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Serpine1

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SerpinE1 is a serine protease inhibitor that regulates the activity of plasminogen activators. It functions as a key regulator of the plasminogen activation system, which is involved in various physiological and pathological processes.

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Lab products found in correlation

Pai 1, by Abcam (2 mentions) Thbs1, by LifeSpan BioSciences (2 mentions) Timp 1, by R&D Systems (2 mentions) Enhanced chemiluminescence reagent, by GE Healthcare (1 mentions) β actin, by GE Healthcare (1 mentions) Serpinb2, by Abcam (1 mentions) Phospho c jun, by Santa Cruz Biotechnology (1 mentions) Hrp conjugated secondary antibody, by Santa Cruz Biotechnology (1 mentions) C jun, by Santa Cruz Biotechnology (1 mentions) β actin, by Merck Group (1 mentions) Anti src, by Abcam (1 mentions) Anti ctcf, by Abcam (1 mentions) Anti ctbp1, by Abcam (1 mentions) Axio imager m1 microscope, by Zeiss (1 mentions) Alexa flour 488, by Abcam (1 mentions) 4 6 diamidino 2 phenylindole dapi solution, by Thermo Fisher Scientific (1 mentions) Alexa flour 555, by Abcam (1 mentions) Col18a1, by Thermo Fisher Scientific (1 mentions) Pecam 1, by Santa Cruz Biotechnology (1 mentions) Gapdh, by Yeasen (1 mentions)

7 protocols using serpine1

1

Plasma Protein Quantification by ELISA

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Platelet poor plasma from each treatment group was analyzed by ELISA according to the manufacturer’s instructions. Thbs1 was from LifeSpan Biosciences, SerpinE1 (PAI-1) was from Abcam, uPA was from Innovative Research, and Timp1 was from R&D Systems. Plasma samples were diluted with Assay Buffers before analysis (Thbs1 = 1:5 dilution, PAI-1 = 1:5 dilution, uPA = 1:2 dilution, Timp1 = 1:2 dilution). Thrombopoeitin (Tpo) was measured by ELISA (R&D Systems) on undiluted EDTA-treated plasma according to the manufacturer’s instructions.
Wiley C.D., Liu S., Limbad C., Zawadzka A.M., Beck J., Demaria M., Artwood R., Alimirah F., Lopez-Dominguez J.A., Kuehnemann C., Danielson S.R., Basisty N., Kasler H.G., Oron T.R., Desprez P.Y., Mooney S.D., Gibson B.W., Schilling B., Campisi J, & Kapahi P. (2019). SILAC Analysis Reveals Increased Secretion of Hemostasis-Related Factors by Senescent Cells. Cell reports, 28(13), 3329-3337.e5.
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2

Plasma Protein Quantification by ELISA

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Platelet poor plasma from each treatment group was analyzed by ELISA according to the manufacturer’s instructions. Thbs1 was from LifeSpan Biosciences, SerpinE1 (PAI-1) was from Abcam, uPA was from Innovative Research, and Timp1 was from R&D Systems. Plasma samples were diluted with Assay Buffers before analysis (Thbs1 = 1:5 dilution, PAI-1 = 1:5 dilution, uPA = 1:2 dilution, Timp1 = 1:2 dilution). Thrombopoeitin (Tpo) was measured by ELISA (R&D Systems) on undiluted EDTA-treated plasma according to the manufacturer’s instructions.
Wiley C.D., Liu S., Limbad C., Zawadzka A.M., Beck J., Demaria M., Artwood R., Alimirah F., Lopez-Dominguez J.A., Kuehnemann C., Danielson S.R., Basisty N., Kasler H.G., Oron T.R., Desprez P.Y., Mooney S.D., Gibson B.W., Schilling B., Campisi J, & Kapahi P. (2019). SILAC Analysis Reveals Increased Secretion of Hemostasis-Related Factors by Senescent Cells. Cell reports, 28(13), 3329-3337.e5.
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3

Western Blot Analysis of Protease Inhibitors

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Proteins from cells lysed in RIPA buffer were separated using SDS-PAGE and transferred to nitrocellulose membranes. Membranes were blocked using 5% skim milk in Tris-buffered saline containing Tween-20, incubated overnight at 4°C with primary antibodies directed against SerpinB2 (Abcam, Cambridge, UK), SerpinE1 (Abcam), uPA (Abcam), c-Jun (Santa Cruz Biotechnology, Santa Cruz, CA, USA) or phospho-c-Jun (Santa Cruz Biotechnology), and β-actin (Sigma-Aldrich, St. Louis, MA, USA), and then incubated with HRP-conjugated secondary antibodies (Santa Cruz Biotechnology). Blotted membranes were visualized using enhanced chemiluminescence reagents (GE Healthcare, Piscataway, NJ, USA) and protein expression was depicted as intensity of each protein relative to that of β-actin using ImageJ software.
Jin T., Kim H.S., Choi S.K., Hwang E.H., Woo J., Ryu H.S., Kim K., Moon A, & Moon W.K. (2017). microRNA-200c/141 upregulates SerpinB2 to promote breast cancer cell metastasis and reduce patient survival. Oncotarget, 8(20), 32769-32782.
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4

Immunohistochemical Analysis of Protein Markers

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Paraffin-embedded tissue sections were de-paraffinized with xylene, graded ethanol and ddH2O. Antigen retrieval was achieved by incubating the specimens with boiled citrate buffer (10 mM, pH 6.0) for 15 minutes. The tissue sections were subsequently exposed to 3% hydrogen peroxide for 10 minutes to inhibit endogenous peroxidase activity. After blocking with goat serum for 20 minutes at room temperature, the sections were incubated at 4°C overnight with the following primary antibodies: anti-CTCF (Abcam, Cambridge, UK), anti-Ki-67 (Bioss Antibodies Inc., Woburn, MA, USA), anti-SRC (Abcam), anti-CTBP1 (Abcam), and SERPINE1 (Abcam). Then, the sections were incubated with HRP-labeled secondary antibodies at 37°C for 20 minutes and visualized with the DAB detection kit following the manufacturer’s instructions. The negative control samples were incubated with PBS in the absence of primary antibodies. The images were recorded with MCID, and the expression of positive cells was scored as previously described [30 (link)]. Briefly, each sample was assigned an intensity score (0-3) and a percentage of positive cells score (0=0%, 1=1-19%, 2=20-79%, 3=80-100%). An overall IHC score was calculated by multiplying the intensity score and the percentage value of positive cells.
Zhao L., Yang Y., Yin S., Yang T., Luo J., Xie R., Long H., Jiang L, & Zhu B. (2017). CTCF promotes epithelial ovarian cancer metastasis by broadly controlling the expression of metastasis-associated genes. Oncotarget, 8(37), 62217-62230.
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5

Immunofluorescence Analysis of Pancreatic Tissue

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Cells were fixed with 4% FA solutions and paraffin-embedded pancreatic tissues were deparaffinized. Fixed cells and tissues were permeabilized with Triton X-100, sequentially incubated with blocking solution and primary antibodies, including Col18a1 (Invitrogen™), Serpin E1, CD68 (Abcam Plc.), NG2 (Sigma-Aldrich), PECAM-1 (Santa Cruz Biotechnology, Inc.), and MPO (Agilent Technologies, lnc., Santa Clara, CA, USA), at 4 °C overnight, and further incubated with secondary antibodies conjugated with Alexa Flour® 488 or Alexa Flour® 555 (Abcam Plc.). DAPI (4’,6-diamidino-2-phenylindole) solution (Invitrogen™) was used to stain the nuclei. Fluorescence signals were observed and imaged using the ZEISS Axio Imager M1 microscope (Carl Zeiss, Oberkochen, Germany).
Jung M., Ryu S., Kim C., Cha S., Kang H., Ji E., Hong Y., Lee Y., Han S., Jeong S.M., Kim W, & Lee E.K. (2022). RNA binding protein HuD mediates the crosstalk between β cells and islet endothelial cells by the regulation of Endostatin and Serpin E1 expression. Cell Death & Disease, 13(12), 1019.
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6

Western Blot Analysis of Protein Expression

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Tissues or cells were lysed on ice with precooled lysis buffer for 30 min and centrifuged at 12 000 rpm for 10 min at 4 ℃. The supernatant was transferred to centrifuge tubes, and 5 × SDS loading buffer was added. Samples were denatured for 10 min at 99 ℃ and subjected to sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and transferred onto a polyvinylidene fluoride membrane (Merck). The membrane was blocked with 5% BSA for 60 min at room temperature and incubated with the primary antibodies against Serpine1 (1:1000; Abcam), Nr4a1 (1:1000, Abcam), β-actin (1:1500, Yeasen), Gapdh (1:1500, Yeasen), and transferrin (1:1000, Beyotime) overnight at 4 ℃. After washing three times with 1 × TBST, the membrane was probed with the HRP-linked goat anti-rabbit secondary antibody (1:1000, Yeasen) for 60 min at room temperature and washed with 1 × TBST buffer. Proteins were visualized using electrogenerated chemiluminescence reagents (Epizyme) and detected with an ImageQuant LAS 4000 chemiluminescent Image Analyzer (General Electric). The relative densitometric density of the target band to the internal reference band was analysed using the ImageJ software.
Yao D., Zhao J., Zhang Q., Wang T., Ni M., Qi S., Shen Q., Li W., Li B., Ding X, & Liu Z. (2022). Aberrant methylation of Serpine1 mediates lung injury in neonatal mice prenatally exposed to intrauterine inflammation. Cell & Bioscience, 12, 164.
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7

Urinary Biomarkers for Diagnostic Evaluation

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Levels of human Interleukin 8 (IL8, Cat # ab46032 Abcam), Matrix Metalloproteinase 9 (MMP9, Cat # DMP900 R&D Systems Inc.), Plasminogen Activator Inhibitor 1 (SERPINA1, Cat # EA-0207 Signosis Inc.), Vascular Endothelial Growth Factor A (VEGFA, Cat # 100663 Abcam), Angiogenin (ANG, Cat # CK400 CellSciences), Carbonic Anhydrase 9 (CA9, Cat # DCA900 R&D Systems Inc.), Matrix Metalloproteinase 10 (MMP10, Cat # DMP1000 R&D Systems Inc.), human Apolipoprotein E (APOE, Cat # KA 1031 Abnova), human Syndecan (SDC1, Cat # ab46507 Abcam) and human A1AT (SERPINE1, Cat # ab108799, Abcam) were monitored in urine samples using commercial enzyme-linked immunosorbent assays (ELISA) as listed above. Frozen supernatants were thawed and the ELISA’s were conducted according to the manufacturer’s instructions. Calibration curves were prepared using purified standards for each protein assessed. Curve fitting was accomplished by either linear or four-parameter logistic regression following the manufacturer’s instructions. Due to the unavoidable variability of voided urine with respect to total volume and time within the bladder, biomarkers were normalized to urinary creatinine and to urinary protein for comparison [24 (link)]. Laboratory personnel were blinded to final diagnosis.
Chen L.M., Chang M., Dai Y., Chai K.X., Dyrskjøt L., Sanchez-Carbayo M., Szarvas T., Zwarthoff E.C., Lokeshwar V., Jeronimo C., Parker A.S., Ross S., Borre M., Ørntoft T.F., Jaeger T., Beukers W., Lopez L.E., Henrique R., Young P.R., Urquidi V., Goodison S, & Rosser C.J. (2014). External Validation of a Multiplex Urinary Protein Panel for the Detection of Bladder Cancer in a Multicenter Cohort. Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology, 23(9), 1804-1812.
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