Murine Gremlin-1 recombinant Protein
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Grem1, ld, Drm, Cktsf1b1
Description of Murine Gremlin-1
Gremlin was identified in a Xenopus expression cloning screen as a dorsalizing factor that can induce a secondary axis. A rat homolog, called Drm, was identified as a cDNA that was down regulated in v Mos transfected cells. Gremlin/Drm belongs to the DAN family of secreted glycoproteins that are BMP antagonists. Other members of the family include: Cerberus, Dante, PRDC, Caronte and DAN. DAN family members share a cysteine-rich domain that is structurally related to the cysteine-knot motif found in TGFß superfamily ligands. In vitro, Gremlin/Drm binds BMP4 and BMP2 indicating that it might interfere with BMP signaling. Gremlin/Drm acts as a BMP2/ 4 antagonist in a variety of tissues and developmental processes including: Xenopus animal cap explants, chick limb bud outgrowth and chondrogenesis, murine lung branching morphogenesis, and osteogenic differentiation of mouse myoblasts and bone marrow stromal cells. In addition, expression of Gremlin/Drm has been shown to be down-regulated in a wide range of human cancer cell lines. Murine, human, chick and Xenopus homologs of Gremlin share over 80% amino acid identity. It is likely that various DAN family members and other BMP antagonists including Noggin, Chordin, Follistatin and TSG can selectively antagonize the activities of different subsets of TGFß superfamily ligands.
Data not available.
Mouse Grem-1 should be reconstituted in 50 mM acetic acid or water to a concentration of 0.1 mg/ml. This solution can be diluted in water or other buffer solutions or stored at -20 °C.
Amino Acid Sequence
MKKKGSQGAI PPPDKAQHND SEQTQSPPQP GSRTRGRGQG RGTAMPGEEV LESSQEALHV TERKYLKRDW CKTQPLKQTI HEEGCNSRTI INRFCYGQCN SFYIPRHIRK EEGSFQSCSF CKPKKFTTMM VTLNCPELQP PTKKKRVTRV KQCRCISIDL D
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