Measured by its ability to modulate collagen fibrillogenesis. Ge, G. et al. (2004) J. Biol. Chem. 279:41626. At 15 µg/mL, rmMimecan can significantly retard the rate of type I collagen fibrillogenesis.
Source
Mouse myeloma cell line, NS0-derived mouse Mimecan protein Ala20-Phe298, with a C-terminal 6-His tag
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
32.6 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
50 kDa, reducing conditions
Publications
Read Publications using 2949-MC in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Mimecan Protein, CF
DKFZp586P2421
KSPG25
mimecan proteoglycan
Mimecan
OGN
OIF
OIFOG
osteoglycin (osteoinductive factor)
osteoglycin
Osteoinductive factor
SLRR3A
SLRR3Acorneal keratan sulfate proteoglycan
Background
Mimecan is a 34 kDa secreted monomeric glycoprotein that belongs to the SLRP, or small leucine-rich proteoglycan family of matrix molecules (1, 2). All SLRP family members contain multiple leucine rich repeats, of which there are two types; a 21 amino acid (aa) proline-containing S-type, and a 26 aa phenylalanine-containing T-type (2, 3). Mimecan is a class III SLRP subfamily member, which means it contains an S-T (vs. S-T-T) repeating motif. Mouse Mimecan is synthesized as a 298 aa precursor that contains a 19 aa signal sequence and a 279 aa mature region (3, 4). The mature region contains a 75 aa N-terminus followed by a 13 aa cysteine-rich region and seven consecutive LRR repeats. There is one (presumably occupied) C-terminal N-linked glycosylation site and a potential keratan sulfate attachment point in LRR #4 (aa 161 - 180) (3). Nomenclature for the mimecan molecule is confusing. Mimecan is best thought of as being the full-length, 279 aa glycoprotein (5). Proteolytic removal of the first 56 aa by BMP-1/Tolloid-like proteinases generates the 25 kDa KSPG form (aa 57 - 279) (3). The 17 kDa, 56 aa mature N-terminus has been referred to as the minecam prosegment (3). When the prosegment is removed, mature mouse KSPG (aa 57 - 279) is 98%, 91%, 90% and 91% aa identical to rat, bovine, human and canine KSPG, respectively. A 12 kDa form (aa 175 - 279) consisting of the 105 aa of the C-terminus (OIF/osteoglycan) has also been observed (6). Noncoding alternate splice forms for mouse are believed to exist and should be expressed in a tissue specific fashion (7, 8). No splice forms are known that impact the coding region. Mimecan seems to exist as proteoglycan (PG) and non-PG forms. In cornea, keratan sulfate is present, although the exact function of the PG is unknown. The corneal extracellular matrix is normally transparent. While mimecan is reported to inhibit fibrillogenesis, possibly by limiting lateral accretion of collagen monomers, it is unclear if the mimican PG actually contributes to transparency (3, 9). In other tissues, mimecan and its derivatives can exist as simple glycoproteins, absent of any PG adduct (6). The uncertain nature of mimecan’s structure and function gives rise to its name: Mime is a Norse-legend dwarf that was notoriously deceitful and misleading (6).
Iozzo, R.V. (1999) J. Biol. Chem. 275:18843.
Matsushima, N. et al. (2000) Proteins 38:210.
Ge, G. et al. (2004) J. Biol. Chem. 279:41626.
Ujita, M. et al. (1995) Gene 158:237.
Hu, S-M. et al. (2005) J. Clin. Endocrinol. Metab. 90:6657
Funderburgh, J.L. et al. (1997) J. Biol. Chem. 272:28089.
Tasheva, E.S. et al. (1999) J. Biol. Chem. 274:18693.
Tasheva, E.S. et al. (1997) J. Biol. Chem. 272:32551.
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