Recombinant Human Serpin B2/PAI-2 Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit uPA cleavage of a peptide substrate, N-carbobenzyloxy-Gly-Gly-Arg-7-amido-4-methylcoumarin (Z-GGR-AMC). <br /><p>The inhibition IC<sub>50</sub> is <15 nM, as measured under the described conditions. <br></p><br /><br />
<1.000 EU per 1 µg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Enzyme Activity
Theoretical MW
44 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
41 kDa, reducing conditions
Publications
Read Publication using 9206-PI in the following applications:
Store the unopened product at -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
Buffer
Supplied as a 0.2 μm filtered solution in Sodium Acetate, NaCl and Chaps.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Serpin B2/PAI-2 Protein, CF
HsT1201
Monocyte Arg-serpin
PAI
PAI2
PAI2Urokinase inhibitor
Placental plasminogen activator inhibitor
PLANH2
PLANH2PAI-2
plasminogen activator inhibitor 2
plasminogen activator inhibitor, type II (arginine-serpin)
serine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 2
Serpin B2
serpin peptidase inhibitor, clade B (ovalbumin), member 2
Urokinase Inhibitor
Background
Serpin B2, also known as PAI-2, is an approximately
60 kDa serine protease inhibitor (1). It is primarily secreted by macrophages
and monocytes (2, 3) and can form disulfide-linked multimers (4, 5). Serpin B2
inhibits both the urokinase-type and tissue-type plasminogen activators (uPA
and tPA) (3, 4, 6). Serpin B2 also promotes the clearance of uPA by enhancing
its binding and uptake by LRP (7). It limits fibril formation by Huntington
protein (HTT) and beta-Amyloid peptides (8). It promotes Th2 biased immune
responses and is important for intestinal CCL2 production, monocyte recruitment,
and nematode clearance (2, 9). A non-glycosylated form of Serpin B2 is retained
intracellularly where it interferes with TNF-a induced
apoptosis by protecting the Retinoblastoma protein (RB1) from calpain digestion
(10). It also inhibits proteasome activity in activated endothelial cells (11).
Serpin B2 is upregulated in HIV-1 infected PBMC, induces RB1 upregulation, and
promotes HIV-1 replication (12). Human Serpin B2 shares 76% and 73% amino acid
sequence identity with mouse and rat Serpin B2, respectively.
Shea-Donohue, T. et al. (2014) Gut Microbes 5:254.
Schroder, W.A. et al. (2010) J. Immunol. 184:2663.
Ritchie, H. et al. (1999) Thomb. Haemost. 81:96.
Mikus, P. et al. (1993) Eur. J. Biochem. 218:1071.
Wilczynska, M. et al. (2003) EMBO J. 22:1753.
Baker, M.S. et al. (1990) Cancer Res. 50:4676.
Croucher, D. et al. (2006) J. Biol. Chem. 281:10206.
Lee, J.A. et al. (2015) PLoS One 10:e0130136.
Zhao, A. et al. (2013) J. Immunol. 190:5779.
Tonnetti, L. et al. (2008) Cancer Res. 68:5648.
Boncela, J. et al. (2011) J. Biol. Chem. 286:43164.
Darnell, G.A. et al. (2006) J. Biol. Chem. 281:31348.
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