Measured by its binding ability in a functional ELISA. When human Cytochrome c is coated at 1 μg/mL (100 μL/well), the concentration of Recombinant Human LRG1 that produces 50% of the optimal binding response is 3-15 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human LRG1 protein Val36-Gln347, with a C-terminal 6-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
35.2 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
40-60 kDa, reducing conditions
Publications
Read Publications using 7890-LR 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 and Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 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 LRG1 Protein, CF
1300008B03Rik
2310031E04Rik
HMFT1766
leucine-rich alpha-2-glycoprotein 1
leucine-rich alpha-2-glycoprotein
LRG1
LRGleucine rich alpha 2 glycoprotein
Background
LRG1 (leucine-rich alpha -2-glycoprotein 1) is an approximately 50 kDa secreted glycoprotein present in the plasma and other body fluids (1‑4). The human LRG1 cDNA encodes 347 amino acids (aa) that include a 35 aa signal sequence, eight leucine‑rich repeats (LRR), and an LRRCT (LRR C‑terminal) domain (1). Mature human LRG1 shares 66%, 63%, 75% and 72% aa sequence identity with mouse, rat, canine and porcine LRG1, respectively. LRG1 is up‑regulated during differentiation of neutrophils and present with myeloperoxidase in primary neutrophilic granules (1, 2). It can be produced by hepatocytes as an acute phase protein (5). LRG1 can interact directly with Cytochrome c, and is thought to act as a survival factor for lymphocytes in the presence of extracellular Cytochrome c (3, 6). Serum or plasma LRG1 is reported to be elevated in toxic shock syndrome, cardiac damage (produced by cardiomyocytes and correlating with BNP), autoimmune syndromes such as rheumatoid arthritis and Crohn’s disease, and some cancers such as those in the ovary and biliary tract (4, 7‑10). It is elevated in coronary sinus fluid during ventricular dysfunction and heart failure, and in peritoneal fluid of patients with uterine lyomyomas (8, 11).
O’Donnell, L.C. et al. (2002) J. Leukoc. Biol. 72:478.
Ai, J. et al. (2008) J. Leukoc. Biol. 83:1277.
Cummings, C. et al. (2006) Apoptosis 11:1121.
Weivoda, S. et al. (2008) J. Immunol. Methods 336:22.
Shirai, R. et al. (2009) Biochem. Biophys. Res. Commun. 382:776.
Codina, R. et al. (2010) Apoptosis 15:139.
Serada, S. et al. (2010) Ann. Rheum. Dis. 69:770.
Watson, C.J. et al. (2011) Circ. Heart Fail. 4:188.
Andersen, J.D. et al. (2010) J. Ovarian Res. 3:21.
Sandanayake, N.S. et al. (2011) Br. J. Cancer 105:1370.
Ferrero, S. et al. (2009) Arch. Gynecol. Obstet. 279:365.
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