>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
29.8 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
39 kDa, reducing conditions
Publications
Read Publications using 2326-TS in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse TSG-6 Protein, CF
Hyaluronate-binding protein
TNF alpha-induced protein 6
TNFAIP6
TNF-stimulated gene 6 protein
TSG6
TSG-6
TSG-6tumor necrosis factor alpha-inducible protein 6
TSG6tumor necrosis factor-inducible gene 6 protein
Tumor necrosis factor alpha-induced protein 6
tumor necrosis factor, alpha-induced protein 6
tumor necrosis factor-stimulated gene-6 protein
Background
TSG-6 (TNF-stimulated gene 6; also named TNFIP6) is a secreted, 35 - 39 kDa group A member of the LINK-Module superfamily of proteins (1 - 4). Mouse TSG-6 is synthesized as a 275 amino acid (aa) precursor. It contains a 17 aa signal sequence and a 258 aa mature region (5, 6). The mature region has an N-terminal link module (aa 36 - 129) and a C-terminal CUB (C1s/C1r; urchin embryonic growth factor; BMP1) domain (aa 135 - 246). Link modules bind hyaluronan (HA) and participate in extracellular matrix (ECM) assembly (7). Mature mouse TSG-6 shares 97%, 94% and 94% aa identity with rat, human and canine TSG-6, respectively. Cells reported to express TGF-6 include activated fibroblasts, synoviocytes, chondrocytes, neutrophils, proximal tubular epithelium, bronchial epithelium, endothelium, and visceral plus vascular smooth muscle (2, 8). TSG-6 has multiple functions, many of which involve the ECM. It is suggested to stabilize HA-rich ECM. It does so by serving as an intermediary, or as a link between the individual subunits of the extracellular decameric pentraxin 3 and the surrounding hyaluronan matrix (9). It also provides structure and organization to hyaluronan. This is accomplished by a TSG-6 mediated transfer of an 80 - 85 kDa protein subunit from I alpha I (inter-alpha -inhibitor) to HA. I alpha I is a four-component, 225 kDa serine protease inhibitor. It contains a protease inhibitor subunit (bikunin), two independent, accompaning protein chains (HC1 and HC2), and a short chondroitin sulfate linking moiety. TSG-6 is a catalyst for the removal and transient binding of either HC chain. Each chain is subsequently transferred and covalently-linked to the surrounding HA. This provides substance and reinforcement to the ECM (1, 2, 10, 11, 12). This disassembly of I alpha I also leads to free bikunin, which in the “free” state becomes a potent inhibitor of serine proteases (8).
Milner, C.M. et al. (2006) Biochem. Soc. Trans. 34:446.
Milner, C.M. and A.J. Day (2003) J. Cell Sci. 116:1863.
Wisnieewski, H-G. and J. Vilcek (2004) Cytokine Growth Factor Rev. 15:129.
Blundell, C.D. et al. (2005) J. Biol. Chem. 280:18189.
Fulop, C. et al. (1997) Gene 202:95.
Fulop, C. et al. (2003) Development 130:2253.
Kohda, D. et al. (1996) Cell 86:767.
Forteza, R. et al. (2007) Am. J. Respir. Cell Mol. Biol. 36:20.
Salustri, A. et al. (2003) Development 131:1577.
Rugg, M.S. et al. (2005) J. Biol. Chem. 280:25674.
Sanggaard, K.W. et al. (2006) Biochemistry 45:7661.
Sanggaard, K.W. et al. (2005) J. Biol. Chem. 280:11936.
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