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Horseradish peroxidase conjugated antimouse and antirabbit secondary antibodies

Manufactured by GE Healthcare
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Horseradish peroxidase conjugated antimouse and antirabbit secondary antibodies are laboratory reagents used for the detection and quantification of target proteins in various immunoassays. These antibodies are designed to bind to primary antibodies raised against mouse or rabbit antigens, enabling the visualization of the target proteins through the enzymatic activity of the conjugated horseradish peroxidase.

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Lab products found in correlation

Ab108337, by Abcam (1 mentions) Occludin, by Santa Cruz Biotechnology (1 mentions) N cadherin, by Santa Cruz Biotechnology (1 mentions) Phospho foxo1, by Cell Signaling Technology (1 mentions) Gapdh, by Merck Group (1 mentions) Enhanced chemiluminescence detection reagent, by GE Healthcare (1 mentions) Sb203580, by Merck Group (1 mentions)

Close spelling variants of this product

Secondary horseradish peroxidase antibodies Secondary horseradish-conjugated antibodies Horseradish peroxidase

3 protocols using horseradish peroxidase conjugated antimouse and antirabbit secondary antibodies

1

Endothelin-1 Signaling Pathway Regulation

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Human recombinant ET‐11 (E7764), anti‐ET‐1 antibody1 (mouse monoclonal; E166), and anti‐ETAR antibody1 (rabbit polyclonal; E3651) were purchased from Sigma‐Aldrich. Atrasentan hydrochloride2 (ABT‐627) was purchased from MedchemExpress. Phosphatidylinositol‐specific phospholipase C3 (P‐6466) was purchased from Life Technologies. Anti‐phosphorylated c‐jun antibody4 (rabbit monoclonal, 3270), anti‐c‐jun antibody4 (rabbit monoclonal, 9165), and anti‐c‐fos antibody4 (rabbit monoclonal; 2250) were purchased from Cell Signaling Technology. Horseradish peroxidase conjugated antimouse and antirabbit secondary antibodies were purchased from GE Healthcare, UK. Anti‐β actin antibody5 (mouse monoclonal; AC‐15) and anti‐ALP antibody5 (mouse monoclonal; ab108337) were purchased from Abcam.
Neumann Z.L., Pondenis H.C., Masyr A., Byrum M.L., Wycislo K.L, & Fan T.M. (2015). The Association of Endothelin‐1 Signaling with Bone Alkaline Phosphatase Expression and Protumorigenic Activities in Canine Osteosarcoma. Journal of Veterinary Internal Medicine, 29(6), 1584-1594.
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2

Western Blot Antibody Validation

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Antibodies used for Western blotting are as follows: phospho-Akt (4051S
and 4056S), total Akt (9272S), and phospho-FOXO1 (9461S; Cell Signaling
Technology), total FOXO1 (Santa Cruz Biotechnology; sc-11350), CD44 (R&D
Systems; BBA10), HAS2 (Santa Cruz Biotechnology; sc-365263), GAPDH (Millipore;
MAB374), N-cadherin (BD 610920), and occludin (Santa Cruz Biotechnology;
sc-5562). Horseradish peroxidase–conjugated anti-mouse and anti-rabbit
secondary antibodies were obtained from GE Healthcare. Blocking antibodies used
for HA-CD44 binding experiments are as follows: Anti-human CD44 Clone 515
(BD550988), anti-mouse CD44 antibody KM81 (AB112178), anti-human CD44
(R&D Systems BBA10), and anti-human/mouse CD44 antibody IM7 (BioXcell
BE0039).
Liu S, & Cheng C. (2017). Akt Signaling Is Sustained by a CD44 Splice Isoform–Mediated Positive Feedback Loop. Cancer research, 77(14), 3791-3801.
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3

Western Blot Analysis of p38 Signaling

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Western blotting was performed on cell homogenates, as previously described (36 (link), 37 (link)) using Cell Signaling Technology (New England BioLabs, Ipswich, MA, USA) antibodies for p38α (9228), phospho-p38 (9211), and phospho-HSP27 (2401). Horseradish peroxidase–conjugated anti-mouse and anti-rabbit secondary antibodies and enhanced chemiluminescence detection reagent were from GE Healthcare Life Sciences (Little Chalfont St. Giles, United Kingdom). mAb β-actin (ab8226) from Abcam (Cambridge, United Kingdom) was used as a loading control. The p38 inhibitor SB203580 (Merck, Kenilworth, NJ, USA) was used to evaluate the importance of p38α in mediating DAMP-induced changes in hypertrophic gene expression.
Bageghni S.A., Hemmings K.E., Zava N., Denton C.P., Porter K.E., Ainscough J.F., Drinkhill M.J, & Turner N.A. (2018). Cardiac fibroblast-specific p38α MAP kinase promotes cardiac hypertrophy via a putative paracrine interleukin-6 signaling mechanism. The FASEB Journal, 32(9), 4941-4954.
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