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Anti-ribosomal P protein autoantibodies

Anti-ribosomal P protein autoantibodies are a type of autoantibody that target the ribosomal P proteins, which are essential components of the cellular machinery responsible for protein synthesis.
These autoantibodies have been associated with various autoimmune disorders, including systemic lupus erythematosus, neuropsychiatric lupus, and others.
Accurate and reproducible detection and quantification of anti-ribosomal P protein autoantibodies are crucial for disease diagnosis, monitoring, and research.
PubCompare.ai, the leading AI platform for scientific protocols, can help optimize your anti-ribosomal P protein autoantibody research by discovering the best protocols and products from literature, preprints, and patents using AI-driven comparisons.
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Most cited protocols related to «Anti-ribosomal P protein autoantibodies»

1
Autoantibody and Cytokine Profiling in Murine Lupus
Cited 10 times
HEp-2 immunofluorescence assays (Antibodies, Davis, CA) were performed as previously described (14 (link)) with serum diluted at 1/200 and were scored for relative fluorescence intensity of nuclear and cytoplasmic staining on a scale of 0–3 and for the presence or absence of mitotic chromatin by an observer blinded to the genotype of the mice.
For anti-nucleosome ELISA, polystyrene plates were coated with poly-L-lysine (Sigma-Aldrich, St. Louis, MO). Plates were then incubated with phenol-extracted and S1 nuclease-treated dsDNA from calf thymus (Sigma-Aldrich), followed by calf thymus histones type II-AS (Sigma-Aldrich). After blocking with 1% BSA in PBS, serial dilutions of serum from 1/200 to 1/5400 were added. Specific Abs were detected with alkaline phosphatase-conjugated goat anti-mouse IgG (Southern Bio-technology Associates, Birmingham, AL), and absorbance at 405/630 nm was compared with a purified PL2-3 monoclonal anti-nucleosome standard (27 (link)) for quantitation.
Anti-Sm ELISA was performed as previously described (14 (link)) with serial dilutions of serum from 1/200 to 1/5400. ELISAs for anti-ribosomal P Ag autoantibodies and anti-RNA Abs were described previously (28 (link)).
Anti-IgG2a RF titers were determined by ELISA essentially as described previously (29 (link)). Polystyrene plates were coated with purified mAb 23.3 (IgG2a,λ anti–4-hydroxy-3-nitro-phenylacetyl) overnight. After blocking with 1% BSA in PBS, serial dilutions of serum from 1/200 to 1/5400 were added. Specific Abs were detected with biotinylated anti-κ L chain (clone 187.1; BD Pharmingen, San Diego, CA), followed by alkaline-phosphatase–conjugated streptavidin (Invitrogen, Carlsbad, CA), and absorbance at 405/630 nm was compared with a 400tμ23 (IgM-RF) standard for quantitation.
Total serum IgG was determined by ELISA as described previously (14 (link)). Titers of individual IgG isotypes were measured by cytometric bead assay (Millipore, Bedford, MA) per the manufacturer’s protocols.
Serum IL-6, TNF-α, IL-12p40, IL-12p70, and IL-10 were measured by multiplex cytometric bead assay (Bio-Rad, Hercules, CA) per the manufacturer’s instructions. Serum IL-23(p19/p40) was measured by ELISA (eBioscience, San Diego, CA). Serum IFN-α was measured as previously described (14 (link)) with serum diluted 1/20.
Nickerson K.M., Christensen S.R., Shupe J., Kashgarian M., Kim D., Elkon K, & Shlomchik M.J. (2010). TLR9 Regulates TLR7- and MyD88-Dependent Autoantibody Production and Disease in a Murine Model of Lupus. Journal of immunology (Baltimore, Md. : 1950), 184(4), 1840-1848.
Publication 2010
Alkaline Phosphatase anti-IgG Anti-ribosomal P protein autoantibodies Antibodies Biological Assay Chromatin Clone Cells Cytoplasm DNA, Double-Stranded Enzyme-Linked Immunosorbent Assay Fluorescence Fluorescent Antibody Technique, Direct Genotype Goat Histones IgG2A IL10 protein, human Immunoglobulin Isotypes Interferon-alpha Interleukin-12 Interleukin-12 Subunit p40 Lysine Mus Nucleosomes Phenols Poly A Polystyrenes Ribosomes Serum Streptavidin Technique, Dilution Thymus Plant Tumor Necrosis Factor-alpha
2
Transgenic Plasmodium Parasite Analysis
Cited 5 times
The growth of blood stages of the reporter and transgenic P. berghei parasites was determined during the cloning period as described30 (link)49 (link). Feeding of An. stephensi mosquitoes, determination of oocyst production, sporozoite collection were performed as described30 (link). Expression of PvCSP-VK210 and PvCSP-VK247 antigens in sporozoites of the transgenic parasites was analysed by immunofluorescence- staining assay (IFA), using anti-P. vivax antigen monoclonal antibodies (anti-PvCSP-VK210 (MR4) or anti-PvCSP-247 (MR4) antibodies; diluted 200 times) or anti-PbCSP 3D11 antibodies as a control; diluted 1000 times. Purified sporozoites were fixed with 4% paraformaldehyde in PBS for 20 min on ice, then washed three times with PBS and blocked with 20 ul10% FCS + 1% BSA in PBS for 30 min at room temperature. The excess blocking medium was removed, followed by the addition of 20–25 uL primary monoclonal antibody in 10% FCS + 1% BSA in PBS (blocking medium) for 1–2 hours at room temperature or overnight at 4 °C. After incubation the primary antibody was removed and the slides washed three times with PBS, followed by the staining with the secondary antibody (Alexa Fluor® 488 Goat Anti-Mouse IgG from life technologies, Cat# A-11001) diluted 800 times in 10% FCS + 1% BSA in PBS (blocking medium) for 1 hour at room temperature. After washing three times with PBS, nuclei were stained with 2% Hoechst-33342 (Cell Signaling Technology #4082S) in PBS for 10 minutes at room temperature, washed twice with PBS and left to air-dry, this followed by adding Fluorescence Mounting Medium (Dako, code S3023) before complete dry out. Cover slips were mounted onto the slides, and the slides were sealed with nail polish and left to dry overnight in dark. The parasites in both blue and green channels were analyzed using a DMI-300B Leica fluorescence microscope and images processed using ImageJ software.
Salman A.M., Montoya-Díaz E., West H., Lall A., Atcheson E., Lopez-Camacho C., Ramesar J., Bauza K., Collins K.A., Brod F., Reis F., Pappas L., González-Cerón L., Janse C.J., Hill A.V., Khan S.M, & Reyes-Sandoval A. (2017). Rational development of a protective P. vivax vaccine evaluated with transgenic rodent parasite challenge models. Scientific Reports, 7, 46482.
Publication 2017
alexa fluor 488 Animals, Transgenic Anti-Antibodies anti-IgG Anti-ribosomal P protein autoantibodies Antibodies Antigens BLOOD CD244 protein, human Cell Nucleus Culicidae Fluorescence Goat HOE 33342 Immunofluorescence Immunoglobulins Mice, Laboratory Microscopy, Fluorescence Monoclonal Antibodies Oocysts paraform Parasites Sporozoites
3
Neurological Biomarker Analysis in Rats
Cited 5 times
All commercial chemicals were of the highest available grade: Sprague-Dawley rats were from Charles-River Laboratories (Lecco, Italy). The 5% CO2: 95% N2 gas cylinder was from Sapio, Monza, Italy. Complete protease inhibitor cocktail was from Roche Diagnostics S.p.A (Milano, Italy). Hydroxy-1,4-naphtoquinone (juglone), Lactacystin, 1-β-D arabinofuranosylcytosine (Ara-C), lithium chloride solution, SB-216763 Gsk-3 inhibitor, solutions for electrophoresis were from Sigma Chemical Co. (Milano, Italy). All the stock solutions for cell culture were from Euroclone (Celbio Milano, Italy). Gibco Neurobasal medium (NBM) and B27 supplement, Dynabeads® protein G, sodium dodecyl sulphate (SDS) NuPAGE reagents (4–12% Bis-Tris gel; sample buffer; running buffer), Novex Sharp Protein Standard, anti-Tau was from Life Technologies (Milano, Italy).
Anti-Pin1, anti P-Pin1S16 and anti-Ubiquitin (PD41) were from Cell Signaling (Beverly, USA). Anti-HIF-1α and anti-lactate dehydrogenase (LDH) antibodies were from Abcam (Cambridge Science Park, UK). Anti P-Ser/Thr-Pro (MPM2) and Anti-Pin1 for immunoprecipitation antibodies were from Millipore S.p.A (Milano, Italy). Anti-BACE1 antibody was from Santa Cruz Biotechnology Inc. (Santa Cruz, CA, USA). Secondary HRP-conjugated antibodies and ECL SuperSignal detection kit were from Pierce (Rockford, IL, USA). Anti-Actin and anti P-TauT231 antibodies were from Sigma Chemical Co (Milano, Italy).
Lonati E., Brambilla A., Milani C., Masserini M., Palestini P, & Bulbarelli A. (2014). Pin1, a new player in the fate of HIF-1α degradation: an hypothetical mechanism inside vascular damage as Alzheimer’s disease risk factor. Frontiers in Cellular Neuroscience, 8, 001.
Publication 2014
Actins Anti-Antibodies Anti-ribosomal P protein autoantibodies Antibodies Antibodies, Anti-Idiotypic BACE1 protein, human Bistris Buffers Cell Culture Techniques Chloride, Lithium Cytarabine Diagnosis Dietary Supplements Electrophoresis G-substrate Glycogen Synthase Kinase 3 Immunoprecipitation juglone lactacystin Lactate Dehydrogenase PIN1 protein, human Protease Inhibitors Proteins Rats, Sprague-Dawley Rivers SB 216763 seryl-proline Sulfate, Sodium Dodecyl Ubiquitin
4
Quantifying Cochlear Protein Expression
Cited 4 times
Cochlea proteins were incubated in cell lysis buffer (10 mM Tris, pH=7.4, 1% Triton X-100, 150 mM NaCl, 1 mM EDTA, 0.2 mM PMSF) and extracted using a homogenizer. The proteins from the samples (50 μg) were subjected to SDS-polyacrylamide gel electrophoresis and blotted onto a polyvinylidene difluoride membrane. The primary antibodies used were anti-p-Akt rabbit monoclonal antibodies (Millipore; 1 : 200), anti-p27kip rabbit polyclonal antibodies (Abcam; 1 : 200), and anti-GAPDH mouse monoclonal antibodies (Millipore; 1 : 3333). Subsequently, the membrane was incubated for 1 h at room temperature with the appropriate secondary antibodies coupled with horseradish peroxidase. Finally, the immunoreactive bands were visualized using ECL detection reagents.
Sun C., Zhao J., Jin Y., Hou C., Zong W., Lu T., Li H, & Gao J. (2014). PTEN regulation of the proliferation and differentiation of auditory progenitors through the PTEN/PI3K/Akt-signaling pathway in mice. Neuroreport, 25(3), 177-183.
Publication 2014
Anti-Antibodies Anti-ribosomal P protein autoantibodies Antibodies Buffers Cells Cochlea Edetic Acid GAPDH protein, human Horseradish Peroxidase Monoclonal Antibodies Mus polyvinylidene fluoride Proteins Rabbits SDS-PAGE Sodium Chloride Tissue, Membrane Triton X-100 Tromethamine
5
TCA Precipitation and Antibody Dilutions
Cited 4 times
TCA precipitation protocol was followed for total protein extracts (Caspari et al., 2000 (link)). The following dilutions of antibodies were used in this study: 1:100 anti-Tor1, 1:100 anti–P-Tor1.T1972, 1:100 anti–P-Tor2.S1975, 1:1,000 anti–P-Gad8.S546, 1:100 anti–P-Gad8.T387, 1:100 anti-Gad8 antibodies, 1:2,000 Phospho-(Ser/Thr) Akt substrate (PAS) antibody (Cell Signaling Technology), 1:100 p70 S6Kα (Santa Cruz Biotechnology, Inc.), 1:100 P-S6Kα.T389 (Cell Signaling Technology), and 1:1,000 S6 antibody (Abcam). 1:100 mTOR antibodies were from EMD Millipore. 1:100 AKT and 1:100 P-AKT.S473 antibodies were from Cell Signaling Technology. Anti–p-Tor1.T1972, anti–P-Gad8.S546, and anti–P-Gad8.T378 were all generated by Eurogentec. Anti–P-Tor2.S1975 antibodies were used to detect both S. pombe Tor2 and mTOR phosphorylation and were generated by Eurogentec. Anti-Tor1 antibodies were raised against the unique Tor1 sequence (aa 2,231–2,274). Alkaline phosphatase– or peroxidase (only for loading control in Figs. 1 D, 3 A, and 5 I)-coupled secondary antibodies were used for all blots followed by direct detection with NBT/BCIP (VWR International) substrates on polyvinylidene fluoride membranes.
Hálová L., Du W., Kirkham S., Smith D.L, & Petersen J. (2013). Phosphorylation of the TOR ATP binding domain by AGC kinase constitutes a novel mode of TOR inhibition. The Journal of Cell Biology, 203(4), 595-604.
Publication 2013
Alkaline Phosphatase Anti-Antibodies Anti-ribosomal P protein autoantibodies Antibodies Figs FRAP1 protein, human Immunoglobulins Peroxidase Phosphorylation polyvinylidene fluoride Proteins Schizosaccharomyces pombe Technique, Dilution Tissue, Membrane

Most recents protocols related to «Anti-ribosomal P protein autoantibodies»

1
Detecting RSV Protein P with Monoclonal Antibodies
Not available on PMC !

Example 6

The assay was made for determining the maximum dilution of the monoclonal antibodies RSV anti-P from the hybridomas 2E6/D2 and 6H5/H1, which allow the detection of the viral antigen using ELISA. For this, the same indirect ELISA technique was used of the example 6. The well was activated with 50 ng of the purified antigen and the anti-P antibodies 2E6/D2 or 6H5/H1 were used in dilutions 1:2, starting from the concentration of work (3.4 μg/ml) to the dilution 11 in PBS/FBS 10%. In FIG. 3 is observed that to all the dilutions, which were used in the assay, the anti-P 2E6/D2 and 6H5/H1 antibodies are able of detecting the RSV protein P. The anti-P RSVH102 antibody, catalogue number #AB94965, of Abcam, was also able of detecting in all the dilutions the RSV protein P, but it was less efficient than the anti-P 6H5/H1 antibody.

The negative control included on this assay, correspond to a well which does not contain sample (protein P), it was blocked with PBS/FBS 10%, primary antibody was not added (anti-P 2E6/D2 or anti-P 6H5/H1) and it contains only the mouse anti-IgG antibody conjugated with HRP.

US11873331B2. Monoclonal antibodies specifically for the antigen P of the human respiratory syncytial virus, produced and secreted by the cells hybridomas, useful for detection and diagnostic of the infection caused by RSV (2024-01-16). PONTIFICIA UNIVERSIDAD CATOLICA DE CHILE [CL]. Inventors: Susan Marcela Bueno Ramirez [CL], Alexis Mikes Kalergis Parra [CL], Jorge Eugenio Mora Alarcon [CL].
Patent 2024
anti-IgG Anti-ribosomal P protein autoantibodies Antibodies Antibodies, Anti-Idiotypic Antigens Antigens, Viral Biological Assay Enzyme-Linked Immunosorbent Assay Hybridomas Immunoglobulins Mice, House Monoclonal Antibodies Proteins Technique, Dilution
2
Phos-tag SDS-PAGE Analysis of Sch9 Phosphorylation
To analyze differential phosphorylation of Sch9 with Phos-tag SDS-PAGE, cells expressing either HA-Sch9 or Sch9-FLAG were grown on synthetic medium to mid-log phase. For the experiments with HA-tagged Sch9, cells were collected and washed with ice cold PBS and subsequently snap frozen in liquid nitrogen. A bead beating based lysis technique was used for protein extraction using a Triton-Deoxycholate buffer (50 mM HEPES pH7.4; 13.5 mM NaCl; 1% Triton X-100; 0.05% sodium deoxycholate), complemented with a protease and phosphatase inhibitor cocktail (Thermo Fisher Scientific, Merelbeke, Belgium). The cell lysates were cleared by a couple of subsequent centrifugation steps. Protein concentration was measured with the Bradford method (Bio-Rad, Temse, Belgium) and the samples were diluted to the same protein concentration in lysis buffer supplemented with Laemmli loading buffer. Samples were run on a 6,5% SDS-PAGE gel containing 25 μM Phos-tag (Fujifilm Wako Chemicals, Neuss, Germany). Full length HA-Sch9 was detected using an anti-HA-antibody (Roche, Merck, Hoeilaart, Belgium). For the experiments with FLAG-tagged Sch9, cells were heat-inactivated prior to collection and the preparation of protein extracts followed a protocol described previously [18 (link)]. Detection was done using an anti-FLAG antibody (Agilent, Basel, Switzerland). Both methods yielded comparable results.
For the analysis of Sch9 phosphorylation levels, cells expressing GFP-Sch9, GFP-FYVE-Sch9 or only endogenous Sch9 were grown to mid-log phase on synthetic medium. Cell lysate preparation was done as previously described, using bead beating in urea lysis buffer [61 (link)]. The phosphospecific anti-Sch9-P-Thr737 and anti-Sch9 antibodies [61 (link),128 (link)], and the anti-GFP antibody (Roche, Merck, Hoeilaart, Belgium) were used to detect phosphorylated, endogenous Sch9, and GFP-Sch9 respectively after running the samples on an SDS-PAGE gel. Densitometry measurements were done with ImageJ to quantify the phosphorylation levels. The anti-GFP antibody was also used to determine the expression levels of the Fab1-GFP and Fab1VLA-GFP constructs as compared to the loading control Adh2 (anti-Adh2 antibody, Millipore, Merck, Hoeilaart, Belgium). For the detection of Atg13 and Lst4 phosphorylation levels, the strains were transformed with plasmids expressing the tagged constructs Atg13-HA3 or Lst4-V5, respectively. Sample preparations, detection using the anti-HA or anti-Lst4-P-Ser523 antibodies and quantifications were done as previously described [62 (link),66 (link)].
Deprez M.A., Caligaris M., Rosseels J., Hatakeyama R., Ghillebert R., Sampaio-Marques B., Mudholkar K., Eskes E., Meert E., Ungermann C., Ludovico P., Rospert S., De Virgilio C, & Winderickx J. (2023). The nutrient-responsive CDK Pho85 primes the Sch9 kinase for its activation by TORC1. PLOS Genetics, 19(2), e1010641.
Publication 2023
1,3-bis(bis(pyridin-2-ylmethyl)amino)propan-2-ol Anti-Antibodies Anti-ribosomal P protein autoantibodies Antibodies, Anti-Idiotypic Buffers Cells Centrifugation Cold Temperature Densitometry Deoxycholate Deoxycholic Acid, Monosodium Salt Freezing HEPES Laemmli buffer Nitrogen Peptide Hydrolases Phosphoric Monoester Hydrolases Phosphorylation Plasmids Proteins SDS-PAGE Sodium Chloride Strains Triton X-100 Urea
3
Alveolar Bone Protein Extraction and Analysis
As described, alveolar bone was ground to a powder and RIPA lysis buffer (Lot 02408/60412, CwBio Biotechnology Co., Ltd. China) used to extract proteins. Protein concentrations were determined using a bicinchoninic acid protein assay detection kit (P0012S, BeyoTime Biotechnology, China). Samples were mixed with a 1/4 volume of 5× sodium dodecyl sulfate loading buffer and heated to 95°C for 5 min. Proteins then underwent sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were transferred to polyvinylidene fluoride membranes, and blocked in 5% BSA in Tris buffered saline with Tween-20 (TBST) (5% BSA-TBST) at room temperature for 1 h. Membranes were incubated overnight at 4°C with the following: (Tonetti et al., 2018 (link)) anti-p-STAT3 (1:1000; ab76315, Abcam), (Cecoro et al., 2020 (link)) anti-p-STAT5 antibodies (1:1000, AF3304, Affinity Biosciences), (Barutta et al., 2022 (link)) anti- STAT3 (1:1000; ab68153, Abcam), (Zheng et al., 2021 (link)) anti- STAT5 (1:1000; ab32043, Abcam) and followed by incubation with a horseradish peroxidase-conjugated goat anti-rabbit IgG antibody (1:1000, ab6721, Abcam) for 1 h. Immunoreactive bands were detected using enhanced chemiluminescence reagent (B500024, Proteintech, United States) and a gel imaging system (Amersham Imager 600; General Electric Company, United States) to capture images. Image-Pro Plus 6.2 software (Media Cybernetics) was used to analyze and quantify grayscale values normalized to GAPDH levels. Experiments were repeated at least three times.
Gao R., Zhang W., Jiang Y., Zhai J., Yu J., Liu H, & Li M. (2023). Eldecalcitol effectively prevents alveolar bone loss by partially improving Th17/Treg cell balance in diabetes-associated periodontitis. Frontiers in Bioengineering and Biotechnology, 11, 1070117.
Publication 2023
anti-IgG Anti-ribosomal P protein autoantibodies bicinchoninic acid Biological Assay Bones Buffers Chemiluminescence Electricity GAPDH protein, human Goat Horseradish Peroxidase Immunoglobulins polyvinylidene fluoride Powder Proteins Rabbits Radioimmunoprecipitation Assay Saline Solution SDS-PAGE STAT3 protein, human STAT5A protein, human Sulfate, Sodium Dodecyl Tissue, Membrane Tween 20
4
Immunofluorescence Staining of Periodontal Membrane
For immunofluorescence staining, paraffin-embedded sections were immersed in 0.3% H2O2 for 30 min and blocked in 1% BSA-PBS for 20 min. Double immunofluorescence staining was performed on sections to localize Treg cells, Th17 cells, p-STAT3+IL-17A+ cells and p-STAT5+FOXP3+ cells. Sections were incubated overnight at 4°C with the following mixed antibodies: (Tonetti et al., 2018 (link)) anti-IL-17A antibody (1:100; ab189377, Abcam) and anti-CD4 antibody (1:300; ab183685, Abcam), (Cecoro et al., 2020 (link)) anti-FOXP3 antibody (1:100; ab253297, Abcam) and anti-CD4 antibody (1:300; ab183685, Abcam), (Barutta et al., 2022 (link)) anti-IL-17A antibody (1:100; ab189377, Abcam) and anti-p-STAT3 (1:100; ab76315, Abcam), (Zheng et al., 2021 (link)) anti-FOXP3 antibody (1:100; ab253297, Abcam) and anti-p-STAT5 antibodies (1:100, AF3304, Affinity Biosciences, United States). Sections were incubated with mixed green fluorescent goat anti-rabbit IgG H&L (Alexa Fluor 647) (1:200; ab150081, Abcam) and red fluorescent goat anti-mouse IgG H&L (Alexa Fluor 488) (1:200; ab150119, Abcam) antibodies at room temperature in the dark for 1 h. After washing three times in PBS, samples were nuclear stained with 4′,6-diamidino-2-phenylindole (ab104139, Abcam) for 5 min. Images were obtained under inverted fluorescence microscopy (DMi8 S; Leica, Germany) and the periodontal membrane near the root of the maxillary second molar was selected as the area of interest. All cells were counted at × 400 magnification of the original magnification in immunofluorescence images.
Gao R., Zhang W., Jiang Y., Zhai J., Yu J., Liu H, & Li M. (2023). Eldecalcitol effectively prevents alveolar bone loss by partially improving Th17/Treg cell balance in diabetes-associated periodontitis. Frontiers in Bioengineering and Biotechnology, 11, 1070117.
Publication 2023
alexa fluor 488 Alexa Fluor 647 anti-IgG Anti-ribosomal P protein autoantibodies Antibodies Antibodies, Anti-Idiotypic Cells Fluorescent Antibody Technique Goat Interleukin-17A Maxilla Microscopy, Fluorescence Molar Mus Paraffin Periodontal Ligament Peroxide, Hydrogen Rabbits Regulatory T-Lymphocytes STAT3 Protein STAT5A protein, human Th17 Cells Tooth Root
5
Western Blot Analysis of Inflammatory Mediators
Kidney tissues were homogenized in RIPA lysis buffer containing 1 mM phenylmethanesulfonyl fluoride and protease inhibitors. The supernatant was obtained after centrifugation, and the protein concentration was determined using BCA assay, after which 5× loading buffer was added and boiled for 10 min. Protein samples were transferred onto polyvinylidene fluoride membranes after electrophoresis. Anti-NLRP3, anti-ASC, anti-caspase1, anti-TLR4, anti-NF-κB p65 and anti-NF-κB p-p65 antibodies were incubated overnight at 4 °C on a shaker. The membranes were washed five times with Tris-buffered saline with Tween 20 (TBST) for 6 min and incubated with the secondary antibodies for 1 h at room temperature. After incubation, the membranes were washed five times with TBST for 6 min. Finally, the membranes were monitored with an enhanced chemiluminescence reagent and quantified using Image J software (Bethesda, MD).
Wang F., Liu C., Ren L., Li Y., Yang H., Yu Y, & Xu W. (2023). Sanziguben polysaccharides improve diabetic nephropathy in mice by regulating gut microbiota to inhibit the TLR4/NF-κB/NLRP3 signalling pathway. Pharmaceutical Biology, 61(1), 427-436.
Publication 2023
Anti-ribosomal P protein autoantibodies Antibodies Biological Assay Buffers Centrifugation Chemiluminescence Electrophoresis Kidney NF-kappa B Phenylmethylsulfonyl Fluoride polyvinylidene fluoride Protease Inhibitors Proteins Radioimmunoprecipitation Assay Saline Solution Tissue, Membrane Tissues Tween 20

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More about "Anti-ribosomal P protein autoantibodies"

Anti-ribosomal P protein autoantibodies (ARPAs) are a type of autoantibody that target the ribosomal P proteins, which are essential components of the cellular machinery responsible for protein synthesis.
These autoantibodies have been associated with various autoimmune disorders, including systemic lupus erythematouss (SLE), neuropsychiatric lupus, and others.
Accurate and reproducible detection and quantification of ARPAs are crucial for disease diagnosis, monitoring, and research.
Antibodies such as Anti-AKT, Anti-p-p38, Anti-p-ERK, Anti-p-AKT, Anti-ERK1/2, Anti-JNK, and Anti-p-JNK can be used in conjunction with PVDF membranes to study the signaling pathways involved in autoimmune conditions.
Additionally, Anti-β-actin antibodies can serve as loading controls for western blot analyses.
PubCompare.ai, the leading AI platform for scientific protocols, can help optimize your ARPA research by discovering the best protocols and products from literature, preprints, and patents using AI-driven comparisons.
This tool can help take the guesswork out of your research and streamline your workflow, leading to more reproducible and accurate results.
Utilizing PubCompare.ai's powerful features can be particularly beneficial for studying the role of ARPAs in autoimmune disorders, such as SLE, and developing new diagnostic and therapeutic strategies.