H3 | Histone H3 (rabbit antibody) (nuclear marker)

Product no: AS10 710

AS10 710 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, C. reinhardtii, H. vulgare, S. lycopersicum, V. faba, P. patens, S. europaea, Z. mays | cellular [compartment marker] of nucleoplasm

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  • Product Info
  • Immunogen:

    KLH-conjugated synthetic peptide derived from known H3 sequences, inluding Arabidopsis thaliana H3.3 P59169 (At4g40030, At4g40040, At5g10980), H3.2 P59226 (At1g09200, At3g27360, At5g10390, At5g10400, At5g65360), H3-like 2 Q9FXI7 (At1g19890)

    Host: Rabbit
    Clonality: Polyclonal
    Purity: Serum
    Format: Lyophilized
    Quantity: 50 µl
    Reconstitution: For reconstitution add 50 µl of sterile water
    Storage: Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
    Tested applications: ChIp-qPCR (ChIp-qPCR), Immunocytochemistry (ICC), Immunofluorescence (IF), Western blot (WB)
    Recommended dilution: 1 : 100-1 : 500 (ICC), 2 µl of antibody/500 µl solution (ChIp-qPCR), 1: 500 (IF),  1 : 5000 (WB)
    Expected | apparent MW:

    15 | 17 kDa

  • Reactivity
  • Confirmed reactivity: Arabidopsis thaliana, Brassica oleracea, Capsicum annuum, Cicer arietinum L., Chlamydomonas acidophila, Chlamydomonas reinhardtii, Cucumis sativus L cv Suyo, Cucurbita pepo L. var. cylindrica, Hordeum vulgare, human, Nicotiana benthamiana, Phalaenopsis equestris, Physcomitrium patens, Salicornia europaea, Solanum lycopersicum, Solanum sogarandinum, Solanum tuberosum, Vicia faba, Zea mays
    Predicted reactivity:

    Brachypodium distachyon, Brassica napus, Emiliania huxleyi, Glycine max, Nannochloropsis gaditana, Nicotiana tabacum, Malus domestica, Medicago sativa, Oryza sativa, Ostreococcus sp. , Pinus pinaster, Pisum sativum, Porphyridium purpureum, Sorghum bicolor, Triticum aestivum, Vitis vinifera, Volvox sp.


    Species of your interest not listed? Contact us
    Not reactive in: No confirmed exceptions from predicted reactivity are currently known
  • Application Examples
  • Application example

     Histone H3 plant antibody western blot example

    1.2 μg of Arabidopsis thaliana chromatin-enriched fraction (1) and 3.75 µg of total protein from 4-weeks-old Arabidopsis thaliana leaves (2), and were separated on 12% SDS-PAGE and blotted 50 mins to Immobilon-P (Millipore, semi-dry) PVDF membrane. Blots were blocked immediately following transfer in MTBS-T (5% milk) for 30 mins at room temperature with agitation. Blots were incubated in the primary antibody at a dilution of 1:5000 for 1h at room temperature with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed 3 times for 3 min in TBS-T at room temperature with agitation. Blots were incubated in secondary antibody (anti- IgG horse radish peroxidase conjugated, from Agrisera, AS09 602) diluted to 1:20 000 for 30 mins at room temperature with agitation. The blots were washed as above and developed for 5 min with ECL detection reagent according to the manufacturers instructions. Exposure time was 30 seconds. Double band in chromatine-enriched fraction (1) has been outcompeted in peptide neutralization assay by peptide used to elicit H3 antibodies. Chromatin izolation was carried out as described (Zilberman et al. 2008) with minor modifications.

    Courtesy of Weronika Sura and Dr. Piotr A. Ziolkowski, Department of Biotechnology, Adam Mickiewicz University, Poznan, Poland


     

    30 μg of 5 µl of Chlamydomonas reinhardtii protein saturated in 8M urea were separated on 15% SDS-PAGE and blotted for 1hour to 0.2 µm nitrocellulose at 100V using wet transfer system. Blots were blocked with 0.5% cold fish gelatin for 1hr at room temp with agitation. Blot was incubated in the primary antibody (anti-H3) at a dilution of 1:2500 for an hour at RT with agitation. The blots were washed with 3X 15min TBS-TT at RT with agitation. Blots as incubated in the secondary antibody (DayLight 800) 1:5000 dilution for 30min at RT with agitation and washed 1X with TBSTT for 15min, 1X with TBST for 15min before scanning with the ODyssey IRD scanner.

    Courtesy of Dr. Betty Chung, University of Cambridge, United Kingdom



    western blot using anti-H3 antibodies on tomato samples
    5 µl of 15μg/µl Solanum lycopersicum protein saturated in 8M urea were separated on 15% SDS-PAGE and blotted for 1hour to 0.2 µm nitrocellulose at 100V using wet transfer system. Blots were blocked with 0.5% cold fish gelatin for 1hr at room temp with agitation. Blot was incubated in the primary antibody (anti-H3) at a dilution of 1:2500 for an hour at RT with agitation. The blots were washed with 3X 15min TBS-TT at RT with agitation. Blots as incubated in the secondary antibody, fluorescent antibody (AS12 2460, Agrisera) 1:5000 dilution for 30min at RT with agitation and washed 1X with TBSTT for 15min, 1X with TBST for 15min before scanning with the ODyssey IRD scanner.

    Courtesy of Dr. Betty Chung and Dr Zhengming Wang, University of Cambridge, United Kingdom


    ICC

    Immunocytochemical assays were performed according to the method described earlier (Rybaczek and Maszewski 2006). Excised apical parts of Vicia faba roots (1.5 mm long) were fixed for 45 min (18°C) in PBS-buffered 3.7% paraformaldehyde, washed several times with PBS and placed in a citric acid-buffered digestion solution (pH 5.0; 37°C for 45 min) containing 2.5% pectinase (Fluka), 2.5% cellulase (Onozuka R-10; Serva) and 2.5% pectoliase (ICN). After removing the digestion solution, root tips were washed 3 times in PBS, rinsed with distilled water and squashed onto Super Frost Plus glass slides (Menzel-Gläser). Air-dried slides were pretreated with PBS-buffered 5% BSA at 20°C for 50 min and incubated overnight in a humidified atmosphere (4°C) with rabbit antibody raised against H3 histone (Agrisera), dissolved in PBS containing 1% BSA (at a dilution of 1:50). Following incubation, slides were washed 3 times with PBS and incubated for 1 h (18°C) with Agrisera secondary goat anti-rabbit IgG DyLight®488 antibody (AS09 633, 1:1000). Nuclear DNA was stained with 4’,6-diamidino-2-phenyl-indole (DAPI, 0.4 μg/ml; Sigma-Aldrich). Following washing with PBS, slides were air dried and embedded in Vectashield Mounting Media for Fluorescence (Vector Laboratories). Observations were made using Optiphot-2 fluorescence microscope (Nikon) equipped with B-2A filter (blue light; λ ≈ 495 nm) for DyLight-conjugated antibodies and UV-2A filter (UV light; λ ≈ 365 nm) for DAPI. All images were recorded at exactly the same time of integration using DXM 1200 CCD camera.

    Courtesy Dr. Dorota Rybaczek, Łódź University, Poland

    Application examples:

    Reactant: Malus domestica (Apple)

    Application: Western Blotting

    Pudmed ID: 23886449

    Journal: Plant Methods

    Figure Number: 2B

    Published Date: 2013-07-28

    First Author: Sikorskaite, S., Rajamäki, M. L., et al.

    Impact Factor: 5.139

    Open Publication

    Analysis of protein fractions from different steps of nuclei isolation. The protein fractions obtained following the main steps of the procedure used for isolation of nuclei from leaves of apple are shown. Equal amounts of proteins (4 ?g) from each fraction were loaded on the gel. A) Lumenal-binding protein 2 (BiP2), B) histone H3 and C) plastocyanin (PC) were detected with specific antibodies by western blot analysis. D) Coomassie blue staining of the fractionated proteins separated by polyacrylamide gel electrophoresis. Lane 1: crude extract of proteins from homogenized leaf tissue; lane 2: resuspended pellet of the whole cell lysate obtained following treatment with Triton X-100 and centrifugation; lane 3: nuclei collected from the 60% Percoll layer (see nuclear fraction in Figure 1B); lane 4: the interface fraction of 60% Percoll and 2.5 M sucrose layers in the density gradient containing chloroplasts and unbroken cells (see 60% P/2.5 M S interface in Figure 1B); lane 5: sucrose layer of the density gradient (see 2.5 M sucrose layer in Figure 1B); lane 6: nuclei purified by centrifugation on a 35% Percoll cushion.


    Reactant: Arabidopsis thaliana (Thale cress)

    Application: Western Blotting

    Pudmed ID: 27109828

    Journal: Nat Commun

    Figure Number: 6A

    Published Date: 2016-04-25

    First Author: Yang, B. J., Han, X. X., et al.

    Impact Factor: 13.783

    Open Publication

    Auxin stimulates PTRE1 accumulation at the plasma membrane.(a) Western blot analysis showed that auxin treatment results in relatively more PTRE1 at the plasma membrane, but decreased levels in nucleus and cytoplasm. Arabidopsis seedlings expressing PTRE1-GFP were treated with NAA (1??M, 60 or 120?min) and then surface-exposed membrane proteins were analysed using PTRE1 antibody or plasma membrane marker H+-ATPase. Nucleus and cytoplasm fractions were prepared from Col seedlings and analysed by western blot using antibody against PTRE1, nuclear marker H3 or cytoplasm marker UGPase. The relative quantities of the proteins were calculated by using image pro plus and indicated. (b) A proposed model for how PTRE1 and TIR1 coordinate auxin responses regulating proteasome activity and Aux/IAA protein degradation. Under normal condition (with basal auxin levels), 26S proteasome activity is maintained by appropriate distribution of PTRE1 at the plasma membrane and in intracellular compartments. In response to auxin, auxin rapidly stimulates the association of TIR1 and Aux/IAA proteins resulting in degradation of Aux/IAAs (1). Later, auxin suppresses PTRE1 to inhibit proteasome activity (possibly through stimulating the accumulation of PTRE1 at plasma membrane, resulting in decreased intracellular and nuclear localization) and hence suppresses Aux/IAA protein degradation (2) to coordinate regulation of auxin responses, reflecting a mechanism for fine control of Aux/IAA homeostasis and auxin signalling.


    Reactant: Arabidopsis thaliana (Thale cress)

    Application: Western Blotting

    Pudmed ID: 28204553

    Journal: J Exp Bot

    Figure Number: 4A

    Published Date: 2017-01-01

    First Author: Jensen, G. S., Fal, K., et al.

    Impact Factor: 6.088

    Open Publication

    ths1 and vip3-2 mutants have altered global and genic histone H3 methylation patterns and fail to induce TCH3 and TCH4 in response to touch. (A) Chromatin extracts from cauline leaves of the indicated genotypes were separated by SDS-PAGE and detected with antibodies specific to H3K36me3 or H3K27me3. (B) Relative enrichment for H3K36me3 at the TCH3 and TCH4 loci in cauline leaf chromatin. Chromatin was isolated as in (A), then immunoprecipitated with the H3K36me3 antibody or without antibody and precipitated DNA amplified by qRT-PCR. Data presented is a percentage of the input, normalized to the S-ADENOSYLMETHIONINE SYNTHASE (SAM) gene and represented as a fold difference with the wild type non-treated sample. Error bars indicate the SEM for three biological replicates with two technical replicates each. (C) Quantitative reverse-transcriptase PCR analysis of TCH3 and TCH4 expression in response to touch in wild type and mutant seedlings. Seedlings were brushed for 2 minutes with a paintbrush according to the scheme shown in the top panel. RNA was prepared from the aerial tissues of treated and untreated plants and cDNA amplified with gene specific primers. The data was normalized to TUB4 (upper panels) or TCTP (lower panels) as reference genes and is presented as fold change compared to wild type non-treated samples. The error bars indicate SEM from three replicates. Asterisks mark significant difference from the untouched control P<0 05.


    Reactant: Arabidopsis thaliana (Thale cress)

    Application: Western Blotting

    Pudmed ID: 28935922

    Journal: Nat Commun

    Figure Number: 2D

    Published Date: 2017-09-21

    First Author: Chen, P., Takatsuka, H., et al.

    Impact Factor: 13.783

    Open Publication

    MYB3R3 accumulation in the root tip. a, c Confocal microscopy images of root tips. Five-day-old myb3r3 seedlings harbouring ProMYB3R3::MYB3R3-GFP were treated with 2??M zeocin for the indicated times a, or with 2??M zeocin, 50??M MG132 or 25??M roscovitine for 24?h c. Scale bars, 100??m. b, d Protein level of MYB3R3-GFP in roots. Ten-day-old myb3r3 seedlings harbouring ProMYB3R3::MYB3R3-GFP were treated with 5 or 10??M zeocin for 24 or 48?h b, or with 2??M zeocin, 50??M MG132 or 25??M roscovitine for 24?h d. Forty (b) or 20?µg (d) of total protein extracted from roots were subjected to immunoblotting using antibodies against GFP, ?-tubulin or histone H3. Protein extract from the myb3r3 mutant was used as a control (d). Relative levels of MYB3R3-GFP are expressed as the fold change, normalized with respect to the band of ?-tubulin or histone H3


    Reactant: Arabidopsis thaliana (Thale cress)

    Application: Western Blotting

    Pudmed ID: 28935922

    Journal: Nat Commun

    Figure Number: 6B

    Published Date: 2017-09-21

    First Author: Chen, P., Takatsuka, H., et al.

    Impact Factor: 13.783

    Open Publication

    Phosphorylation state of MYB3R3 is associated with protein accumulation and zeocin response. a Confocal microscopy images of myb3r3 root tips harbouring ProMYB3R3::MYB3R3AAA-GFP or ProMYB3R3::MYB3R3DDD-GFP. Five-day-old seedlings were treated with or without 2??M zeocin, or with 50??M MG132, for 24?h. Scale bars, 100??m. b Protein level of MYB3R3-GFP in roots. Ten-day-old myb3r3 seedlings harbouring ProMYB3R3::MYB3R3-GFP (WT), ProMYB3R3::MYB3R3AAA-GFP (AAA) or ProMYB3R3::MYB3R3DDD-GFP (DDD) were treated with or without 2??M zeocin for 24?h, and 40?µg of total protein extracted from roots was immunoblotted with anti-GFP or anti-histone H3 antibodies. Protein extract from myb3r3 was used as a control. Relative levels of MYB3R3-GFP are expressed as the fold change, normalized with respect to the band of histone H3. c Eighteen-day-old seedlings of WT, myb3r3 and myb3r3 carrying ProMYB3R3::MYB3R3AAA-GFP or ProMYB3R3::MYB3R3DDD-GFP. Scale bars, 2?cm. d, e Root growth of WT, myb3r3 and myb3r3 carrying ProMYB3R3::MYB3R3-GFP, ProMYB3R3::MYB3R3AAA-GFP or ProMYB3R3::MYB3R3DDD-GFP. Five-day-old seedlings were transferred to medium with or without 2?µM zeocin, and root length was measured for 6 days d. Root length after 6 days of zeocin treatment is shown in e. Data are presented as mean?±?SD (n?>?30). Significant differences from WT were determined by Student’s t-test: *P?

    Reactant: Arabidopsis thaliana (Thale cress)

    Application: Western Blotting

    Pudmed ID: 29180698

    Journal: Nat Commun

    Figure Number: 4B

    Published Date: 2017-11-27

    First Author: Huot, B., Castroverde, C. D. M., et al.

    Impact Factor: 13.783

    Open Publication

    Induction of NPR1 nuclear localization is retained at 30?°C. a Representative confocal microscopy images of NPR1-YFP plants (n?=?4) 24?h after spraying with mock or BTH. Images are of YFP (yellow) alone or YFP overlaid on Brightfield (BF, grey-scale). Scale bar length represents 10?µm. b Western blots of whole-cell lysate (W), non-nuclear (C, cytosolic) and nuclear (N) enriched fractions isolated from NPR1-Y1 transgenic plants treated with mock (?) or BTH (+) solutions at 23?°C or 30?°C. Equal volumes (10?µl) of each protein sample were loaded and run in two separate 4–12 % gradient SDS-PAGE gels. Following transfer to PVDF membranes, one blot was probed with ?-GFP primary antibody to detect the NPR1-YFP protein while the other blot was cut in two and the upper portion probed with ?-UGPase (a cytosolic protein control) and the lower portion probed with ?-H3 (a nuclear protein control). Whole-cell lysate extracted from npr1 plants treated with BTH at 23?°C was used as the negative control for the NPR1-YFP band. All data are representative of three independent experiments

    Reactant: Botrytis cinerea

    Application: Western Blotting

    Pudmed ID: 32098836

    Journal: mSystems

    Figure Number: 1E

    Published Date: 2020-02-25

    First Author: Li, H., Zhang, Z., et al.

    Impact Factor: None

    Open Publication

    Generation of ?bcactA mutants. (A) Replacement strategy for deletion of the bcactA gene. The 5? flank and 3? flank of bcactA were amplified and ligated into pLOB7 to flank the hygromycin resistance cassette to obtain the replacement vectors. Deletion mutants were generated by replacing the bcactA gene with the hygromycin resistance cassette through transformation of the protoplasts of the wild-type (WT) strain. (B) PCR diagnosis of ?bcactA mutants. PCR was performed using the primer pair bcactA-homo-up/HPH-det, to ensure that homologous recombination occurred at the target site. (C) Diagnosis of the homozygotes of ?bcactA mutants. PCR was performed with the primer pair bcactA-homo-up/bcactA-R-down, to ensure that the mutants were homozygous with no wild-type bands. (D) Southern blot analysis of WT and ?bcactA strains. The genomic DNA was digested with SacI and BamHI, separated in an agarose gel, and hybridized with a probe (a fragment on the hygromycin resistance cassette labeled with digoxigenin). Numbers represent different strains. (E) Immunoblotting analysis of BcactA protein in WT and ?bcactA strains. Total cytoplasmic proteins were extracted from 2-day-old mycelia cultured in PDB and immunoblotted with commercially available antibody to actin (Abmart; M20011). Histone 3 (H3) was used as a loading control.

    Reactant: Arabidopsis thaliana (Thale cress)

    Application: Western Blotting

    Pudmed ID: 32210987

    Journal: Front Plant Sci

    Figure Number: 3A

    Published Date: 2020-03-27

    First Author: Fu, C., Liu, X., et al.

    Impact Factor: 5.435

    Open Publication

    Western blot results exhibiting the expression of BRF2 protein in 10-day-old seedlings of WT and fes1a mutants.

    Reactant: Arabidopsis thaliana (Thale cress)

    Application: Western Blotting

    Pudmed ID: 34194459

    Journal: Front Plant Sci

    Figure Number: 5A

    Published Date: 2021-07-02

    First Author: Noh, S. W., Seo, R. R., et al.

    Impact Factor: 5.435

    Open Publication

    Monomethylation of histone H3K4 is associated with the transcription of genes encoding transcription factors in Arabidopsis. (A) Abundance of H3K4me1, H3K4me2, and H3K4me3 marked proteins in WT and ldl1 ldl2 plants. The right panel shows modified histone H3 protein levels in Arabidopsis (average ± SD, *p < 0.05, Student’s t-test, n = 3). The results of all independent experiments are shown in Supplementary Figure 6. (B) Genomic DNA regions of gene-specific primers used in panels (C-E). (C-E) ChIP-qPCR to examine the enrichment of modified histone H3 proteins in the identified LDL1-target genes (C), transcription factors overrepresented in the ldl1 ldl2 mutants (D), and PR1 and FRK1 genes (E). Enrichment of Lys 4- mono-, Lys 4- di-, and Lys 4-trimethylated histone H3 protein at the chromatin regions of genes was measured in wild type (white bars) and ldl1 ldl2 (gray bars). The amount of DNA after ChIP was quantified by qPCR, and the means represent the average immunoprecipitation efficiencies (%) against total input DNA used. Each plot shows a representative of two independent biological replications (with similar results), and the data points are the average values of technical triplicates (average ± SEM, *p < 0.05, Student’s t-test, n = 3). The blue bars are the amplicon regions used for ChiP-qPCR, and the primer sequences used in this study are shown in Supplementary Table 2.

  • Additional Information
  • Additional information:

    Cellular [compartment marker] of nucleoplasm, loading control antibody for Chlamydomonas reinhardtii

    Additional information (application): Specific fluorescence in ICC has been observed for interphase nuclei as well as around centromer region (where Ser10 of histone H3 is phosphorylated) in mitotic chromosomes
  • Background
  • Background:

    Histone 3 (H3) located in nuclei, incorporated into chromatin. Present in nucleosome together with H2A, H2B and H4.

  • Product Citations
  • Selected references: Farago et al. (2022) Small paraquat resistance proteins modulate paraquat and ABA responses and confer drought tolerance to overexpressing Arabidopsis plants. Plant Cell Environ. 2022 Jul;45(7):1985-2003. doi: 10.1111/pce.14338. Epub 2022 Apr 29. PMID: 35486392; PMCID: PMC9324991.
    Margaritopoulou et al (2021) Enriched HeK4me3 marks at Pm-0 resistance-related genes prime courgette against Podosphaera xanthii. Plant Physiol. 2021 Sep 21:kiab453. doi: 10.1093/plphys/kiab453. Epub ahead of print. Erratum in: Plant Physiol. 2021 Nov 11;: PMID: 34597395.
    Perlaza (2021). Organelle Size and Quality Control in Chlamydomonas Reinhardtii. UCSF. ProQuest ID: Perlaza_ucsf_0034D_12217. Merritt ID: ark:/13030/m5257z1d. Retrieved from https://escholarship.org/uc/item/1jg3874h
    Sun et al. (2021) The epigenetic factor FVE orchestrates cytoplasmic SGS3-DRB4-DCL4 activities to promote transgene silencing in Arabidopsis. Sci Adv. 2021 Aug 4;7(32):eabf3898. doi: 10.1126/sciadv.abf3898. PMID: 34348894; PMCID: PMC8336953.
    Chen et al. (2019). Phalaenopsis LEAFY COTYLEDON1-Induced Somatic Embryonic Structures Are Morphologically Distinct From Protocorm-Like Bodies. Front Plant Sci. 2019 Nov 29;10:1594. doi: 10.3389/fpls.2019.01594. PMID: 31850050; PMCID: PMC6896055.
    Perlaza et al. (2019). The Mars1 kinase confers photoprotection through signaling in the chloroplast unfolded protein response. Elife. 2019 Oct 15;8. pii: e49577. doi: 10.7554/eLife.49577. (immunofluorescence)
    Dalmadi et al. (2019). AGO-unbound cytosolic pool of mature miRNAs in plant cells reveals a novel regulatory step at AGO1 loading. Nucleic Acids Res. 2019 Aug 8. pii: gkz690. doi: 10.1093/nar/gkz690.
    Barua et al. (2019). Dehydration-responsive nuclear proteome landscape of chickpea (Cicer arietinum L.) reveals phosphorylation-mediated regulation of stress response. Plant Cell Environ. 2019 Jan;42(1):230-244. doi: 10.1111/pce.13334.
    Du et al (2019). Proteomic identification of lipid-bodies-associated proteins in maize seeds. Acta Physiologiae Plantarum, May 2019, 41:70
    Lai et al. (2018). Salicylic acid-independent role of NPR1 is required for protection from proteotoxic stress in the plant endoplasmic reticulum. Proc Natl Acad Sci U S A. 2018 May 29;115(22):E5203-E5212. doi: 10.1073/pnas.1802254115.
    Wang et al. (2018). Degradation of unmethylated miRNA/miRNA*s by a DEDDy-type 3' to 5' exoribonuclease Atrimmer 2 in Arabidopsis. Proc Natl Acad Sci U S A. 2018 Jul 10;115(28):E6659-E6667. doi: 10.1073/pnas.1721917115.
    Hartmann et al. (2018). Subcellular Compartmentation of Alternatively Spliced Transcripts Defines SERINE/ARGININE-RICH PROTEIN30 Expression. Plant Physiol. 2018 Apr;176(4):2886-2903. doi: 10.1104/pp.17.01260.
    Duan et al. (2017). A Lipid-Anchored NAC Transcription Factor Is Translocated into the Nucleus and Activates Glyoxalase I Expression during Drought Stress. Plant Cell. 2017 Jul;29(7):1748-1772. doi: 10.1105/tpc.17.00044. (Nicotiana benthamiana)
    Rihan et al. (2017). An analysis of the development of cauliflower seed as a model to improve the molecular mechanism of abiotic stress tolerance in cauliflower artificial seeds. Plant Physiol Biochem. 2017 Jul;116:91-105. doi: 10.1016/j.plaphy.2017.05.011.
    Shin et al. (2017). The metabolic sensor AKIN10 modulates the Arabidopsis circadian clock in a light-dependent manner. Plant Cell Environ. 2017 Jan 5. doi: 10.1111/pce.12903.
    Correa-Galvis et al. (2016). Photosystem II Subunit PsbS Is Involved in the Induction of LHCSR Protein-dependent Energy Dissipation in Chlamydomonas reinhardtii. J Biol Chem. 2016 Aug 12;291(33):17478-87. doi: 10.1074/jbc.M116.737312.
    Castellano et al. (2016). A pathogenic long noncoding RNA redesigns the epigenetic landscape of the infected cells by subverting host Histone Deacetylase 6 activity. New Phytol. 2016 Sep;211(4):1311-22. doi: 10.1111/nph.14001. Epub 2016 May 12.
    Ghandi et al. (2016). Tomato yellow leaf curl virus infection mitigates the heat stress response of plants grown at high temperature. Sci Rep. 2016 Jan 21;6:19715. doi: 10.1038/srep19715.
    Gorovits et al. (2016). Tomato yellow leaf curl virus confronts host degradation by sheltering in small/midsized protein aggregates. Virus Res. 2016 Feb 2;213:304-13. doi: 10.1016/j.virusres.2015.11.020. Epub 2015 Dec 1
  • Protocols
  • Agrisera Western Blot protocol and video tutorials

    Protocols to work with plant and algal protein extracts

    Agrisera Educational Posters Collection




    Preparation of cytosolic and nuclear protein fractions


    1. Prepare protoplasts from 50 ml Arabidopsis thaliana cell culture according to the protocol of PEG transfection.
    2. Resuspend protoplasts in 10 ml GH buffer and keep the solution on ice for 10 min.
    GH buffer: 100mM glycine
    0.1% Hexylene glycol
    0.37M (4.7% w/v) saccharose
    0.3mM Spermine
    1.0mM Spermidine
    pH 8.3 with Ca(OH)2
    3. To release nuclei add Triton X100 to a final concentration of 0.1%. Pipetting gently up and down several
    times with a plastic pipette might be necessary to lyse cells.
    4. After 5min sediment nuclei by centrifugation at 1000 xg for 15 min at 4°C. Save supernatant as the
    cytoplasmic fraction. Wash the pelleted nuclei two times with GHT (GH+0.1% TX100) then finally
    resuspended in a suitable volume of extraction buffer + protease inhibitors.

    Courtesy Dr. Laszlo Bako, Umeå Plant Science Centre

  • Reviews:
  • Reviews
    Below, you can grade the product on a scale from 0 to 5.
    Please also provide information about species, application, dilution and obtained result for the reviewed antibody.
    Your name will be displayed as the sender.
    Number of reviews: (7)
    Peter Ma | 2023-04-10
    0 | 0
    This H3 antibody worked very well and showed no background with our samples. We used 1:5000 dilution of H3 for total Arabidopsis protein extractions and 1:10000 dilution for secondary antibody.
    KAILI XIE | 2021-05-12
    0 | 0
    This H3 antibody worked well in western blot with a dilution of 1:5000 and the signal is very strong. If you want use it to do the ChIP assay, maybe you need to do the test firstly.
    Kaili Xie | 2021-05-06
    0 | 0
    This H3 antibody worked really well in ChIP and western blot in our hands. The dilution for western blot is 1:5000 and signal is very strong!
    INMACULADA SNCHEZ-VICENTE | 2019-10-10
    0 | 0
    We used H3 antibody with nuclear protein extracts from Arabidopsis at a dilution of 1:5000 and it gave very good result. I recomend this product.
    Sidona | 2011-11-16
    0 | 0
    We have used H3 antibody with nuclear protein extracts from Nicotiana and Malus plants at a dilution of 1:10000 and it gave very strong signal. The same dilution could be re-used at least 3 times.
    Rena Gorovits | 2011-09-20
    0 | 0
    strong signal in nuclear fraction of tomato protein extracts
    Dr. Leonardo Magneschi | 2011-06-29
    0 | 0
    I tested this antibody for WB on Chlamydomonas reinhardtii whole cells and nuclei-enriched protein samples at a dilution of 1:5000 (see figure in the ''info'' section of this antibody). The antibody has high affinity for the Chlamydomonas H3 protein and generates a good signal after short time exposures with standard ECL.

Accessories

AS09 602 |  Clonality: Polyclonal | Host: Goat | Reactivity: Rabbit IgG (H&L)

10 % until end of 2023. Use discount code: Conj10

201 €
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AS09 607 |  Clonality: Polyclonal Host: Goat Reactivity: Rabbit IgG (H&L)

10 % until end of 2023. Use discount code: Conj10

206 €
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AS16 ECL-S | extreme low femtogram detection

This product can be purchased in 3 different volumes:

AS16 ECL-S-10, 10 ml. Trial size limited to one per customer

AS16 ECL-S-100, 100 ml

AS16 ECL-S-1L, 1L

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