Detects human Serpin E1 in direct ELISAs and Western blots. In direct ELISAs, no cross-reactivity with recombinant human Serpin A1, A3, A4, A8, C1, F1, F2, I1, I2, recombinant mouse Serpin D1 or E2 is observed.
Monoclonal Mouse IgG1 Clone # 242816
Protein A or G purified from hybridoma culture supernatant
S. frugiperda insect ovarian cell line Sf 21-derived recombinant human Serpin E1/PAI-1 Met1-Pro402 Accession # P05121
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Human Serpin E1/PAI‑1 Antibody (Catalog #
ELISA Detection (Matched Antibody Pair)
Human Serpin E1/PAI‑1 Biotinylated Antibody (Catalog #
Recombinant Human Serpin E1/PAI-1 Protein, CF (Catalog #
Measured by its ability to neutralize Recombinant Human Serpin E1/PAI-1 (0.25 µg/mL, Catalog # 1786-PI) inhibition of Recombinant Human u‑Plasminogen Activator (uPA)/Urokinase (0.1 µg/mL, Catalog # 1310-SE) cleavage of the fluorogenic peptide substrate Z-GGR-AMC (100 µM). The Neutralization Dose (ND50) is typically 0.3 µg/mL.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Detection of Human Serpin E1/PAI‑1 by Western Blot.
Western blot shows lysates of HUVEC human umbilical vein endothelial cells. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human Serpin E1/PAI‑1 Monoclonal Antibody (Catalog # MAB1786) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for Serpin E1/PAI‑1 at approximately 48 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Neutralization of Serpin E1/ PAI‑1 Activity by Human Serpin E1/PAI‑1 Antibody.
Recombinant Human u‑Plasminogen Activator (uPA)/Urokinase (0.1 µg/mL, Catalog # 1310-SE) activity is measured in the presence of Recombinant Human Serpin E1/PAI-1 (0.25 µg/mL, Catalog # 1786-PI) that has been preincubated with increasing concentrations of Mouse Anti-Human Serpin E1/PAI‑1 Monoclonal Antibody (Catalog # MAB1786). The ND50 is typically 0.3 µg/mL.
Detection of Human Serpin E1/PAI‑1 by Simple WesternTM.
Simple Western lane view shows lysates of HUVEC human umbilical vein endothelial cells, loaded at 0.2 mg/mL. A specific band was detected for Serpin E1/PAI‑1 at approximately 54 kDa (as indicated) using 2.5 µg/mL of Mouse Anti-Human Serpin E1/PAI‑1 Monoclonal Antibody (Catalog # MAB1786). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 recombinant human PAI‑1 has been observed before for both the recombinant and native proteins (9).
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.
Plasminogen Activator Inhibitor
Entrez Gene IDs:
5054 (Human); 18787 (Mouse)
Endothelial plasminogen activator inhibitor; Nexin; PAI1; PAI-1; PAI1PAI-1; PAISerpin E1; PLANH1; PLANH1plasminogen activator inhibitor 1; serine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogenactivator inhibitor type 1), member 1; Serpin E1; serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitortype 1), member 1
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Breast cancer cells
Other Experimental Details
Other Experimental Details
We used this Serpin E1 neutralizing antibody (400 ng/mL) as part of an antibody cocktail containing several other antibodies to neutralize/block Serpin E1 present in the Conditioned Medium (CM) from BT549 Cells treated with Angiotensin II. CM (+/- Serpin E1 Neutralizing ab Cocktail) was used to further look at Endothelial (HUVEC) Cell migration using Incucyte Chemotaxis Assay