When Recombinant Mouse Fc gamma RIIB/CD32b (1460-CD) is immobilized at 1 µg/mL (100 µL/well), Recombinant Mouse FGL2 HA-tag (Catalog # 10691-FL) binds with an ED50 of 0.1‑0.8 µg/mL.
2 μg/lane of Recombinant Mouse FGL2 HA-tag (Catalog # 10691-FL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 61-72 kDa ...read more
Measured by its binding ability in a functional ELISA. When
Recombinant Mouse Fc gamma RIIB/CD32b
(Catalog #
1460-CD) is immobilized at 1 µg/mL
(100 µL/well), Recombinant Mouse FGL2 HA-tag (Catalog # 10691-FL) binds with an
ED50 of 0.1-0.8 µg/mL. Measured
by its ability to inhibit anti-CD3-induced proliferation of mouse T
lymphocytes. The ED50 for this effect is 1.5-12 µg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse FGL2 protein
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Bioactivity2
Theoretical MW
48 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
61-72 kDa, under reducing conditions
Publications
Read Publications using 10691-FL in the following applications:
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 with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 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 Mouse FGL2 HA-tag Protein, CF
FGL2
fibrinogen-like 2
Fibrinogen-like protein 2
Fibroleukin
pT49T49
T49
Background
FGL2 (fibrinogen-like protein 2),
also called fibroleukin, is a 64-70 kDa secreted glycoprotein of the
Fibrinogen-like superfamily. It has prothrombinase activity and also promotes
T regulatory (Treg) activity (1-6). The mouse FGL2 gene encodes a
439 amino acid (aa) protein that contains a 23 aa signal sequence and
a 416 aa mature sequence with an N-terminal coiled-coil region and a C-terminal fibrinogen homology domain or FRED (1, 2). A 260-280 kDa FGL2 complex is
thought to be a tetramer formed by covalent disulfide linkage of dimers that
are associated via coiled-coil interactions (2, 3). Mature mouse FGL2 shares
79% and 91% homology with human and rat FGL2 respectively. FGL2 appears to have two
modes of action. One mode involves its prothrombinase activity, which requires
calcium and acidic phospholipids (4). This mode is thought to be active during
hepatitis viral infections when FGL2, produced by macrophages in response to
IFN-gamma, induces hepatic apoptosis and fibrin deposition (7). In addition,
FGL2 produced by endothelial cells in response to TNF-alpha within cardiac xenografts
or allografts promotes coagulation during acute vascular rejection (7-9). A
second mode of action involves soluble (not phospholipid-associated) FGL2 and
is independent of prothrombinase activity (2). Soluble FGL2 is required for
Treg function, and directly suppresses DC, T, and B cell immune reactivity;
consequently, some FGL2-deficent mice develop autoimmune glomerulonephritis
(5, 6). In vitro, soluble FGL2 can skew T cell polarization toward Th2 and inhibit
proliferation of stimulated T cells and maturation of DC (6). In
pregnancy, fetal trophoblast cells secrete FGL2. The immune suppressive mode of
FGL2 may prevent early fetal loss; however, the procoagulant mode is thought to
mediate infection-triggered abortion (10). In the central nervous system (CNS),
FGL2 was shown to be highly expressed in glioma stem cells and primary
glioblastoma cells and may serve as a critical immune oncology target (11).
Koyama, T. et al. (1987) Proc. Natl. Acad. Sci. USA 84:1609.
Marazzi, S. et al. (1998) J. Immunol.161:138.
Olson, G. E. et al. (2004) J. Biol. Chem. 279:51266.
Chan, C. W. Y. et al. (2002) J. Immunol. 168:5170.
Shalev, I. et al. (2008) J. Immunol.180:249.
Chan, C. W. Y. et al. (2003) J. Immunol. 170:4036.
Liu, M. et al. (2006) J. Immunol. 176:7028.
Mendicino, M. et al. (2005) Circulation 112:248.
Ning, Q. et al. (2005) J. Immunol. 174:7403.
Clark, D. A. et al. (2004) Mol. Hum. Reprod. 10:99.
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