Recombinant Human Serpin E2/PN1 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Inhibition Activity
Format
Carrier-Free

Order Details

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.
Source
Mouse myeloma cell line, NS0-derived human Serpin E2/PN1 protein
Met1-Pro397, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Ser20
Protein/Peptide Type
Recombinant Enzymes
Gene
SERPINE2
Purity
>95%, 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

Theoretical MW
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.
SDS-PAGE
50 kDa, reducing conditions
Publications
Read Publications using
2980-PI in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Sodium Acetate, NaCl and Glycerol.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Assay Procedure
  • Assay Buffer: 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5 (TCNB)
  • Recombinant Human Serpin E2/PN1(rhSerpin E2) (Catalog # 2980-PI)
  • Trypsin (Sigma, Catalog # T-1426)
  • Substrate: MCA-Arg-Pro-Lys-Pro-Val-Glu-NVAL-Trp-Arg-Lys(DNP)-NH2 (Catalog # ES002)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute Trypsin to 0.25 μg/mL in Assay Buffer and KEEP ON ICE.
  2. Prepare a curve of rhSerpin E2 (MW: 43,200 Da) in Assay Buffer. Make the following serial dilutions: 250, 100, 50, 30, 20, 10, 5, 2.5, and 0.5 nM.
  3. Combine equal volumes of diluted Trypsin and rhSerpin E2 at each concentration of the curve. Include two controls containing equal volumes of Assay Buffer and diluted Trypsin without any rhSerpin E2.
  4. Incubate at room temperature for 30 minutes.
  5. Dilute reaction mixtures five fold in Assay Buffer.
  6. Dilute Substrate to 20 μM in Assay Buffer.
  7. Load 50 μL of the rhSerpin E2 curve in a plate, and start the reaction by adding 50 μL of 20 μM Substrate to wells.
  8. Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively, in kinetic mode for 5 minutes.
  9. Derive the 50% inhibition concentration (IC50) for rhSerpin E2 by plotting RFU/min (or specific activity) vs. concentration with 4-PL fitting.
  10. The specific activity for Trypsin at each point may be determined using the following formula (if needed):

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

     *Adjusted for Substrate Blank
     **Derived using calibration standard MCA-Pro-Lys-OH (Bachem, Catalog # M-1975).

Per Well:
  • Trypsin:  0.00125 μg
  • rhSerpin E2 curve: 12.5, 5, 2.5, 1.5, 1, 0.5, 0.25, 0.125, and 0.025 nM
  • Substrate: 10 μM

Notes

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

  • GDN
  • GdNPF
  • GDNserine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogenactivator inhibitor type 1), member 2
  • glia-derived nexin
  • glial-derived neurite promoting factor
  • Peptidase inhibitor 7
  • PI-7
  • PI7DKFZp686A13110
  • PN-1
  • PN1nexin
  • PNI
  • Protease nexin 1
  • Protease nexin I
  • Proteinase Nexin 1
  • Serpin E2
  • serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitortype 1), member 2

Background

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).

  1. Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
  2. Rossignol, P. et al. (2004) J. Biol. Chem. 279:10346.
  3. Lin, H.J. et al. (2005) Int. J. Dev. Neurosci. 23:9.
  4. Meins, M. et al. (2001) J. Neurosci. 21:8830.
  5. Buchholz, M. et al. (2003) Cancer Res. 63:4945.
  6. Murer, V. et al. (2001) Proc. Natl. Acad. Sci. USA 98:3029.
  7. Strausberg, R.L. et al. (2002) Proc. Natl. Acad. Sci. USA 99:16899.
  8. Sommer, J. et al. (1987) Biochemistry 26:6407.
  9. Gloor, S. et al. (1986) Cell 47:687.
  10. McGrogan, M. et al. (1988) Bio/Technology 6:172.

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Publications for Serpin E2/PN1 (2980-PI)(8)

We have publications tested in 2 confirmed species: Human, Synthetic.

We have publications tested in 1 application: Bioassay.


Filter By Application
Bioassay
(7)
All Applications
Filter By Species
Human
(6)
Synthetic
(1)
All Species
Showing Publications 1 - 8 of 8.
Publications using 2980-PI Applications Species
R Szabo, TH Bugge Loss of HAI-2 in mice with decreased prostasin activity leads to an early-onset intestinal failure resembling congenital tufting enteropathy PLoS ONE, 2018;13(4):e0194660. 2018 [PMID: 29617460] (Bioassay) Bioassay
EM Langer, ND Kendsersky, CJ Daniel, GM Kuziel, C Pelz, KM Murphy, MR Capecchi, RC Sears ZEB1-repressed microRNAs inhibit autocrine signaling that promotes vascular mimicry of breast cancer cells Oncogene, 2017;0(0):. 2017 [PMID: 29084210] (Bioassay, Human) Bioassay Human
The Involvement of Protease Nexin-1 (PN1) in the Pathogenesis of Intervertebral Disc (IVD) Degeneration Sci Rep, 2016;6(0):30563. 2016 [PMID: 27460424] (Bioassay, Human) Bioassay Human
Santoro A, Conde J, Scotece M, Abella V, Lois A, Lopez V, Pino J, Gomez R, Gomez-Reino J, Gualillo O SERPINE2 Inhibits IL-1alpha-Induced MMP-13 Expression in Human Chondrocytes: Involvement of ERK/NF-kappaB/AP-1 Pathways. PLoS ONE, 2015;10(8):e0135979. 2015 [PMID: 26305372] (Bioassay, Human) Bioassay Human
Szabo, Roman, Uzzun Sales, Katiuchi, Kosa, Peter, Shylo, Natalia, Godiksen, Sine, Hansen, Karina K, Friis, Stine, Gutkind, J Silvio, Vogel, Lotte K, Hummler, Edith, Camerer, Eric, Bugge, Thomas H Reduced prostasin (CAP1/PRSS8) activity eliminates HAI-1 and HAI-2 deficiency-associated developmental defects by preventing matriptase activation. PLoS Genet, 2012;8(8):e1002937. 2012 [PMID: 22952456] (Synthetic) Synthetic
Sales KU, Masedunskas A, Bey AL Matriptase initiates activation of epidermal pro-kallikrein and disease onset in a mouse model of Netherton syndrome. Nat. Genet., 2010;42(8):676-83. 2010 [PMID: 20657595] (Bioassay, Human) Bioassay Human
Myerburg MM, McKenna EE, Luke CJ, Frizzell RA, Kleyman TR, Pilewski JM Prostasin expression is regulated by airway surface liquid volume and is increased in cystic fibrosis. Am. J. Physiol. Lung Cell Mol. Physiol., 2008;294(5):L932-41. 2008 [PMID: 18310226] (Bioassay, Human) Bioassay Human
List K, Currie B, Scharschmidt TC, Szabo R, Shireman J, Molinolo A, Cravatt BF, Segre J, Bugge TH Autosomal ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice. J. Biol. Chem., 2007;282(50):36714-23. 2007 [PMID: 17940283] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol SERPINE2
Uniprot