金山科研平台，产品价格货期咨询微信：jinshanbio Source:Mouse myeloma cell line, NS0-derived, Lys25-Asp184, with a C-terminal 10-His tag Accession #:O60565 N-terminal Sequence Analysis:Lys25 Purity:>90%, by SDS-PAGE with silver staining. Predicted Molecular Mass:19.7 kDa SDS-PAGE:25-30 kDa, under reducing conditions Activity:Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cells.The ED₅₀ for this effect is typically 0.3-1.5 µg/mL in the presence of 75 ng/mL of Recombinant Human BMP‑4 (Catalog# 314-BP). Formulation:Lyophilized from a 0.2 µm filtered solution in PBS and EDTA.See Certificate of Analysis for details. Molecule Information: Gremlin Aliases: DAND2; DRM; GREM1 Entrez Gene IDs: 26585 (Human); 23892 (Mouse) Background: Gremlin

Post-translational modifications include glycosylation and phosphorylation. Gremlin exists in both secreted and membrane-associated forms. 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.

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. This mechanism is thought to be responsible for the pattern-inducing activity of Gremlin during embryonic development and to play a role in human diseases, such as diabetic nephropathy. However, intracellular BMP-independent mechanisms of action may mediate the ability of Gremlin to suppress transformation and tumorigenesis under certain experimental conditions. Gremlin also interacts with Slit proteins and acts as an inhibitor of monocyte chemotaxis. In addition, Gremlin has been found to be a proangiogenic factor expressed by endothelium.