IF (cc)
Cat. No. ABIN707396
Quantity 100 μL
Datasheet Datasheet
Reactivity Human, Mouse, Rat
Clonality Monoclonal
Application IHC (p), IF
Cat. No. ABIN7212370
Quantity 100 μL
Datasheet Datasheet
Reactivity Human
Clonality Polyclonal
Application ELISA
Cat. No. ABIN135052
Quantity 0.2 mg
Datasheet Datasheet

Type 5 Collagen Antibodies

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Mouse, Rat
Clonality Polyclonal
Application WB, IHC, IF
Cat. No. ABIN7073547
Quantity 100 μL
Datasheet Datasheet
Reactivity Human
Clonality Polyclonal
Application ELISA
Cat. No. ABIN135054
Quantity 0.2 mg
Datasheet Datasheet
Reactivity Cow, Human, Mammalian
Clonality Polyclonal
Application ELISA, WB, IHC, IP
Cat. No. ABIN5596841
Quantity 100 μg
Datasheet Datasheet
Reactivity Cow, Human, Mammalian
Clonality Polyclonal
Application ELISA, WB, IHC, IP
Cat. No. ABIN5596843
Quantity 50 μg
Datasheet Datasheet

Type 6 Collagen Antibodies

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Cow, Human
Clonality Polyclonal
Application WB, ELISA, IHC, IP, IHC (p), IF
Cat. No. ABIN214581
Quantity 50 μg
Datasheet Datasheet
Reactivity Human
Clonality Polyclonal
Application ELISA, IHC, IHC (p), IHC (fro), ICC, DB
Cat. No. ABIN462457
Quantity 50 μg
Datasheet Datasheet
Reactivity Human
Clonality Polyclonal
Application ELISA
Cat. No. ABIN135056
Quantity 0.2 mg
Datasheet Datasheet
Reactivity Cow, Human, Mammalian
Clonality Polyclonal
Application WB, ELISA, IHC, IP
Cat. No. ABIN5596844
Quantity 100 μg
Datasheet Datasheet

Other Core ECM Component Proteins

The following targets are directly related to research on ECM. Search Antibodies, Kits, Reagents and other products.

ECM Remodellers

The following targets are directly related to research on ECM. Search Antibodies, Kits, Reagents and other products. THe MMP family around MMP1 (Collagenase-1) is responsible for ECM Degradation. EMC targets are: Collagens I, II, III, VII, and X; gelatins; aggrecan; entactin; tenascin; perlecan.

References

Hubmacher, Apte: "The biology of the extracellular matrix: novel insights." in: Current opinion in rheumatology, Vol. 25, Issue 1, pp. 65-70, (2013) (PubMed).

Sottile, Hocking: "Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions." in: Molecular biology of the cell, Vol. 13, Issue 10, pp. 3546-59, (2002) (PubMed).

Daley, Peters, Larsen: "Extracellular matrix dynamics in development and regenerative medicine." in: Journal of cell science, Vol. 121, Issue Pt 3, pp. 255-64, (2008) (PubMed).

Hynes, Naba: "Overview of the matrisome--an inventory of extracellular matrix constituents and functions." in: Cold Spring Harbor perspectives in biology, Vol. 4, Issue 1, pp. a004903, (2012) (PubMed).

Taipale, Keski-Oja: "Growth factors in the extracellular matrix." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 11, Issue 1, pp. 51-9, (1997) (PubMed).

López, González, Díez: "Circulating biomarkers of collagen metabolism in cardiac diseases." in: Circulation, Vol. 121, Issue 14, pp. 1645-54, (2010) (PubMed).

Lu, Weaver, Werb: "The extracellular matrix: a dynamic niche in cancer progression." in: The Journal of cell biology, Vol. 196, Issue 4, pp. 395-406, (2012) (PubMed).

Lu, Takai, Weaver, Werb: "Extracellular matrix degradation and remodeling in development and disease." in: Cold Spring Harbor perspectives in biology, Vol. 3, Issue 12, (2012) (PubMed).

Hamill, Kligys, Hopkinson, Jones: "Laminin deposition in the extracellular matrix: a complex picture emerges." in: Journal of cell science, Vol. 122, Issue Pt 24, pp. 4409-17, (2010) (PubMed).

Singh, Carraher, Schwarzbauer: "Assembly of fibronectin extracellular matrix." in: Annual review of cell and developmental biology, Vol. 26, pp. 397-419, (2010) (PubMed).

Frantz, Stewart, Weaver: "The extracellular matrix at a glance." in: Journal of cell science, Vol. 123, Issue Pt 24, pp. 4195-200, (2011) (PubMed).

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