Mouse Matrilin-3 Antibody

Catalog # Availability Size / Price Qty
AF3357
AF3357-SP
Product Details
Citations (4)
FAQs
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Mouse Matrilin-3 Antibody Summary

Species Reactivity
Mouse
Specificity
Detects mouse Matrilin-3 in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 50% cross-reactivity with recombinant human Matrilin-3 is observed and 5% cross-reactivity with recombinant mouse (rm) Matrilin-2 and rmMatrilin-4 is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse Matrilin-3
Ala35-Arg481
Accession # AAH71224
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Mouse Matrilin‑3 (Catalog # 3357-MN)

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.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 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-3

Matrilin-3 is a 50‑60 kDa extracellular matrix protein that belongs to the superfamily of von Willebrand factor A (VWA) containing proteins. It is primarily expressed in cartilage and functions as a bridging component between proteins of the collagenous matrix (1‑3). The mouse Matrilin-3 cDNA encodes a 481 amino acid (aa) precursor with a 27 aa signal sequence, an N-terminal VWA domain, four tandem EGF-like repeats, and a C-terminal coiled-coil domain (4). The Matrilins differ in the number of VWA domains (one or two) and EGF-like repeats (one, three, four, or ten) they contain. Mouse Matrilin-3 shares 82% aa sequence identity with human Matrilin-3. Within the first VWA domain, mouse Matrilin-3 shares approximately 51% aa sequence identity with mouse Matrilin-1, -2, and -4. The coiled-coil domain of Matrilin-3 mediates disulfide-linked homo-oligomerization, with tetramer formation being the most dominant (5‑7). It can also assemble into hetero-oligomers with Matrilin-1 (5‑7). Matrilin-3 is more plentiful than Matrilin-1 in the proliferative zone of the growth plate, whereas the reverse is true in the maturation zone (5). Matrilin-3 interacts directly with Collagen IX and COMP (8, 9). In the absence of Collagen IX, the expression of Matrilin-3 is unchanged, although it is retained inside chondrocytes and is not incorporated into the matrix (9). Intracellular retention of Matrilin-3 also occurs with particular point mutations in the VWA domain that results in multiple epiphyseal dysplasia (11‑13). In contrast, a point mutation in the first EGF-like repeat which has been linked to hand osteoarthritis does not prevent Matrilin-3 secretion (13). Matrilin-3 knockout mice do not display any obvious abnormalities, suggesting that other molecules may compensate for the lack of Matrilin-3 (10).

References
  1. Wagener, R. et al. (2005) FEBS Lett. 579:3323.
  2. Deak, F. et al. (1999) Matrix Biol. 18:55.
  3. Whittaker, C.A. and R.O. Hynes (2002) Mol. Biol. Cell 13:3369.
  4. Wagener, R. et al. (1997) FEBS Lett. 413:129.
  5. Zhang, Y. and Q. Chen (2000) J. Biol. Chem. 275:32628.
  6. Klatt, A.R. et al. (2000) J. Biol. Chem. 275:3999.
  7. Frank, S. et al. (2002) J. Biol. Chem. 277:19071.
  8. Mann, H.H. et al. (2004) J. Biol. Chem. 279:25294.
  9. Budde, B. et al. (2005) Mol. Cell. Biol. 25:10465.
  10. Ko, Y. et al. (2004) Mol. Cell. Biol. 24:1691.
  11. Jackson, G.C. et al. (2004) J. Med. Genet. 41:52.
  12. Cotterill, S.L. et al. (2005) Hum. Mutat. 26:557.
  13. Otten, C. et al. (2005) J. Med. Genet. 42:774.
Entrez Gene IDs
4148 (Human); 17182 (Mouse)
Alternate Names
DIPOA; EDM5; HOA; matrilin 3; Matrilin3; Matrilin-3; NDUFC2; OADIP; OS2

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Citations for Mouse Matrilin-3 Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

4 Citations: Showing 1 - 4
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  1. XBP1 signalling is essential for alleviating mutant protein aggregation in ER-stress related skeletal disease
    Authors: KA Piróg, EP Dennis, CL Hartley, RM Jackson, J Soul, JM Schwartz, JF Bateman, RP Boot-Handf, MD Briggs
    PLoS Genet., 2019-07-01;15(7):e1008215.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC
  2. An inducible cartilage oligomeric matrix protein mouse model recapitulates human pseudoachondroplasia phenotype.
    Authors: Posey KL, Veerisetty AC, Liu P, Wang HR, Poindexter BJ, Bick R, Alcorn JL, Hecht JT
    Am. J. Pathol., 2009-09-17;175(4):1555-63.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC
  3. Skeletal abnormalities in mice lacking extracellular matrix proteins, thrombospondin-1, thrombospondin-3, thrombospondin-5, and type IX collagen.
    Authors: Posey KL, Hankenson K, Veerisetty AC, Bornstein P, Lawler J, Hecht JT
    Am. J. Pathol., 2008-05-08;172(6):1664-74.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: IHC-P
  4. Mesencephalic astrocyte-derived neurotropic factor is an important factor in chondrocyte ER homeostasis
    Authors: P. A. Bell, E. P. Dennis, C. L. Hartley, R. M. Jackson, A. Porter, R. P. Boot-Handford et al.
    Cell Stress and Chaperones

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