Human Matrilin-2 Antibody Summary
Arg24-Arg937
Accession # AAH10444
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Matrilin‑2 in U2OS Human Cell Line. Matrilin‑2 was detected in immersion fixed U2OS human osteosarcoma cell line using Goat Anti-Human Matrilin‑2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3044) at 5 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; NL001) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. Staining was performed using our protocol for Fluorescent ICC Staining of Non-adherent Cells.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Matrilin-2
Matrilin-2 is an extracellular matrix protein that belongs to the superfamily of von Willebrand factor A (VWA) containing proteins. It is expressed in many tissues and functions as a bridging component between other matrix proteins (1‑4). The human Matrilin-2 cDNA encodes a 956 amino acid (aa) precursor with a 23 aa signal sequence, two VWA domains separated by ten tandem EGF-like repeats, and a C-terminal coiled-coil domain (5, 6). Alternate splicing generates Isoform 2 (with an 18 aa deletion near the C-terminus), Isoform 3 (with a deletion of the fourth EGF-like repeat), and Isoform 4 (with a deletion of the first VWA and first EGF-like repeat). Human Matrilin-2 shares 87% and 84% aa sequence identity with mouse and canine Matrilin-2, respectively, and 27%, 22%, and 33% aa sequence identity with human Matrilin-1, -3, and -4, respectively. Matrilin-2 forms a variety of disulfide-linked oligomers via its coiled-coil domain (4, 7, 8, 9). It can assemble into homotrimers or heterotrimers with Matrilin-1 and/or Matrilin-4 (4, 7, 8) but has not been detected in heterotrimers containing Matrilin-3 (8). The VWA domains are thought to mediate Matrilin-Matrilin interactions as well as interactions with other matrix proteins such as Fibronectin, Collagen I, Fibrillin-2, and Laminin-1/Nidogen-1 complexes (7). Matrilin-2 knockout mice do not display any obvious abnormalities, suggesting that the expression of other molecules can compensate for the lack of Matrilin-2 (10).
- Wagener, R. et al. (2005) FEBS Lett. 579:3323.
- Deak, F. et al. (1999) Matrix Biol. 18:55.
- Whittaker, C.A. and R.O. Hynes (2002) Mol. Biol. Cell 13:3369.
- Piecha, D. et al. (1999) J. Biol. Chem. 274:13353.
- Muratoglu, S. et al. (2000) Cytogenet. Cell Genet. 90:323.
- Deak, F. et al. (1997) J. Biol. Chem. 272:9268.
- Piecha, D. et al. (2002) Biochem. J. 367:715.
- Frank, S. et al. (2002) J. Biol. Chem. 277:19071.
- Pan, O.H. and K. Beck (1998) J. Biol. Chem. 273:14205.
- Mates, L. et al. (2004) Matrix Biol. 23:195.
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