Recombinant Human Twisted Gastrulation (TSG) Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Twisted Gastrulation (TSG) Protein, CF Summary

• 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 4-16 μg/mL in the presence of 100 ng/mL of Recombinant Human BMP-6 (Catalog # 507-BP).

• Source: Chinese Hamster Ovary cell line, CHO-derived human TSG protein
  Met1-Phe223
• Accession #: NP_065699
• N-terminal Sequence: Cys26
• Structure / Form: Monomer
• Protein/Peptide Type: Recombinant Proteins
• Gene: TWSG1
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 22.1 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.
• SDS-PAGE: 35-43 kDa, reducing conditions

Packaging, Storage & Formulations

• 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Twisted Gastrulation (TSG) Protein, CF

• TSG
• TSGtwisted gastrulation protein homolog 1
• twisted gastrulation homolog 1 (Drosophila)
• TWSG1

Background

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). Human 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). An alternate start site at aa 76 can create a 148 aa isoform that lacks the BMP binding region (4). Human TSG shares 98% aa identity with mouse and rat TSG, and 99.5% aa identity with canine, equine, bovine and porcine TSG. TSG can act as either an antagonist or an agonist for BMP signaling (1 ‑ 11). As an antagonist, the N-terminal domain of TSG can bind and inhibit BMP proteins directly, interfering with BMP receptor binding and activity (1, 5). Formation of a complex of TSG with chordin further enhances BMP inhibition (1, 5). As a BMP agonist, TSG promotes TLL-1 metalloproteinase cleavage of chordin to fragments that no longer inhibit BMP activity (3, 6). 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, 6 ‑ 9). In bone, TSG participates with crossveinless-2 (CV-2) to create BMP activity gradients and limit osteoclast differentiation (7, 8). Postnatally, TSG is strongly expressed in growth plate cartilage where it limits collagen expression and enhances osteoblast differentiation and endochondral ossification (2, 5). TSG also modulates BMP and TGF-beta signaling in thymocytes, T cells and early erythrocytes (10 ‑ 12).

1. Scott, I.C. et al. (2001) Nature 410:475.
2. Gazzerro, E. et al. (2006) Bone 39:1252.
3. Oelgeschlager, M. et al. (2003) Development 130:4047.
4. SwissProt Accession # Q9GZX9.
5. Schmidl, M. et al. (2006) J. Biol. Chem. 281:31790.
6. Zakin, L. and E.M. De Robertis (2004) Development 131:413.
7. Sotillo Rodriguez, J.E. (2009) J. Bone Miner. Res. 24:1917.
8. Zakin, L. et al. (2008) Dev. Biol. 323:6.
9. Nosaka, T. et al. (2003) Mol. Cell. Biol. 23:2969.
10. Graf, D. et al. (2002) J. Exp. Med. 196:163.
11. Tzachanis, D. et al. (2007) Blood 109:2944.
12. Tanno, T. et al. (2009) Blood 114:181.

Publications for TSG (6684-TG)(3)

Publications using 6684-TG

• JS Esser, RE Steiner, M Deckler, H Schmitt, B Engert, S Link, A Charlet, C Patterson, C Bode, Q Zhou, M Moser Extracellular bone morphogenetic protein modulator BMPER and twisted gastrulation homolog 1 preserve arterial-venous specification in zebrafish blood vessel development and regulate Notch signaling in endothelial cells FEBS J., 2018-03-09;0(0):. 2018-03-09 [PMID: 29473997] (Bioassay, Human)
• Olsen O, Wader K, Misund K, Vatsveen T, Ro T, Mylin A, Turesson I, Stordal B, Moen S, Standal T, Waage A, Sundan A, Holien T Bone morphogenetic protein-9 suppresses growth of myeloma cells by signaling through ALK2 but is inhibited by endoglin. Blood Cancer J, 2014-03-21;4(0):e196. 2014-03-21 [PMID: 24658374] (Bioassay, Human)
• Yamada , Sachiko, Nakamura , Jin, Asada , Misako, Takase , Masayuki, Matsusaka , Taiji, Iguchi , Taku, Yamada , Ryo, Tanaka , Mari, Higashi , Atsuko Y, Okuda , Tomohiko, Asada , Nariaki, Fukatsu , Atsushi, Kawachi , Hiroshi, Graf , Daniel, Muso , Eri, Kita , Toru, Kimura , Takeshi, Pastan , Ira, Economides , Aris N, Yanagita , Motoko Twisted gastrulation, a BMP antagonist, exacerbates podocyte injury. PLoS ONE, 2014-02-25;9(2):e89135. 2014-02-25 [PMID: 24586548] (Bioassay, Mouse)

Bioinformatics

• Gene Symbol: TWSG1
• Uniprot:
  • NP_065699()