Recombinant Human Decorin Protein, CF

Measured by its binding ability in a functional ELISA. Recombinant Human Decorin Protein (Catalog # 11808-DE) binds to collagen with an ED50 of <100 ng/mL.

2 μg/lane of Recombinant Human Decorin Protein (Catalog # 11808-DE) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands 38-47 kDa, under reducing conditions.

• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Decorin Protein, CF Summary

• Additional Information: CHO expressed
• Details of Functionality: Measured by its binding ability in a functional ELISA. Recombinant Human Decorin binds to collagen with an ED₅₀ of <100 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human Decorin protein
  Asp31-Lys359
• N-terminal Sequence: Asp31
• Protein/Peptide Type: Recombinant Proteins
• Purity: >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
• Theoretical MW: 36 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: 38-47 kDa, under reducing conditions.

Packaging, Storage & Formulations

• 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 100 μg/mL in water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Decorin Protein, CF

• Bone proteoglycan II
• CSCD
• DCN
• decorin proteoglycan
• Decorin
• dermatan sulphate proteoglycans II
• DSPG2
• PG40
• PGII
• PG-II
• PGS2
• PG-S2
• proteoglycan core protein
• SLRR1B
• SLRR1BPGS2
• small leucine-rich protein 1B

Background

Decorin, also known as PG40 and PGS2, is a secreted chondroitin/dermatan sulfate proteoglycan in the family of small leucine‑rich proteoglycans (SLRPs). SLRP family members are characterized by N‑terminal and C‑terminal cysteine‑rich regions which flank the central region containing 10 ‑ 12 tandem leucine‑rich repeats (LRR) (1). The human Decorin cDNA encodes a 359 amino acid (aa) precursor that includes a 16 aa signal sequence and a 14 aa propeptide (2). Mature human Decorin contains twelve tandem LRR and shares 80% and 78% aa sequence identity with mouse and rat Decorin, respectively. Alternate splicing of human Decorin generates five isoforms with variable length deletions. Decorin is an N‑glycosylated protein that also carries a variably‑sized hybrid chondroitin/dermatan sulfate chain at Ser34 (3, 4). Naturally occurring Decorin proteoglycan has a molecular mass of approximately 100 kDa, and the deglycosylated Decorin core protein has a mass of approximately 40 kDa (5). Decorin regulates assembly of the extracellular collagen matrix and the bioactivity of the matrix associated growth factors FGF‑2, GDF‑8/Myostatin, TGF‑ beta , and WISP‑1 (4, 6 ‑ 9). It also binds and activates EGF R, ErbB4, and IGF‑I R (10 ‑ 12). In vivo, Decorin promotes myoblast differentiation, supports angiogenesis, and inhibits tumor progression (13 ‑ 16). Decorin is cleared from the extracellular space by LRP‑mediated endocytosis (17).

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4. Zamfir, A. et al. (2003) Glycobiology 13:733.
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12. Schonherr, E. et al. (2005) J. Biol. Chem. 280:15767.
13. Olguin, H.C. et al. (2003) Dev. Biol. 259:209.
14. Schonherr, E. et al. (2004) J. Vasc. Res. 41:499.
15. Seidler, D.G. et al. (2006) J. Biol. Chem. 281:26408.
16. Reed, C.C. et al. (2005) Oncogene 24:1104.
17. Brandan, E. et al. (2006) J. Biol. Chem. 281:31562.