详细说明
Purity
>95%, by SDS-PAGE with silver staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to inhibit BMP-4-induced activity in MC3T3‑E1 mouse preosteoblast cells. The ED 50 for this effect is 0.03-0.12 μg/mL
Source
E. coli-derived Arg22-Gln168 with an N-terminal Met
Accession #
N-terminal Sequence
AnalysisMet
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
17 kDa
SDS-PAGE
18 kDa, reducing conditions
8436-PR |
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Formulation Lyophilized from a 0.2 μm filtered solution in HCl. | ||
Reconstitution Reconstitute at 500 μg/mL in 4 mM HCl | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Data Images
| Recombinant Human PRDC/GREM2 (Catalog # 8436-PR) inhibits BMP-4-induced activity in MC3T3‑E1 mouse preosteoblast cells. The ED50 for this effect is 0.03-0.12 μg/mL |
Background: PRDC/GREM2
PRDC/GREM2 (Protein Related to DAN and Cerberus/Gremlin-2) is a secreted BMP antagonist belonging to the Cerberus/DAN (CAN) family. Similar to other CAN family members, PRDC/GREM2 has 6 conserved cysteine residues that form a cysteine knot, and two additional cysteine residues located in the loops of the cysteine knot (1-3). Mature human PRDC/GREM2 is synthesized as a 168 amino acid (aa) monomer. At the amino acid level, mature human PRDC/GREM2 shares 97% sequence identity with mature mouse PRDC/GREM2. PRDC/GREM2 is biologically active as a homodimer that assembles its subunits in a head-to-tail orientation. PRDC/GREM2 is up-regulated through Wnt/ beta -catenin signaling and has been shown to potently inhibit BMP-2, -4, and -7 (4-6). During early development PRDC/GREM2 is involved in tooth morphogenesis, osteogenesis, and neurogenesis (7-9). In the adult, PRDC/GREM2 is involved in bone repair and bone remodeling (10). PRDC/GREM2 has been detected in the adult ovary, brain, spleen, and colon (11). The biological activity of PRDC/GREM2 can be blocked by binding to heparin (4).
References:
Pearce, J.J. et al. (1999) Dev. Biol. 209:98.
Kattamuri, C. et al. (2012) Protein Expr. Purif. 82:389.
Minabe-Saegusa, C. et al. (1998) Dev. Growth Differ. 40:343.
Nolan, K. et al. (2013) Structure 21:1417.
Kattamuri, C. et al. (2012) J. Mol. Biol. 424:313.
Im, J. et al. (2007) Biochem. Biophys. Res. Commun. 354:296.
Vogel, P. et al. (2014) Vet. Pathol. [Epub ahead of print; PMID 24686385].
Kriebitz, N.N. et al. (2009) Dev. Biol. 336:280.
Ideno, H. et al. (2009) Exp. Cell Res. 315:474.
Dean, D.B. et al. (2010) J. Anat. 216:625.
Sudo, S. et al. (2004) J. Biol. Chem. 279:23134.
Long Name:
Protein Related to DAN and Cerberus/Gremlin-2
Entrez Gene IDs:
64388 (Human); 23893 (Mouse)
Alternate Names:
CKTSF1B2; CKTSF1B2FLJ21195; Cysteine knot superfamily 1, BMP antagonist 2; DAN domain family member 3; DAND3; DAND3Prdc; GREM2; gremlin 2; gremlin 2, cysteine knot superfamily, homolog; gremlin-2; PRDC; PRDCgremlin 2, cysteine knot superfamily, homolog (Xenopus laevis); Protein related to DAN and cerberus