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Goat anti mouse igg h l hrp

Manufactured by Jackson ImmunoResearch
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Sourced in United States, United Kingdom

Goat anti-mouse IgG (H+L)-HRP is a secondary antibody conjugated with horseradish peroxidase (HRP). It is designed to detect and bind to mouse immunoglobulin G (IgG) antibodies, recognizing both the heavy (H) and light (L) chains.

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Lab products found in correlation

Goat anti rabbit igg h l hrp, by Jackson ImmunoResearch (2 mentions) Alliance 2695, by Waters Corporation (1 mentions) Flat bottom microtitration plates, by Corning (1 mentions) Ab2171, by Abcam (1 mentions) Ab226346, by Abcam (1 mentions) P egfr, by Cell Signaling Technology (1 mentions) P stat3, by Cell Signaling Technology (1 mentions) Stat3, by Cell Signaling Technology (1 mentions) Mouse anti α tubulin t5168, by Merck Group (1 mentions) Alexa 647 goat anti mouse igg, by Thermo Fisher Scientific (1 mentions) Goat anti rabbit igg alexa 568, by Thermo Fisher Scientific (1 mentions) Goat anti mouse igg dylight488, by Jackson ImmunoResearch (1 mentions) Rabbit anti cleaved caspase 3, by Cell Signaling Technology (1 mentions) Elisa plate, by Thermo Fisher Scientific (1 mentions) Tmb substrate, by Thermo Fisher Scientific (1 mentions) Anti p53 antibody, by Proteintech (1 mentions) Anti timp1 antibody, by Santa Cruz Biotechnology (1 mentions) Anti caspase 3 antibody, by Proteintech (1 mentions) Ecl assay kit, by Beyotime (1 mentions) Anti α sma antibody, by Proteintech (1 mentions)

Close spelling variants of this product

Goat anti-mouse HRP (99 citations) Goat anti-mouse IgG (H+L) (36 citations) HRP-conjugated goat anti-mouse IgG (H + L) (17 citations) HRP anti-mouse (5 citations) HRP-labeled goat anti-mouse IgG (H + L) (3 citations) HRP-conjugated goat anti-mouse or goat anti-human IgG (H+L) (2 citations) HRP‐labelled goat anti‐mouse IgG (H&L) (2 citations) Goat anti-mouse IgG (H+L)-horseradish peroxidase (HRP) (2 citations) HRP-conjugated goat anti-mouse IgG (H + L) antibody (2 citations) Goat anti Rabbit IgG (H+L)-HRP conjugate and Goat anti Mouse IgG (H+L)-HRP conjugate (2 citations)

8 protocols using goat anti mouse igg h l hrp

1

Isolation and Purification of N. atra Toxins

Cited 2 times
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Lyophilized N. atra venom was purchased from Latoxan (Portes-lès-Valence, France). Toxins, including cytotoxin A3 (CTX A3) and short-chain neurotoxin (sNTX), were isolated from the venom of N. atra (Taiwan) using a high-performance liquid chromatography (HPLC) system (Alliance 2695; Waters, Milford, MA, USA) equipped with a dual absorbance ultraviolet light described in a previous study [31 (link)]. Mouse serum anti-CTX A3 and anti-sNTX were raised against the corresponding purified toxins [31 (link)]. The horse anti-N. atra F(ab’)2 was obtained from the Centers for Disease Control (CDC), Taiwan. The horse and rabbit polyclonal antibody was affinity-purified using a Taiwan cobra venom-immobilized column prepared as described in our previous study [51 (link)]. Goat anti-horse IgG (H+L)-HRP and goat anti-mouse IgG (H+L)-HRP, the secondary antibodies, were purchased from Jackson ImmunoResearch Inc. (West Grove, PA, USA). The flat-bottom microtitration plates and the TMB substrate were obtained from Corning Inc. (Corning, NY, USA) and SeraCare Life Science Inc. (Milford, MA, USA), respectively. All other chemicals used in this study were analytical grade and purchased from Sigma-Aldrich (St. Louis, MO, USA).
Lin J.H., Sung W.C., Mu H.W, & Hung D.Z. (2022). Local Cytotoxic Effects in Cobra Envenoming: A Pilot Study. Toxins, 14(2), 122.
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2

Western Blotting Analysis of Cell Signaling

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Western blotting analysis was performed as previously described (14 (link)). Proteins were isolated using the RIPA method. After adjusting the protein concentration, the proteins were separated by SDS-polyacrylamide gel electrophoresis (PAGE) and transferred to polyvinylidene difluoride membranes using an eBLOT system. The membranes were incubated with primary antibodies diluted in TBS with 5% skimmed milk powder. The primary antibodiecs p53 (2524, Cell Signaling Technology, Danvers, MA, USA), caspase 3 (ab2171, Abcam, Cambridge, UK), Stat3 (12640, Cell Signaling Technology), p-Stat3 (9145, Cell Signaling Technology), EGFR (2232, Cell Signaling Technology), p-EGFR (3777, Cell Signaling Technology), and GP130 (ab226346, Abcam) and second antibodies Goat anti-rabbit IgG(H+L), HRP (Jackson ImmunoResearch, Cat. No.111035003), Goat anti-mouse IgG(H+L), HRP (Jackson ImmunoResearch, Cat. No.115035003) were used. The membranes were developed using ECL for 3–5 min.
Zhang Y., Zhang Y., Shi X.J., Li J.X., Wang L.H., Xie C.E, & Wang Y.L. (2022). Chenodeoxycholic Acid Enhances the Effect of Sorafenib in Inhibiting HepG2 Cell Growth Through EGFR/Stat3 Pathway. Frontiers in Oncology, 12, 836333.
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3

Western Blot Antibody Evaluation

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The following primary antibodies were used for western blotting: Mouse monoclonal to GAPDH diluted 1:2000, purchased from Proteintech (#60004-1-Ig), Mouse monoclonal [236A/E7] to FOXP3 from Abcam (1:1000) and Goat Anti-Mouse IgG (H+L)-HRP diluted 1:3000 (Jackson ImmunoResearch #115-035-003).
Forstnerič V., Oven I., Ogorevc J., Lainšček D., Praznik A., Lebar T., Jerala R, & Horvat S. (2019). CRISPRa-mediated FOXP3 gene upregulation in mammalian cells. Cell & Bioscience, 9, 93.
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4

SARS-CoV-2 RBD Antibody Binding Assay

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ELISA plates were coated with SARS-CoV-2 RBD with His6 tag at 0.02 μg/mL in carbonate buffer solution at 4°C overnight. After washing and blocking with 5% milk, antiserums diluted in 5% milk was added to each well. After incubation at 37°C for 4 h, plates were washed and incubated with goat anti-mouse IgG (H+L)/HRP (Jackson lab) for 2 h. After washing, TMB solution was added to the plates and incubated at 37°C for 20 min. Then the same volume 1.0 M H2SO4 was added to stop the reaction. Absorbance at 450 nm was measured by a microplate reader (synergy neo2).
Liu Z., Yang C., Zhang H., Cao G., Wang S., Yin S, & Wang Y. (2022). SARS-CoV-2 tetrameric RBD protein blocks viral infection and induces potent neutralizing antibody response. Frontiers in Immunology, 13, 960094.
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5

Immunohistochemical Staining of Ly6A

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Anti-Sca-1/Ly6A/E antibody (Abcam, Cambridge, UK) with a 1:100 dilution and goat anti-mouse IgG (H+L)-HRP (Jackson ImmunoResearch) with a 1:500 dilution were used as primary antibody and secondary antibody, respectively. The staining procedure was carried out according to the manufacturer's instructions (Abcam).
Hao Y.H., Liu Z.Z., Zhao H., Wang L., Khan A., Mu J.B., Wang Y.F., Yang L.H., Zhou R, & Xie J. (2021). Identification and characterization of murine adipose tissue-derived somatic stem cells of Shenque (CV8) acupoint. Chinese Medical Journal, 134(22), 2730-2737.
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6

Antibody-based Detection of Apoptosis and Viral Proteins

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The following antibodies and reagents were used in this study, rabbit anti-cleaved
caspase-3 (#9661) was purchased from Cell Signaling Technology (Danvers, MA, U.S.A.),
mouse anti-α-tubulin (T5168) from Sigma-Aldrich (St. Louis, MO, U.S.A.), and goat
anti-rabbit IgG (H+L)-HRP, goat anti-mouse IgG (H+L)-HRP, and goat anti-mouse IgG-DyLight
488 from Jackson ImmunoResearch (West Grove, PA, U.S.A.). Goat anti-rabbit IgG-Alexa 488,
goat anti-rabbit IgG-Alexa 568, goat anti-mouse IgG-Alexa 647 was purchased from Thermo
Fisher Scientific (Waltham, MA, U.S.A.), and mouse anti-IBAV antiserum was generated in
our laboratory by intraperitoneal injection of ddY mice with 50–100 µg
purified IBAV particles/mouse along with Freund’s complete adjuvant (first injection) or
Freund’s incomplete adjuvant (second and third injections). IBAV purification was
performed as detailed in a previous study [11 (link)].
TSURUTA Y., SHIBUTANI S., WATANABE R, & IWATA H. (2018). Apoptosis induced by Ibaraki virus does not affect virus replication and cell death in hamster lung HmLu-1 cells. The Journal of Veterinary Medical Science, 81(2), 197-203.
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7

Anti-LMB-100 Antibody Titer Quantification

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Anti–LMB-100 titers were measured as previously described [12 (link)]. In brief, ELISA plates (Thermo Fisher) were coated with 100 μl of LMB-100 (91 μg/ml). Plates were blocked with 3% BSA and serial dilutions of plasma were incubated for 1 h. Anti-LMB-100 antibodies were detected with goat anti-mouse IgG (H+L) HRP (Jackson ImmunoResearch) (1:3000) and TMB substrate (Thermo Fisher). Optical density of the wells was read immediately after the addition of H2SO4 stop solution, at a wavelength of 450 nm with subtraction at 650 nm. Titers were calculated based on a four-parameter logistic curve-fit graph and interpolated on the half maximal value of the anti–LMB-100 (IP12) [13 (link)] (BioXcell, custom lot).
Mazor R., King E, & Pastan I. (2018). Anti-drug antibodies to LMB-100 are enhanced by mAbs targeting OX40 and CTLA4 but not by mAbs targeting PD1 or PDL-1. Cellular immunology, 334, 38-41.
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8

Quantitative Western Blot Analysis

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The total protein of the cells with different treatments was extracted using RIPA lysis buffer, and a BCA protein assay kit was used to measure the total protein concentrations. After that, the protein samples (20 μg) were separated by 10% SDS-PAGE and transferred onto polyvinylidene difluoride membranes. After blocking with 5% skim milk at 37°C for 2 h, the membranes were incubated with anti-Axl antibody (1:1,000; Protein Tech Group, Inc.), anti-α-SMA antibody (1:1,000; Protein Tech Group, Inc.), anti-MMP3 antibody (1:1,000; Protein Tech Group, Inc.), anti-STAT4 antibody (1:1,000; Protein Tech Group, Inc.), anti-TIMP1 antibody (1:200; Santa Cruz, Inc.), anti-p53 antibody (1:2,000; Protein Tech Group, Inc.), anti- Caspase3 antibody (1:1,000; Protein Tech Group, Inc.), and anti-GAPDH antibody (1:10,000; Protein Tech Group, Inc.) at 4°C overnight. On the next day, the secondary antibody (goat anti-mouse IgG (H + L)-HRP [1:10,000; Jackson ImmunoResearch Laboratories, Inc.]) was added, and cells were incubated at 37°C for 2 h. Finally, the membrane was visualized using an ECL assay kit (Beyotime Institute of Biotechnology), and the protein expression levels of the related proteins were quantified using Image-Pro Plus software.
Shu J., Shi J., Gu Y., Deng L., Zhao C., Wu C., Zhao J., Wang H, & Jin L. (2023). Levocarnitine regulates the growth of angiotensin II-induced myocardial fibrosis cells via TIMP-1. Open Life Sciences, 18(1), 20220554.
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