Ha peroxidase

Manufactured by Merck Group

HA-peroxidase is a laboratory reagent produced by Merck Group. It is an enzyme-conjugated antibody that binds to hyaluronic acid (HA). The core function of HA-peroxidase is to facilitate the detection and quantification of hyaluronic acid in various biological samples through colorimetric or chemiluminescent assays.

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Lab products found in correlation

Flag m2, by Merck Group (2 mentions) Protease inhibitor mixture tablet, by Roche (2 mentions) Iodoacetic acid, by Thermo Fisher Scientific (2 mentions) Anti egfr, by Santa Cruz Biotechnology (2 mentions) Anti phospho egfr, by Cell Signaling Technology (2 mentions) Anti flag m2 peroxidase, by Merck Group (2 mentions) Anti pan akt, by Cell Signaling Technology (2 mentions) Anti pser473 akt, by Cell Signaling Technology (2 mentions) Anti ptp1b fg6, by Merck Group (2 mentions) Pt 66 agarose conjugated beads, by Merck Group (2 mentions) Anti ptp1b pser50 ab62320, by Abcam (2 mentions) Streptavidin hrp, by GE Healthcare (2 mentions) Surfact amps nonidet p 40, by Thermo Fisher Scientific (2 mentions) Zeba desalt spin column, by Thermo Fisher Scientific (2 mentions) Ez link biotin iodoacetyl peg2 biotin iap, by Thermo Fisher Scientific (2 mentions) Biacore sensor nta, by GE Healthcare (2 mentions) Streptavidin chip, by GE Healthcare (2 mentions) Anti ha beads, by Merck Group (2 mentions) Anti flag m2 bead, by Merck Group (2 mentions) Gapdh, by Santa Cruz Biotechnology (2 mentions)

Close spelling variants of this product

Anti-HA-peroxidase (7 citations) Anti-HA peroxidase-conjugated antibody (5 citations) Anti-HA-peroxidase antibody (4 citations) Anti-HA-Peroxidase in APEX assay (2 citations) Mouse anti-HA-peroxidase (2 citations) Peroxidase-conjugated anti-HA (2 citations) Horseradish peroxidase (HRP)-conjugated anti-HA (2 citations)

6 protocols using ha peroxidase

Lentiviral Constructs for KMT1A and p38 Studies

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Lentiviral pLV vector expressing Flag-KMT1A [38 (link)] and LV-HA-MKK6EE and pLV-HA-MKK6DN were generated by subcloning inserts from pcDNA-HA-MKK6EE and pcDNA-HA-MKK6DN (provided by Dr. L. Puri) [39 (link)] into pLV vector. For expression of shRNA, KMT1A, p38α, or scramble shRNAs are cloned individually into lentiviral pLKO.1-TRC vector (Addgene) and sequence verified. The shRNA sequences for KMT1A and scramble were described previously [38 (link)]. The sequence for p38α shRNA was 5′-AGCCCAGCAACCTAGCTGTTT-3′. Vectors pGEX-4T-3-H3(N) [26 (link)] and pGEX-ATF2 (provided by Dr. J. Han) [40 (link)] express GST fusion N-terminal histone H3 and ATF2 proteins, respectively.
Antibodies used were phospho-p38 (Cell Signaling 9215), β-actin-peroxidase (Sigma A3854), Flag-M2 (Sigma F3165), myogenin (BD Pharmingen 556358), KMT1A (Cell Signaling 8729, and Millipore 07-550 and 05-615), MyoD (Santa Cruz sc-760 and BD Pharmingen 554130), p38α (Cell Signaling 9790), HA-peroxidase (Sigma H6533), acetyl-histone H3 (Millipore, 06-599), trimethyl-histone H3 (Lys-9) (Millipore 07-442), trimethyl-histone H3 (Lys27) (Millipore 07-449), GAPDH (Biodesign H86504M), Brg-1 (Santa Cruz sc-10768), p21^cip1 (Santa Cruz sc-397), myosin heavy chain (Developmental Studies Hybridoma Bank, MF-20), total p38 (Cell Signaling 9212), and normal rabbit IgG (Santa Cruz sc-2027).

Chatterjee B., Wolff D.W., Jothi M., Mal M, & Mal A.K. (2016). p38α MAPK disables KMT1A-mediated repression of myogenic differentiation program. Skeletal Muscle, 6, 28.

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Yeast Protein Immunoblotting Reagents

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The following antibodies were from Sigma-Aldrich: glucose-6-phosphate dehydrogenase (G6PDH), HA-peroxidase, and FLAG M2. Antibodies for ubiquitin (P4D1) and VCP/Cdc48 were from Cell Signaling Technology. The antibody for Por1 was from Thermo Fisher Scientific. The GFP antibody was obtained from CWbio.
Yeast extract, peptone, and yeast nitrogen base without amino acids were purchased from BD. Yeast complete supplement mixture was purchased from MP Biomedicals. Yeast amino acid dropout supplements were obtained from Takara Bio Inc. CHX was obtained from Amresco. MG132 was from EMD Millipore. Other chemicals or reagents were obtained from Sigma-Aldrich if not otherwise indicated.

Wu X., Li L, & Jiang H. (2016). Doa1 targets ubiquitinated substrates for mitochondria-associated degradation. The Journal of Cell Biology, 213(1), 49-63.

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Co-Immunoprecipitation of Protein Interactors

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AMOTL1 (HPA001196), Flag (M2), FAT1 (HPA001869) and HA-peroxidase antibodies were obtained from Sigma. Merlin (E-2 and A-19), RNA Pol2 (N-20), SPT16 (H-4), HA (Y-11), MYC (A-14) and anti-goat-HRP (sc-2020) antibodies from Santa Cruz and p21 (05–345) from Millipore. AMOT (303A), CDC73 (170A), CHD1 (218A), CTR9 (395A), DDB1 (462A), LEO1 (175A), Merlin iso1 (A578), Merlin iso2 (A579), PAF1 (172A), PELP1 (180A), RTF1 (179A), YAP (309A), SF3A3 (507A), SF3B1 (997A), SF3B3 (508A), TAT-SF1 (023A), VPRBP (887A and 888A), FAT1 (402A and 403A) antibodies were from Bethyl Laboratories, FLAG-Dylight680 and HA-IRDye800 from rockland. Anti-mouse-HRP (NA 931) and anti-rabbit-HRP (NA934) were obtained from Amersham. cDNAs were cloned into the pENTR vector (Invitrogen) and transferred to Gateway-compatible expression vectors using recombination-mediated Gateway technology (Invitrogen). Mutations were generated using the QuikChange site-directed mutagenesis kit (Stratagene).

Roehrig A.E., Klupsch K., Oses-Prieto J.A., Chaib S., Henderson S., Emmett W., Young L.C., Surinova S., Blees A., Pfeiffer A., Tijani M., Brunk F., Hartig N., Muñoz-Alegre M., Hergovich A., Jennings B.H., Burlingame A.L, & Rodriguez-Viciana P. (2021). Cell-cell adhesion regulates Merlin/NF2 interaction with the PAF complex. PLoS ONE, 16(8), e0254697.

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Quantifying Cellular Proteins and Metabolites

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Antibodies: anti-Myc (Millipore 05-724), β-Actin (Abcam ab8224), HA-peroxidase (Sigma Aldrich 12013819001), V5 (Thermo Fisher Scientific R960-25), GST (Santa Cruz sc-459), Rpb1 (BioLegend 664906). Metabolite assays were carried out using a Bridge-It® SAM fluorescence assay (Mediomics 1-1-1003B), or a Bridge-It® l-Methionine (L-Met) Fluorescence Assay (Mediomics 1-1-1005B).

Church M.C., Price A., Li H, & Workman J.L. (2023). The Swi-Snf chromatin remodeling complex mediates gene repression through metabolic control. Nucleic Acids Research, 51(19), 10278-10291.

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Protein Interaction and Modification Analysis

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Anti-EGFR, GAPDH and 14-3-3ζ were from Santa Cruz Biotechnology. Anti-Pan-AKT, anti-AKT pSer⁴⁷³, anti phosphoEGFR antibodies were from Cell Signaling Technology. HA-peroxidase and anti-PTP1B (FG6) was from Millipore. PT-66-agarose-conjugated beads, anti-FLAG M2 beads, and anti-HA beads and anti-Flag M2 peroxidase were purchased from Sigma. Anti-PTP1B pSer⁵⁰ (Ab62320) were from Abcam. Streptavidin-HRP was from GE Healthcare. HRP-conjugated secondary antibodies were from Jackson ImmunoResearch Laboratories, Inc. Protease inhibitor mixture tablets were from Roche. Catalase and superoxide dismutase were from Calbiochem. Surfact-Amps Nonidet P-40, zeba desalt spin columns, EZ-Link biotin-iodoacetyl-PEG2 (biotin-IAP), and iodoacetic acid were from ThermoScientific. The pTyr loop-derived peptide (CKNRNRYRDVS) and phospho-Ser⁵⁰ pTyr loop-derived peptide (CKNRNRYRDVpS) were from GenScript USA Inc. BIACore sensor NTA and Streptavidin chips were from GE healthcare.

Londhe A.D., Bergeron A., Curley S.M., Zhang F., Rivera K.D., Kannan A., Coulis G., Rizvi S.H., Kim S.J., Pappin D.J., Tonks N.K., Linhardt R.J, & Boivin B. (2019). Regulation of PTP1B activation through disruption of redox-complex formation. Nature chemical biology, 16(2), 122-125.

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Protein Interaction and Modification Analysis

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