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Hrp rabbit anti mouse igg h l

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The HRP-rabbit anti-mouse IgG (H + L) is a secondary antibody reagent designed for use in various immunoassay techniques. It consists of horseradish peroxidase (HRP) conjugated to rabbit-derived polyclonal antibodies that recognize both the heavy and light chains of mouse immunoglobulin G (IgG).

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Lab products found in correlation

Goat anti rabbit igg h l hrp, by Thermo Fisher Scientific (2 mentions) Elispot plate, by Merck Group (2 mentions) Aec substrate, by BD (2 mentions) Phospho atm ser1981, by Rockland Immunochemicals (1 mentions) Phospho h2ax ser139, by Merck Group (1 mentions) Phospho chk2 thr68, by Cell Signaling Technology (1 mentions) Phospho chk1 ser345, by Cell Signaling Technology (1 mentions) Pan ras, by Santa Cruz Biotechnology (1 mentions) Ab2811, by Abcam (1 mentions) Ha tag clone 3f10, by Roche (1 mentions) A6455, by Thermo Fisher Scientific (1 mentions) Cd138 microbeads, by Miltenyi Biotec (1 mentions)

4 protocols using hrp rabbit anti mouse igg h l

1

Immunoblot Analysis of DNA Damage Proteins

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Immunoblot analysis was carried out as described previously.46, 47 Antibodies specific for the following were used: MCM834; MCM934; Pan‐RAS (sc‐166691; Santa Cruz Biotechnology, Dallas, TX, USA); p53 (OP43; Calbiochem, Dallas, TX, USA); Chk1 (sc‐8408; Santa Cruz Biotechnology); phospho‐Chk1 Ser345 (#2348S; Cell Signaling Technology, Danvers, MA, USA); Chk2 (#05‐649; Upstate, Lake Placid, NY, USA); phospho‐Chk2 Thr68 (#2661; Cell Signaling Technology); phospho‐H2AX Ser139 (#07‐164; Millipore, Burlington, MA, USA); phospho‐ATM Ser1981 (#20772; Rockland, Limerick, PA, USA); and Rad51 (70‐012; Bio Academia, Osaka, Japan). The following secondary Abs were used: HRP‐rabbit anti‐mouse IgG (H + L) (61‐6520; Invitrogen, Carlsbad, CA, USA); HRP‐goat anti‐rabbit IgG (H + L) (65‐6120; Invitrogen); Alexa 594‐conjugated donkey anti‐rabbit IgG (H + L) (A21207; Invitrogen); and Alexa 488‐conjugated goat anti‐mouse IgG (H + L) (A11029; Molecular Probes, Eugene, OR, USA).
Morii I., Iwabuchi Y., Mori S., Suekuni M., Natsume T., Yoshida K., Sugimoto N., Kanemaki M.T, & Fujita M. (2019). Inhibiting the MCM8‐9 complex selectively sensitizes cancer cells to cisplatin and olaparib. Cancer Science, 110(3), 1044-1053.
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2

Immunoblotting of Cell Signaling Proteins

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Immunoblotting was performed as described previously7 (link). Antibodies used in this study were as follows: NUP155 (A303-934A, Bethyl Laboratories), IPOβ (ab2811, Abcam), KNTC1 (F2051-10H4, Sigma-Aldrich), hCAP-D2 (E4161-4C12, Sigma-Aldrich), IPO7 (ab88339, Abcam), CLTC (sc-271178, Santa Cruz), Cdc2-phosphorylated vimentin Ser55 (D076-3, MBL), GST (G7781, Sigma-Aldrich), GFP (A6455, Invitrogen), and HA-tag (clone 3F10, Roche). Secondary antibodies were HRP-rabbit anti-mouse IgG (H + L) (61-6520, Invitrogen) or HRP-goat anti-rabbit IgG (H + L) (65–6120, Invitrogen).
Yokoyama T., Yukuhiro M., Iwasaki Y., Tanaka C., Sankoda K., Fujiwara R., Shibuta A., Higashi T., Motoyama K., Arima H., Yoshida K., Sugimoto N., Morimoto H., Kosako H., Ohshima T, & Fujita M. (2019). Identification of candidate molecular targets of the novel antineoplastic antimitotic NP-10. Scientific Reports, 9, 16825.
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3

FVIII-specific memory B cell differentiation

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Splenocytes from FVIII-immunized HA mice were depleted for CD138+ plasmablasts using CD138 microbeads (Miltenyi Biotec), and the resultant pooled CD138– splenocytes served as the source for FVIII-specific memory B cells (5 (link)–7 (link)). In 48-well culture plates, 6 × 10^6 of CD138– splenocytes were cultured with 40,000 of A2-BAR Tregs or A2-BAR Tcon cells in the presence of 10 ng/ml rFVIII at 37°C for 6 days to promote FVIII-specific memory B cells differentiation into anti-FVIII antibody-secreting cells (ASC). For the B-cell ELISPOT assay, after 6 days the cells were washed twice in culture medium and transferred to 5 μg/ml rFVIII-coated 96-well ELISPOT plates (EMD Millipore) and cultured overnight. The spots indicating FVIII-specific ASCs were visualized through incubation with HRP-rabbit anti-mouse IgG (H + L) (Thermo Fisher Scientific), followed by AEC substrate (BD Biosciences).
Pohl A.D., Venkatesha S.H., Zhang A.H, & Scott D.W. (2020). Suppression of FVIII-Specific Memory B Cells by Chimeric BAR Receptor-Engineered Natural Regulatory T Cells. Frontiers in Immunology, 11, 693.
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4

ELISPOT to Assess FVIII-Specific B Cell Suppression by BAR Tregs

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To measure the FVIII-specific B cell suppression by BAR Tregs in vitro, an Enzyme-Linked ImmunoSpot (ELISPOT) protocol was used (14 (link)). As a model for inhibitor development in HA patients, anti-FVIII antibody response were established in E16 mice by weekly intravenous injection of 1 μg recombinant human FVIII in PBS for 4 weeks in most experiments. Pooled splenocytes (2 × 106) from four FVIII-immunized E16 mice were co-cultured with 1 × 105 of either A2-, C2-, or the control OVA-BAR human Tregs (BAR hTregs) in complete culture media. Two hours after mixing the Tregs and splenocytes to allow for potential interaction of specific B cells with the BARs, human rFVIII protein (0.1 μg/ml) was added and culture was continued for 5 days. The cells were washed twice in culture medium and transferred to 2 μg/ml rFVIII coated 96-well ELISPOT plates (EMD Millipore) and cultured overnight. The number of spots by FVIII-specific antibody secretion B cells (ASCs) was visualized by incubation with second antibody HRP-rabbit anti-mouse IgG (H+L) (ThermoFisher Scientific) followed by AEC substrate (BD Biosciences).
For measuring anti-FVIII total IgG antibody levels, an enzyme-linked immunosorbent assay (ELISA) was used as previously reported (15 (link)).
Zhang A.H., Yoon J., Kim Y.C, & Scott D.W. (2018). Targeting antigen-specific B cells using antigen-expressing transduced regulatory T cells. Journal of immunology (Baltimore, Md. : 1950), 201(5), 1434-1441.
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