Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Details of Functionality | Measured by its ability to inhibit BMP-6-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cells. The ED50 for this effect is 1‑4 µg/mL in the presence of 150 ng/mL of Recombinant Human BMP-6 (Catalog # 507-BP). |
Source | Mouse myeloma cell line, NS0-derived mouse TSG protein Cys25-Phe222, with a C-terminal 10-His tag |
Accession # | |
N-terminal Sequence | Cys25 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Twsg1 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 23.5 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 25-35 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Twisted Gastrulation-1 (TSG or TWSG1) is a cysteine-rich 24 kDa secreted glycoprotein that regulates BMP signaling (1, 2). It was initially identified for its role in dorsal/ventral patterning in Drosophila and Xenopus (1). Mouse TSG cDNA encodes 223 amino acids (aa) including a 25 aa signal peptide and a 198 aa mature protein with a cysteine-rich region (aa 26 ‑ 77) that interacts with BMPs and a C-terminal binding site for chordin (1, 3). Mouse TSG shares 98% aa identity with human, rat, canine, equine, bovine and porcine TSG. TSG can act as either an antagonist or an agonist for BMP signaling (1 ‑ 10). As an antagonist, the N-terminal domain of TSG can bind and inhibit BMP proteins directly, interfering with BMP receptor binding and activity (1, 4). Formation of a complex of TSG with chordin further enhances BMP inhibition (1, 4). As a BMP agonist, TSG promotes TLL-1 metalloproteinase cleavage of chordin to fragments that no longer inhibit BMP activity (3, 5). TSG effects on chordin are influenced by its concentration (2). TSG is widely expressed in the mouse embryo, and is co‑expressed with chordin and BMPs 2, 4 and 7 in the developing limbs (1). Mice lacking TSG show varying degrees of abnormality in bone, cartilage, forebrain, thymus and spleen, in part dependent on the mouse background (2, 5 ‑ 8). In bone, TSG participates with crossveinless-2 (CV-2) to create BMP activity gradients and limit osteoclast differentiation (6, 7). Postnatally, TSG is strongly expressed in growth plate cartilage where it limits collagen expression and enhances osteoblast differentiation and endochondral ossification (2, 4). TSG also modulates BMP and TGF-beta signaling in thymocytes, T cells and early erythrocytes (9 ‑ 11).
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