Anti strep

Manufactured by Qiagen

Sourced in Germany

The Anti-Strep product is a laboratory equipment designed for the detection and identification of Streptococcus bacteria. It provides a reliable method for the analysis of clinical samples to assist in the diagnosis of Streptococcal infections.

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Lab products found in correlation

5 protocols using anti strep

Yeast Mitochondria Isolation and Protein Analysis

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Yeast mitochondria isolation was performed using the method of Glick and Pon (Glick and Pon, 1995 (link)). Standard procedures were performed for SDS-PAGE and immunoblotting. Anti-Sdh2 was from the previous study (Kim et al., 2012 (link)). BN-PAGE was performed as described previously with mitochondrial lysates in 1% digitonin solution (Schilke et al., 1999 (link)). Anti-Strep was purchased from Qiagen. Antibodies against LA-conjugated proteins were from Calbiochem (San Diego, CA). Anti-Myc and anti-HA were from Santa Cruz Biotechnology (Dallas, TX). Anti-Por1 was purchased from Molecular Probes and anti-FLAG was from Sigma-Aldrich.(St. Louis, MO) Protein concentration was determined by the Bradford assay.

Melber A., Na U., Vashisht A., Weiler B.D., Lill R., Wohlschlegel J.A, & Winge D.R. (2016). Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients. eLife, 5, e15991.

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Western Blot Analysis of PfRipr Expression

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Example 1

Samples were taken from the three cell lines at day three of culture and analyzed by western blot to compare PfRipr expression as shown in FIG. 1A. The lane order is as follows: lane 1, SeeBlue Plus2 ladder (Life Technologies); lane 2, sample 1491, cell line WHTZ-04 expressing PfRiprFL only; lane 3, sample 1483, cell line WHTZ-04 expressing PfRiprFL only; lane 4, sample 1320, cell line WHTZG-10 expressing PfRiprFL and PfRh5; lane 5, sample 1482, cell line WHTZGP-13 expressing PfRiprFL and PfRh5 and PfCyrPa. The samples from each cell line were prepared by mixing with buffer and reducing agent and incubation at 95° C. for five minutes. The gel was loaded and run for 35 minutes at 165V and blotted with an iBlott (Life Technologies). The membrane was blotted with anti-Strep (QIAGEN; 34850) and anti-mouse-HRP (DAKO; P0447) as secondary antibody for detection of PfRipr. The blot was then detected by enhanced chemiluminescence. The two samples of WHTZ-04 (from two different productions) show similar expression level. Both WHTZG-10 and WHTZGP-13 show similar expression level and an increased level compared to WHTZ-04. Co-expression of PfRh5 appears to increase the expression of PfRipr. The addition of PfCyrPa does not seem to further increase the expression of PfRipr.

US10940190B2. Malaria vaccine and methods for producing same (2021-03-09). The Walter and Eliza Hall institute of Medical Research [AU], Expres2ion Biotechnologies [DK]. Inventors: Alan Cowman [AU], Julie Healer [AU], Willem Adriaan De Jongh [DK], Teit Max Moscote Sogaard [DK], Thomas Dan Jorgensen [DK], Vladyslav Soroka [DK].

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Cell Culture and Antibody Application

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RAW264.7 (ATCC TIB-71), HEK293T (ATCC-11268), HeLa (ATCC CCL-2), PK-15 (ATCC CCL-33), LFBK (RRID:CVCL_RX26), cells were cultured in Dulbecco’s Modified Eagle Medium (DMEM) (HyClone) supplemented with 10% fetal bovine serum (FBS) (Gibco) and 1% antibiotic/antimycotic (Gibco). Cells were maintained in a humidified 5% CO2 incubator at 37°C. Antibodies used for the immunoblot and immunoprecipitation analysis are as follows, anti-Flag (Cell Signaling, 8146), anti-Strep (Qiagen, 34850), anti-GST (Santa Cruz, sc-138), anti-IRF3 (Abcam, ab25950), anti-phospho IRF3 (Ser396) (Cell Signaling, 4947), anti-p65 (Cell Signaling, 4764S), anti-phospho p65 (Cell Signaling, 3031S), anti-TBK1 (Cell Signaling, 3504S), anti-phospho-TBK1 (Cell Signaling, 5483S), anti-β-actin (Santa Cruz,SC 47778), RIG-I (D14G6; 3743), MDA-5 (D74E4; 5321), Anti-FMDV 2B (homemade), anti-Caspase8 (Cell Signaling, 9746S), anti-Caspase3 (Cell Signaling, 9662S) and anti-β-actin (Santa Cruz,SC 47778)

Weerawardhana A., Uddin M.B., Choi J.H., Pathinayake P., Shin S.H., Chathuranga K., Park J.H, & Lee J.S. (2022). Foot-and-mouth disease virus non-structural protein 2B downregulates the RLR signaling pathway via degradation of RIG-I and MDA5. Frontiers in Immunology, 13, 1020262.

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Antibody Characterization and Validation

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The following antibodies were used: anti-mCherry (Abcam), anti-Pgk1 (Abcam), anti-Kap60 (yD-18) (Santa Cruz Biotechnology), and anti-Strep (QIAGEN).

Mészáros N., Cibulka J., Mendiburo M.J., Romanauska A., Schneider M, & Köhler A. (2015). Nuclear Pore Basket Proteins Are Tethered to the Nuclear Envelope and Can Regulate Membrane Curvature. Developmental Cell, 33(3), 285-298.

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Western Blot Analysis of TRPV3

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Proteins were prepared, denatured, electrophoresed, and blotted onto membranes as described in supplement part B. A primary mouse antibody directed against an epitope (AA 458–474) in the first extracellular loop of hTRPV3 was used at a dilution of 1:3000 (“Anti-TRPV3”; ID: ABIN863127, antibodies-online GmbH, Aachen, Germany). This antibody was previously validated in our group for staining of the bovine homologue of TRPV3 [39 (link)]. For detection of the Strep-tag, a primary mouse antibody (“Anti-Strep”; ID: 34,850, Qiagen, Hilden, Germany) was used at the dilution of 1:2500. After blocking, the membranes were incubated with the primary antibodies (in 2.5% milk in Tris-buffered saline with Tween-20 (0.1 vol%; TBST) supplemented with NaN₃ (0.01%)) overnight (4 °C). Horseradish peroxidase conjugated secondary antibody (anti-mouse, 1:1000 in 2.5% milk in TBST; 45 min; room temperature, Cell Signaling Technology, Frankfurt, Germany) was used to detect the primary antibodies on the membranes. Proteins were visualized by use of the Clarity Western ECL Substrate (Bio-Rad Laboratories GmbH, Munich, Germany).

Liebe H., Liebe F., Sponder G., Hedtrich S, & Stumpff F. (2021). Beyond Ca2+ signalling: the role of TRPV3 in the transport of NH4+. Pflugers Archiv, 473(12), 1859-1884.

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