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.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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.
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.
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