Qk015 Gremlin (human) Qkine protein vial

human-Gremlin-Qk015-protein-bioactivity-lot-011

recombinant human Gremlin 1 protein (Qk015)

Recombinant human Gremlin 1 protein has been optimized by our experts for exceptionally high-purity production and bioactivity. Gremlin-1 is a BMP-inhibitor present in the natural intestinal niche and provides an animal-free substitute for Noggin in chemically-defined media for many ESC, iPSC and organoid culture systems.

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enquiries, bulk and stock reservation, please email orders@qkine.com

1mg may be despatched as 2 x 500µg

description
customer & collaborator data

summary

high purity human Gremlin 1 protein (Uniprot: O60565)
18 kDa
expressed in E. coli
animal-free (AOF) and carrier protein-free.
manufactured in our Cambridge, UK laboratories
lyophilized from acetonitrile, TFA
resuspend in 10mM HCl at >100 µg/ml, prepare single use aliquots, add carrier protein if desired and store frozen at -20 oC or -80 oC

handling and storage FAQ

featured applications

tumor organoid culture

alternative protein names

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

background references

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).
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).
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).

bioactivity

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 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 dilution of Gremlin 1 in BMP2 for 6 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. Data from Qk015 batch #011.

purity

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%

request batch-specific CoA

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.

research areas

protein background

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 proteins¹ 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 cells². 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 suggested³.

We welcome all feedback and specialist collaborator data on all our products. If you would like to provide application-specific feedback for human Gremlin, please contact us info@qkine.com”

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

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