Recombinant Human/Bovine Gremlin 1, Animal-Free Protein

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Gremlin 1 activity is determined using inhibition of the BMP2 response (Qk007 #010, 52 ng/ml) from a BMP2-responsive firefly luciferase reporter in stably transfected HEK293T cells. Cells are treated (n=4) with a serial ...read more
Gremlin 1 protein migrates as a single diffuse band at ~36 kDa in non-reducing (NR) and 19 kDa in reducing (R) conditions. The protein is a non-covalent dimer and it is the dissociation of the dimer during ...read more

Product Details

Summary
Reactivity Hu, Po, BvSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

View Available Formulations
Catalog# & Formulation Size Price

Recombinant Human/Bovine Gremlin 1, Animal-Free Protein Summary

Additional Information
Human/Bovine/Porcine
Details of Functionality
No significant difference between EC50 of reference and test lots
Source
E. coli-derived Gremlin protein
Accession #
Protein/Peptide Type
Animal-Free Recombinant Proteins
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
18 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
Dimeric Gremlin 1 protein only

Packaging, Storage & Formulations

Storage
Store lyophilized protein between -20 °C and -80 °C until the date of expiry.Avoid freeze-thaw cycles.
Buffer
Lyophilized from acetonitrile/TFA
Reconstitution Instructions
Resuspend in 10 mM HCl at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.

Notes

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.

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

Alternate Names for Recombinant Human/Bovine Gremlin 1, Animal-Free Protein

  • Cell proliferation-inducing gene 2 protein
  • CKTSF1B1gremlin 1, cysteine knot superfamily, homolog
  • Cysteine knot superfamily 1, BMP antagonist 1gremlin 1, cysteine knot superfamily, homolog (Xenopus laevis)
  • DAN domain family member 2
  • DAND2
  • DAND2GREMLIN
  • Down-regulated in Mos-transformed cells protein
  • DRM
  • DRMMGC126660
  • GREM1
  • gremlin 1
  • gremlin 1-like protein
  • Gremlin
  • gremlin-1
  • IHG-2
  • Increased in high glucose protein 2
  • increased in high glucose-2
  • proliferation-inducing gene 2

Background

Gremlin, also known as Increased in High Glucose protein 2 (IHG-2) and Down-regulated in Mos-transformed cells protein (Drm), is a 28 kDa member of the Dan family of secreted glycoproteins (1-3). Human Gremlin is synthesized as a 184 amino acid (aa) precursor that contains a 24 aa signal sequence and a 160 aa mature region (SwissProt # O60565). The mature region contains one potential site for N-linked glycosylation (Asn 42), a cysteine-rich region, and a cysteine-knot motif (aa 94‑184) whose structure is shared by members of the TGF-beta superfamily (3). Post-translational modifications include glycosylation and phosphorylation (3). Gremlin exists in both secreted and membrane-associated forms (3). There are two isoforms for human Gremlin. Isoform 1 is the standard protein, and in isoform 2, there is a deletion of aa 39‑79. Human Gremlin shares 99% and 86% aa sequence identity with mouse and chick Gremlin, respectively. Northern blot analysis shows that Gremlin mRNA is highly expressed in the small intestine, fetal brain and colon, and weakly expressed in adult brain, ovary, prostate, pancreas and skeletal muscle (4). Gremlin functions as a bone morphogenetic protein (BMP) antagonist. It acts by binding to, and forming heterodimers with, BMP-2, BMP-4, and BMP-7, thus preventing them from interacting with their cell surface receptors (1). This mechanism is thought to be responsible for the pattern-inducing activity of Gremlin during embryonic development (5) and to play a role in human diseases, such as diabetic nephropathy (6). However, intracellular BMP-independent mechanisms of action (7) may mediate the ability of Gremlin to suppress transformation and tumorigenesis under certain experimental conditions (8-9). Gremlin also interacts with Slit proteins and acts as an inhibitor of monocyte chemotaxis (10). In addition, Gremlin has been found to be a proangiogenic factor expressed by endothelium (9).

  1. Hsu, D.R. et al. (1998) Mol. Cell 1:673.
  2. McMahon, R. et al. (2000) J. Biol. Chem. 275:9901.
  3. Wordinger, R.J. et al. (2008) Exp. Eye Res. 87:78.
  4. Topol, L.Z. et al. (2000) Cytogenet. Cell Genet. 89:79.
  5. Khokha, M.K. et al. (2003) Nat. Genet. 34:303.
  6. Lappin, D.W. et al. (2002) Nephrol. Dial. Transplant 17:65.
  7. Chen, B. et al. (2002) Biochem. Biophys. Res. Commun. 295:1135.
  8. Topol, L.Z. et al. (1997) Mol. Cell. Biol. 17:4801.
  9. Stabile, H. et al. (2007) Blood 109:1834.
  10. Chen, B. et al. (2004) J. Immunol. 173:5914.

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