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Recombinant human Gremlin 1 protein
Qk015 Recombinant human Gremlin 1 protein has been optimised by our experts for exceptionally high-purity expression in E. coli without affecting its bioactivity. Produced in a dedicated ADCF laboratory, our recombinant human Gremlin 1 protein offers a highly pure, animal-free substitute for Noggin in chemically defined media for many ESC, iPSC and organoid culture systems.
Qk015 Recombinant human Gremlin 1 protein
Gremlin 1 protein (GREM1, isoform-1) belongs to the BMP (bone morphogenetic protein) antagonist family. Gremlin 1 protein binds BMP2, BMP4, BMP7 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).
Qk015 recombinant human Gremlin 1 protein is optimized for exceptionally high purity production from E. coli. All our proteins are animal-derived component free making them particularly suitable for applications requiring a chemically defined media. Recombinant human Gremlin-1 protein can also substitute for Noggin in several embryonic and induced-pluripotent stem cell and organoid culture systems.
Summary: human Gremlin 1 protein (Uniprot: O60565) expressed in E.coli and purified to homogeneity.
Molecular mass: 18 kDa
Form: protein is provided lyophilized from a fully volatile solution and is carrier protein free. All our proteins are animal-derived component free making them particularly suitable for applications requiring a chemically defined media.
Purity and bioactivity
For peace of mind that our recombinant human Gremlin 1 protein will work exactly the same way every day, from batch to batch and at any scale you need, we conduct extensive purity and bioactivity analysis, including SDS-PAGE, mass spectrometry, reverse phase chromatography, UV spectroscopy and endotoxin level testing.
To confirm the biochemical identity of our recombinant human Gremlin 1 protein and ensure that its purity meets are rigorous standards, we conduct SDS-PAGE on every protein batch. We also check the final refolded protein is bioactive my quantitative determination of inhibition of BMP protein activity in a BRE-HEK reporter assay in HEK293T cells. By knowing what the expected activity of the protein is and measuring calibrant alongside each batch of protein, we can use this bioassay to define a complete dose-response curve and check the EC50 value of every preparation of our recombinant human Gremlin 1 protein.
Find out more about our extensive purity testing in the next tab.
Example data from batch #011
Protein purity: SDS-PAGE in reduced and non-reduced conditions
Bioactivity: BRE-HEK293 luciferase reporter assay