Recombinant Human Serpin E1/PAI-1 Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 1786-PI
Key Product Details
Source
Accession #
Conjugate
Applications
Product Specifications
Source
Met1-Pro402, with a C-terminal 10-His tag
Purity
Endotoxin Level
N-terminal Sequence Analysis
Predicted Molecular Mass
SDS-PAGE
Activity
The IC50 value is <13 nM, as measured under the described conditions.
Reviewed Applications
Read 1 review rated 5 using 1786-PI in the following applications:
Scientific Data Images for Recombinant Human Serpin E1/PAI-1 Protein, CF
Recombinant Human Serpin E1/PAI-1 Protein Enzyme Activity
Recombinant Human Serpin E1/PAI-1 (Catalog # 1786-PI) is measured by its ability to inhibit uPA cleavage of a peptide substrate, N-carbobenzyloxy-Gly-Gly-Arg-7-amido-4-methylcoumarin (Z-GGR-AMC).Formulation, Preparation and Storage
1786-PI
Formulation | Lyophilized from a 0.2 μm filtered solution in Sodium Acetate, NaCl and CHAPS. |
Reconstitution | Reconstitute at 500 μg/mL in sterile 50 mM Sodium Acetate and 100 mM NaCl, pH 5.5. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: Serpin E1/PAI-1
As a member of the Serpin superfamily of serine protease inhibitors, Serpin E1/PAI‑1 is the principal inhibitor of urokinase‑type plasminogen activator (uPA) and tissue‑type PA (1, 2). As important regulators of extracellular matrix remodeling, uPA and PAI‑1 play a major role in many processes such as angiogenesis, tumor invasion and obesity (2‑4). For example, uPA and PAI-1 are the only tumor prognostic factors validated at the highest level of evidence with regard to their clinical utility in breast cancer (5). The human PAI-1 is initially synthesized as 402 amino acid precursor with a N‑terminal signal peptide (6, 7). PAI‑1 may exist in one of two possible conformations, designated as active or latent (8). The purified rhPAI‑1 is active against rhuPA. The heterogeneity at the N‑terminus of the purified
rhPAI‑1 has been observed before for both the recombinant and native proteins (9).
References
- Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
- Stefansson, S. et al. (2003) Curr. Pharm. Des. 9:1545.
- Duffy, M.J. (2002) Clin. Chem. 48:1194.
- Juhan-Vague, I. et al. (2003) J. Thromb. Haemost. 1:1575.
- Harbeck, N. et al. (2002) Clin. Breast Cancer 3:196.
- Pannekoek, H. et al. (1986) EMBO J. 5:2539.
- Ginsburg, D. et al. (1986) J. Clin. Invest. 78:1673.
- Wang, Z. et al. (1996) Biochemistry 35:16443.
- Stromqvist, M. et al. (1994) Protein Expr. Purif. 5:309.
Long Name
Alternate Names
Gene Symbol
UniProt
Additional Serpin E1/PAI-1 Products
Product Documents for Recombinant Human Serpin E1/PAI-1 Protein, CF
Product Specific Notices for Recombinant Human Serpin E1/PAI-1 Protein, CF
For research use only