Recombinant Human Serpin E2/PN1 Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Catalog # ES002). The IC50 value is <2 nM, as measured under the described conditions.
Mouse myeloma cell line, NS0-derived human Serpin E2/PN1 protein Met1-Pro397, with a C-terminal 10-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
43 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.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Serpin E2/PN1 Protein, CF
GDNserine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogenactivator inhibitor type 1), member 2
glial-derived neurite promoting factor
Peptidase inhibitor 7
Protease nexin 1
Protease nexin I
Proteinase Nexin 1
serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitortype 1), member 2
Serpin E2, also known as protease nexin I or glial-derived nexin (GDN), is a member of the Serpin superfamily of the serine protease inhibitors (1). Serpin E2 is a potent inhibitor of thrombin, plasmin and plasminogen activators (2). It is differentially expressed during neuronal differentiation and is able to transform human embryonic kidney cells into neuron-like cells (3). Its over‑expression in mice leads to progressive neuronal and motor dysfunction in these animals (4). It is also over‑expressed in the majority of pancreatic carcinoma as well as gastric and colorectal cancer samples whereas it is weakly expressed in all normal pancreas and chronic pancreatitis tissue samples (5). It plays an important role in controlling male fertility because its knockout male mice show a marked impairment in fertility from the onset of sexual maturity and its abnormal expression is found in the semen of men with seminal dysfunction (6). The deduced amino acid sequence of rhSerpin E2 is the same as that in NP_001130000, which predicts Arg329 in its 397 amino acid residues (7). An alternatively splice form predicts Thr-Gly at positions 329 and 330 in its 398 amino acid sequence (8-10).
Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
Rossignol, P. et al. (2004) J. Biol. Chem. 279:10346.
Lin, H.J. et al. (2005) Int. J. Dev. Neurosci. 23:9.
Meins, M. et al. (2001) J. Neurosci. 21:8830.
Buchholz, M. et al. (2003) Cancer Res. 63:4945.
Murer, V. et al. (2001) Proc. Natl. Acad. Sci. USA 98:3029.
Strausberg, R.L. et al. (2002) Proc. Natl. Acad. Sci. USA 99:16899.
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