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Strepmab classic

Manufactured by IBA Lifesciences
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Sourced in Germany

The StrepMAB-Classic is a lab equipment product designed for the purification and detection of proteins tagged with the Strep-tag II affinity system. It facilitates the efficient capture and recovery of target proteins from complex mixtures.

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Lab products found in correlation

Pvdf p membrane, by Merck Group (2 mentions) Hoechst 33342 dye, by Thermo Fisher Scientific (1 mentions) Rabbit anti mouse horseradish peroxidase conjugate, by Agilent Technologies (1 mentions) Criterion xt precast gel, by Bio-Rad (1 mentions) Uvp chemstudio imager, by Analytik Jena (1 mentions)

Close spelling variants of this product

StrepMAB-Classic HRP-conjugated Ab StrepMAB-Classic HRP conjugate StrepMAB-Classic-HRP

7 protocols using strepmab classic

1

MERS-S2P Fab Binding Assay

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Several 96-Well Half-Area Microplates were coated overnight at 4 °C with 30 μL per well of 2 μg/mL MERS-S2P. After rinsing twice with tap water, the wells were blocked with 5% skim milk in PBS for 1 h at RT. Serially diluted anti-MERS-S2P Sterp-tagged Fabs were added and incubated for 1 h at 37 °C. After washing four times with PBS-T, HRP-conjugated StrepMAB-Classic (1:10,000, IBA Lifesciences) was added to the plates and incubated for 1 h at 37 °C. After washing four times with PBS-T, TMB substrate solution was incubated for 8 min, and the reaction was stopped with 1 N sulfuric acid. Absorbance was measured at 450 nm using a SpectraMax 190 Microplate Reader. A plot was created using a four-parameter curve fit algorithm and half maximal effective concentration (EC50) values were determined accordingly.
Kim Y., Lee H., Park K., Park S., Lim J.H., So M.K., Woo H.M., Ko H., Lee J.M., Lim S.H., Ko B.J., Park Y.S., Choi S.Y., Song D.H., Lee J.Y., Kim S.S, & Kim D.Y. (2019). Selection and Characterization of Monoclonal Antibodies Targeting Middle East Respiratory Syndrome Coronavirus through a Human Synthetic Fab Phage Display Library Panning. Antibodies, 8(3), 42.
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2

Fluorescent Probes and Antibodies for Organelle Imaging

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SnapTag and HaloTag Janelia Fluor dyes were obtained from the Janelia Research Campus (Grimm et al., 2017 (link)). Rabbit monoclonal antibodies against EEA1 and against LAMP1 were from Cell Signaling Technologies (Catalog #: 3288 and 9091; RRID: AB_2096811 and AB_2687579). Mouse monoclonal antibody against Rab7 (Rab7-117) was from Sigma Aldrich (Catalog #: R8779; RRID: AB_609910). Rabbit polyclonal antibody against TGN46 was from Novus Biologicals (Catalog #: NBP1-49643; RRID: AB_10011762). Rabbit monoclonal antibody against GFP was from Abcam (Catalog #: ab32146, RRID: AB_732717). Mouse monoclonal antibody against the Strep tag (StrepMAB-Classic) was from IBA Lifesciences (Catalog #: 2-1507-001; RRID: AB_513133). Hoechst 33342 dye was from Thermo Fisher (Catalog #: H3570). Alexa Fluor 488 goat anti-mouse and goat anti-rabbit antibodies were from Thermo Fisher (Catalog # A32723 and A32731; RRID: AB_2633275 and AB_2633280). HRP-conjugated mouse and rabbit antibodies were from Jackson ImmunoResearch Laboratories Inc (Catalog # 115-035-174 and 111-035-152; RRID AB_2338512 and AB_2337936).
Miller A.N., Houlihan P.R., Matamala E., Cabezas-Bratesco D., Lee G.Y., Cristofori-Armstrong B., Dilan T.L., Sanchez-Martinez S., Matthies D., Yan R., Yu Z., Ren D., Brauchi S.E, & Clapham D.E. (2023). The SARS-CoV-2 accessory protein Orf3a is not an ion channel, but does interact with trafficking proteins. eLife, 12, e84477.
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3

Antibody sources for HCV research

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Mouse Anti-NS5 mAb (S38) and anti-CD81 mAb (2.131) were a gift from Prof. Jane McKeating (University of Oxford). Rabbit Anti-SR-B1 serum was provided by Dr. Thierry Huby (INSERM, Paris). Mouse anti-E2 mAbs J6.36 and H77.39 were a gift from Michael Diamond (Washington University). Human anti-E2 mAbs were kindly provided by Dr. Mansun Law (SCRIPPS, La Jolla) (AR2A, AR3A, AR3C, AR4A, AR5A), Dr. Steven Foung (Stanford) (HC33.1.53, HC84.26, CBH-7, HC1, CBH-4B, CBH-7, CBH-23), and Prof. James Crowe (Vanderbilt University) (HepC3, HepC43). StrepMAB-classic was purchased from IBA Lifesciences (Göttingen, Germany).
Stejskal L., Kalemera M.D., Lewis C.B., Palor M., Walker L., Daviter T., Lees W.D., Moss D.S., Kremyda-Vlachou M., Kozlakidis Z., Gallo G., Bailey D., Rosenberg W., Illingworth C.J., Shepherd A.J, & Grove J. (2022). An entropic safety catch controls hepatitis C virus entry and antibody resistance. eLife, 11, e71854.
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4

Antibody Sources for Hepatitis C Research

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Rabbit anti-SR-B1 polyclonal serum was a gift from Thierry Huby (INSERM, Paris); mouse monoclonals anti-CD81 (2.131) and anti-NS5 (S38) were gifts from Jane McKeating (University of Oxford); StrepMAB-Classic was acquired from IBA lifesciences (Göttingen, Germany); anti-LDLR (2148-LD) was purchased from R&D Systems (Minneapolis, MN, USA).
Kalemera M., Mincheva D., Grove J, & Illingworth C.J. (2019). Building a mechanistic mathematical model of hepatitis C virus entry. PLoS Computational Biology, 15(3), e1006905.
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5

SDS-PAGE and Immunoblotting of Bacillus Toxins

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SDS-PAGE analyses were carried out on a PhastGel gradient (10 to 15%) minigel system (GE Healthcare, Munich, Germany). For Sypro staining, proteins were fixed on the gel for 2 × 30 min in 50% MeOH and 7% acetic acid. The gel was then incubated with 2 mL Sypro Ruby protein stain overnight at room temperature. After 30 min washing in 10% MeOH and 7% acetic acid and additional washing for 10 min in H2O, fluorescence signals were detected on a Kodak imager (Eastman Kodak Company, Rochester, NY, USA).
For immunoblotting, proteins were blotted to a PVDF-P membrane (Millipore, Billerica, MA, USA), blocked in 3% casein-PBS and incubated with 2 μg/mL mAbs 8B12 (Hbl L2) [32 (link)], 1E9 (Hbl L1) [29 (link)], 1B8 (Hbl B) [29 (link)], 1E11 or 2B11 (NheB) [20 (link)], 1A8 (NheA) [20 (link)], 3D6 (NheC) [21 (link)], mAb 1H9 (this study), or the strep-specific StrepMAB-Classic (iba lifesciences) for 1 h at room temperature. After 3 washing steps in PBS with 0.1% Tween 20, a 1:2000 dilution of rabbit anti-mouse-horseradish peroxidase conjugate (Dako) was used as secondary antibody. After three further washing steps in PBS with 0.1% Tween 20 and two in PBS, Super Signal Western Femto Maximum Sensitivity Substrate (Pierce) was applied. Chemiluminescence signals were detected on a Kodak imager (Eastman Kodak).
Tausch F., Dietrich R., Schauer K., Janowski R., Niessing D., Märtlbauer E, & Jessberger N. (2017). Evidence for Complex Formation of the Bacillus cereus Haemolysin BL Components in Solution. Toxins, 9(9), 288.
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6

SARS-CoV-2 Spike Protein Antibody ELISA

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Antibodies to the trimeric spike protein were detected by ELISA. MAXISORP immunoplates (442404; NUNC; Merck, Darmstadt, Germany) were coated with StrepMAB-Classic (2–1507–001; IBA Life Sciences, Göttingen, Germany). Plates were blocked with 2% skimmed milk in phosphate buffered saline (PBS) for 1 h and then incubated with 0.125 μg of soluble SARS-CoV-2 trimeric spike protein or 2% skimmed milk in PBS. After 1 h, plasma was added at 1:50 dilution, followed by alkaline phosphatase (AP)-conjugated anti-human IgG (A9544; Merck, Darmstadt, Germany) at 1:10,000 dilution or AP-conjugated anti-human IgM (A9794; Merck, Darmstadt, Germany) at 1:5,000 dilution. The reaction was developed by the addition of p-nitrophenyl phosphate (PNPP, Merck, Darmstadt, Germany) substrate and stopped with NaOH. The absorbance was measured at 405 nm after 1 h. Further information is provided in Adams et al. [16 (link)].
Thompson C.P., Grayson N.E., Paton R.S., Bolton J.S., Lourenço J., Penman B.S., Lee L.N., Odon V., Mongkolsapaya J., Chinnakannan S., Dejnirattisai W., Edmans M., Fyfe A., Imlach C., Kooblall K., Lim N., Liu C., López-Camacho C., McInally C., McNaughton A.L., Ramamurthy N., Ratcliff J., Supasa P., Sampson O., Wang B., Mentzer A.J., Turner M., Semple M.G., Baillie K., Harvala H., Screaton G.R., Temperton N., Klenerman P., Jarvis L.M., Gupta S., Simmonds P., Baillie J.K., Semple M.G., Openshaw P.J., Carson G., Alex B., Bach B., Barclay W.S., Bogaert D., Chand M., Cooke G.S., Docherty A.B., Dunning J., da Silva Filipe A., Fletcher T., Green C.A., Harrison E.M., Hiscox J.A., Ho A.Y., Horby P.W., Ijaz S., Khoo S., Klenerman P., Law A., Lim W.S., Mentzer A.J., Merson L., Meynert A.M., Noursadeghi M., Moore S.C., Palmarini M., Paxton W.A., Pollakis G., Price N., Rambaut A., Robertson D.L., Russell C.D., Sancho-Shimizu V., Scott J.T., de Silva T., Sigfrid L., Solomon T., Sriskandan S., Stuart D., Summers C., Tedder R.S., Thomson E.C., AA R.T., Thwaites R.S., Turtle L.C., Zambon M., Hardwick H., Donohue C., Lyons R., Griffiths F., Oosthuyzen W., Norman L., Pius R., Drake T.M., Fairfield C.J., Knight S., Mclean K.A., Murphy D., Shaw C.A., Dalton J., Lee J., Plotkin D., Girvan M., Saviciute E., Roberts S., Harrison J., Marsh L., Connor M., Halpin S., Jackson C., Gamble C., Leeming G., Law A., Wham M., Clohisey S., Hendry R., Scott-Brown J., Greenhalf W., Shaw V., McDonald S., Keating S., Ahmed K.A., Armstrong J.A., Ashworth M., Asiimwe I.G., Bakshi S., Barlow S.L., Booth L., Brennan B., Bullock K., Catterall B.W., Clark J.J., Clarke E.A., Cole S., Cooper L., Cox H., Davis C., Dincarslan O., Dunn C., Dyer P., Elliott A., Evans A., Finch L., Fisher L.W., Foster T., Garcia-Dorival I., Greenhalf W., Gunning P., Hartley C., Ho A., Jensen R.L., Jones C.B., Jones T.R., Khandaker S., King K., Kiy R.T., Koukorava C., Lake A., Lant S., Latawiec D., Lavelle-Langham L., Lefteri D., Lett L., Livoti L.A., Mancini M., McDonald S., McEvoy L., McLauchlan J., Metelmann S., Miah N.S., Middleton J., Mitchell J., Moore S.C., Murphy E.G., Penrice-Randal R., Pilgrim J., Prince T., Reynolds W., Ridley P.M., Sales D., Shaw V.E., Shears R.K., Small B., Subramaniam K.S., Szemiel A., Taggart A., Tanianis-Hughes J., Thomas J., Trochu E., van Tonder L., Wilcock E., Zhang J.E., Adeniji K., Agranoff D., Agwuh K., Ail D., Alegria A., Angus B., Ashish A., Atkinson D., Bari S., Barlow G., Barnass S., Barrett N., Bassford C., Baxter D., Beadsworth M., Bernatoniene J., Berridge J., Best N., Bothma P., Brealey D., Brittain-Long R., Bulteel N., Burden T., Burtenshaw A., Caruth V., Chadwick D., Chambler D., Chee N., Child J., Chukkambotla S., Clark T., Collini P., Cosgrove C., Cupitt J., Cutino-Moguel M.T., Dark P., Dawson C., Dervisevic S., Donnison P., Douthwaite S., DuRand I., Dushianthan A., Dyer T., Evans C., Eziefula C., Fegan C., Finn A., Fullerton D., Garg S., Garg S., Garg A., Gkrania-Klotsas E., Godden J., Goldsmith A., Graham C., Hardy E., Hartshorn S., Harvey D., Havalda P., Hawcutt D.B., Hobrok M., Hodgson L., Hormis A., Jacobs M., Jain S., Jennings P., Kaliappan A., Kasipandian V., Kegg S., Kelsey M., Kendall J., Kerrison C., Kerslake I., Koch O., Koduri G., Koshy G., Laha S., Laird S., Larkin S., Leiner T., Lillie P., Limb J., Linnett V., Little J., MacMahon M., MacNaughton E., Mankregod R., Masson H., Matovu E., McCullough K., McEwen R., Meda M., Mills G., Minton J., Mirfenderesky M., Mohandas K., Mok Q., Moon J., Moore E., Morgan P., Morris C., Mortimore K., Moses S., Mpenge M., Mulla R., Murphy M., Nagel M., Nagarajan T., Nelson M., Otahal I., Pais M., Panchatsharam S., Paraiso H., Patel B., Pattison N., Pepperell J., Peters M., Phull M., Pintus S., Pooni J.S., Post F., Price D., Prout R., Rae N., Reschreiter H., Reynolds T., Richardson N., Roberts M., Roberts D., Rose A., Rousseau G., Ryan B., Saluja T., Shah A., Shanmuga P., Sharma A., Shawcross A., Sizer J., Shankar-Hari M., Smith R., Snelson C., Spittle N., Staines N., Stambach T., Stewart R., Subudhi P., Szakmany T., Tatham K., Thomas J., Thompson C., Thompson R., Tridente A., Tupper-Carey D., Twagira M., Ustianowski A., Vallotton N., Vincent-Smith L., Visuvanathan S., Vuylsteke A., Waddy S., Wake R., Walden A., Welters I., Whitehouse T., Whittaker P., Whittington A., Wijesinghe M., Williams M., Wilson L., Wilson S., Winchester S., Wiselka M., Wolverson A., Wooton D.G., Workman A., Yates B, & Young P. (2020). Detection of neutralising antibodies to SARS-CoV-2 to determine population exposure in Scottish blood donors between March and May 2020. Eurosurveillance, 25(42), 2000685.
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7

Western Blot Detection of Hbl B

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For Western blotting, 30 µl protein solution or B. cereus culture supernatant were applied to Criterion XT precast gels (BioRad Laboratories, Feldkirchen, Germany). After electrophoresis, proteins were blotted to a PVDF-P membrane (Millipore; Merck, Darmstadt, Germany). The membrane was saturated with 3% casein-PBS and incubated for 1 h at room temperature with 2 µg/ml Strep-MAB-Classic (IBA Lifesciences, Göttingen, Germany) or monoclonal antibody (mAb) 11A5 [21 (link)] for detection of Hbl B.’ Afterward, it was washed three times in PBS with 0.1% Tween 20 and incubated overnight with a 1:2000 dilution of rabbit anti-mouse-horseradish peroxidase conjugate (Dako; Merck, Darmstadt, Germany) before three further washing steps in PBS with 0.1% Tween 20 and two in PBS. Subsequently, Super Signal Western Femto (Pierce; Thermo Fisher Scientific, Waltham, MA, USA) was applied, and chemiluminescence signals were sensed on a UVP ChemStudio imager (Analytik Jena, Jena, Germany).
Jessberger N., Diedrich R., Janowski R., Niessing D, & Märtlbauer E. (2022). Presence and function of Hbl B’, the fourth protein component encoded by the hbl operon in Bacillus cereus. Virulence, 13(1), 483-501.
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