Recombinant human gremlin 1 protein (Qk015)

Human gremlin 1 protein is a BMP-inhibitor present in the natural intestinal niche and provides an alternative to noggin for optimisation of intestinal organoid culture and iPSC differentiation.

Qkine gremlin 1 has been optimized by our experts to be an exceptionally high-purity 18 kDa highly bioactive dimeric protein, animal origin-free (AOF) and carrier protein free.

Orders are typically shipped same or next day (except Friday).
Easy world-wide ordering, direct or through our distributors.

1000µg will be despatched as 2 x 500µg

Fast and free shipping.
Buy online with secure credit card or purchase order.
For any questions, please email orders@qkine.com

Summary

  • High purity human gremlin 1 protein (Uniprot: O60565)

  • >98%, by SDS-PAGE quantitative densitometry

  • 18 kDa

  • Expressed in E. coli

  • Animal origin-free (AOF) and carrier protein-free.

  • Manufactured in our Cambridge, UK laboratories

  • Lyophilized from acetonitrile, TFA

  • Resuspend in 10 mM HCl at >100 µg/ml (provided with protein and free of charge), prepare single use aliquots, add carrier protein if desired and store frozen at -20°C or -80°C

Featured applications

  • Tumor organoid culture

Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2, CKTSF1B1, DAND2, DRM

Human, bovine, porcine

Species similarity:
mouse – 99%
rat – 99%

Bioactivity

human Gremlin Qk015 protein bioactivity lot 011

Gremlin-1 inhibits BMP-2 induced luciferase activity BRE-HEK293 luciferase reporter assay with an IC50 = 34 ng/ml (1.88 nM). Gremlin 1 activity is determined using inhibition of the BMP-2 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 dilution of gremlin 1 in BMP-2 for 6 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. Data from Qk015 batch #011.

Purity

Human Gremlin Qk015 protein purity SDS-PAGE lot #011

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 electrophoresis which gives the characteristic diffuse band. Purified recombinant protein (7 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250.  Data from Qk015 lot #011.

Further quality assays

  • Mass spectrometry: single species with expected mass

  • Analytical reversed-phase: single sharp peak

  • Endotoxin: <0.005 EU/μg protein (below level of detection)

  • Recovery from stock vial:  >95%

We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine.  All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.

Protein background

Gremlin 1 protein (GREM1, isoform-1) belongs to the bone morphogenetic protein (BMP) antagonist family. Gremlin 1 protein binds BMP-2, BMP-4, BMP-7 and other BMP family proteins [1] and inhibits receptor binding. It is highly expressed in the small intestine at the base of the intestinal crypts, as are the related proteins, gremlin 2 and chordin-like 1. In this niche, they help maintain the stem cell population by inhibiting BMP produced by mesenchymal cells [2]. Expression of gremlin 1 protein is also detected in fetal brain and colon, and at lower levels in adult brain, prostate, pancreas and skeletal muscle.

Recombinant human gremlin 1 protein and other BMP-antagonists, such as noggin, are used in the derivation, growth and maintenance of organoids from epithelial tissues including intestinal, liver and pancreatic organoids. However, roles for recombinant gremlin 1 protein in cancer stem cell maintenance in glioblastoma have been suggested [3].

[1] Kišonaitė, M., Wang, X. & Hyvönen, M. Structure of Gremlin-1 and analysis of its interaction with BMP-2. The Biochemical journal 473, 1593–1604 (2016).  doi.org/10.1042/BCJ20160254

[2] Kosinski, C. et al. Gene expression patterns of human colon tops and basal crypts and BMP antagonists as intestinal stem cell niche factors. Proceedings of the National Academy of Sciences of the United States of America 104, 15418–15423 (2007). doi.org/10.1073/pnas.0707210104

[3] Yan, K. et al. Glioma cancer stem cells secrete Gremlin1 to promote their maintenance within the tumor hierarchy. Genes & development 28, 1085–1100 (2014). doi: 10.1101/gad.235515.113

Publications using recombinant human gremlin 1 protein (Qk015)

Basal delamination during mouse gastrulation primes pluripotent cells for differentiation.
In ScienceDirect on 20 May 2024 by Sato, N., et al.

Our products are for research use only and not for diagnostic or therapeutic use.  Products are not for resale.

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