Measured by the ability of the immobilized protein to support the adhesion of BCE C/D‑1b bovine corneal endothelial cells. ≥50% of cells will adhere at 10 μg/mL Optimal dilutions should be determined by each laboratory for each application. Also measured by its ability to modulate collagen fibrillogenesis.
Source
Mouse myeloma cell line, NS0-derived mouse Lumican protein Gln19-Asn338, with a C-terminal 6-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Bioactivity2
Theoretical MW
37.3 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
55-65 kDa, reducing conditions
Publications
Read Publications using 2745-LU in the following applications:
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.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Lumican Protein, CF
KSPG lumican
LDC
LUM
lumican proteoglycan
Lumican
SLRR2D
SLRR2DLDCKeratan sulfate proteoglycan lumican
Background
Lumican is a 40 kDa member of the family of small leucine-rich repeat proteoglycans (SLRPs) and the class II subfamily (1). Mouse Lumican is synthesized as a 338 amino acid (aa) precursor that contains an 18 aa signal sequence and a 320 aa mature chain (SwissProt #: 51885). The mature chain contains a negatively charged N-terminal domain containing sulfated tyrosine and disulfide bonds, 12 leucine-rich repeats (LRRs), four potential sites of N-linked glycosylation, and a carboxyl terminal domain containing two conserved cysteines (1). Mature mouse Lumican is 98%, 88%, and 70% aa identical to mature rat, human, and chick Lumican, respectively. SLRPs constitute an important fraction of noncollagenous extracellular matrix proteins (ECM) proteins (1, 2). Lumican is expressed in a variety of tissues, including skin, artery, lung, cornea, kidney, bone, aorta, and articular cartilage (1). Lumican’s role in vivo has been found using Lumican null mice. These mice have functional deficits including corneal opacity as well as skin and tendon fragility associated with disorganized and loosely packed collagen fibers (1, 3-6). The abnormal connective tissue phenotype seen in the Lumican null mice shows the importance of the role of Lumican in collagen fibrillogenesis (1). In addition to the control of collagen fibril assembly, Lumican has been shown to play a role in the regulation of cell proliferation (7, 8), migration (8 - 9), and adhesion (9). Lumican’s overexpression has been reported in carcinoid tumor, breast, colorectal, neuroendocrine, uterine cervical and pancreatic cancers (10).
Nikitovic, D. et al. (2008) IUBMB Life 60:818.
Blochberger, T.C. et al. (1992) J. Biol. Chem. 267:347.
Chakravarti, S. et al. (1998) J. Cell Biol. 141:1277.
Chakravarti, S. et al. (2000) Invest. Ophthalmol. Vis. Sci. 41:3365.
Jepsen, K.J. et al. (2002) J. Biol. Chem. 277:35532.
Chakravarti, S. et al. (2003) Invest. Ophthalmol. Vis. Sci. 44:2422.
Vuillermoz, B. et al. (2004) Exp. Cell Res. 296:294
Nikitovic, D. et al. (2008) FEBS J. 275:350.
D’Onofrio, M.F. et al. (2008) Biochem. Biophys. Res. Commun. 365:266.
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