Mouse TSG Biotinylated Antibody Summary
Met1-Phe222
Accession # Q9EP52
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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TSG in Mouse Embryonic Spinal Cord. TSG was detected in immersion fixed frozen sections of mouse embryonic spinal cord using 25 µg/mL Rat Anti-Mouse TSG Biotinylated Monoclonal Antibody (Catalog # BAM756) overnight at 4 °C. Tissue was stained with the Anti-Rat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS017) and counterstained with hematoxylin (blue). Specific labeling was localized to the mantle layer of the neural tube. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: TSG
Twisted Gastrulation (TSG) is a secreted, cysteine-rich protein that plays a role in dorsal/ventral patterning by regulating BMP signaling in Drosophila and Xenopus. TSG was originally identified in Drosophila melanogaster and shown to be required for the differentiation of the dorsal amnioserosa cells. Vertebrate TSGs were subsequently cloned in mouse, human, zebrafish and frog. Mouse TSG encodes a 222 amino acid (aa) residue precursor protein with a 24 aa residue putative signal peptide that is cleaved to generate the 198 aa residue mature protein. Studies of expression and function of Twisted Gastrulation have been performed in Drosophila and Xenopus. Xenopus TSG is expressed in the ventral regions of the embryo during gastrulation, mimicking the BMP-4 expression pattern. dTSG is expressed in dorsal cells of the blastoderm embryo, where there are also high levels of activity of Dpp and Screw. In vivo, TSG acts as an agonist for BMP signaling by modulating the inhibitory actions of the BMP antagonist, Chordin/Sog and the cleavage properties of the metalloprotease, xolloid/tolloid. The N-terminal domain of TSG can bind BMP protein directly in vitro and shows BMP antagonist activity.
- Mason, et al. (1994) Genes Dev. 8:1489.
- Oelgeschlager, et al. (2000) Nature 405:757.
- Yu, et al. (2000) Development 127:2143.
- Dale (2000) Current Biology 10:R671.
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