电话:
+1 877 302 8632
传真:
+1 888 205 9894 (Toll-free)
电子邮件:
orders@antibodies-online.cn

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:

Important ECM Proteins:

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

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

Fibronectin Antibodies

Matrix assembly is usually initiated by ECM glycoproteins binding to cell surface receptors, such as fibronectin (FN) dimers binding to α5β1 integrin.

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Cow, Human, Monkey, Mouse, Rat
Clonality Polyclonal
Application ELISA, IHC, IP, WB
Cat. No. ABIN5596762
Quantity 100 μg
Datasheet Datasheet
Reactivity Human
Clonality Monoclonal
Application EIA, FACS, IF, IHC (p), WB
Cat. No. ABIN1107234
Quantity 0.1 mL
Datasheet Datasheet
Reactivity Cow, Human, Mouse, Rat
Clonality Polyclonal
Application IF (cc), IF (p)
Cat. No. ABIN671653
Quantity 100 μL
Datasheet Datasheet

Laminin Antibodies

Laminin is key extracellular-matrix regulator of cell adhesion, migration, differentiation and proliferation.

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Human, Mouse
Clonality Polyclonal
Application IF, IHC, ELISA
Cat. No. ABIN1534452
Quantity 100 μg
Datasheet Datasheet
Reactivity Human, Mouse
Clonality Polyclonal
Application ELISA, IF, IHC (p)
Cat. No. ABIN6281996
Quantity 50 μL
Datasheet Datasheet

MMP1 (Collagenase-1) Antibodies

Player in ECM Degradation. EMC targets are: Collagens I, II, III, VII, and X; gelatins; aggrecan; entactin; tenascin; perlecan

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
Datasheet
Reactivity Human
Clonality Monoclonal
Application ICC, FACS, IHC, ELISA, WB
Cat. No. ABIN969287
Quantity 100 μL
Datasheet Datasheet
Reactivity Human
Clonality Polyclonal
Application WB
Cat. No. ABIN3043405
Quantity 100 μg
Datasheet Datasheet

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).

You are here:
客服