Ab16505

Manufactured by Abcam

Sourced in United Kingdom

Ab16505 is a primary antibody that targets a specific protein. The core function of this product is to detect and bind to the target protein in biological samples.

Automatically generated - may contain errors

Lab products found in correlation

Rabbit anti p38, by Cell Signaling Technology (1 mentions) Rabbit anti podocin, by Merck Group (1 mentions) Dapi 4 6 diamidino 2 phenylindole dihydrochloride, by Roche (1 mentions) Axiocam mrm camera, by Zeiss (1 mentions) Cy3 conjugated secondary antibody, by Jackson ImmunoResearch (1 mentions) Axio observer z1 microscope, by Zeiss (1 mentions) Hpa015103, by Merck Group (1 mentions) Anti ptprz1, by Merck Group (1 mentions) Donkey anti sheep igg hrp, by Thermo Fisher Scientific (1 mentions) Anti ptprz, by Santa Cruz Biotechnology (1 mentions) Ab9015, by Abcam (1 mentions) Human upar quantikine elisa kit, by R&D Systems (1 mentions) Fugene 6 transfection reagent, by Promega (1 mentions) Pcmv6 entry vector, by OriGene (1 mentions) Geneart site directed mutagenesis system, by Thermo Fisher Scientific (1 mentions) H0164, by Abcam (1 mentions) Ab33278, by Abcam (1 mentions) Image quant las4000mini, by Cell Signaling Technology (1 mentions) Hrp linked anti mouse igg, by Cell Signaling Technology (1 mentions) Ab177790, by Abcam (1 mentions)

10 protocols using ab16505

Immunoblot Analysis of Podocyte Signaling

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Commercial antibodies used were as follows: rabbit anti-Akt (C67E7, 4691, Cell Signaling Technology, Danvers, MA), rabbit anti-pAkt S473 (D9E, 4060, Cell Signaling Technology), rabbit anti-Akt1 (C73H10, 2938, Cell Signaling Technology), rabbit anti-Akt2 (5B5, 2964, Cell Signaling Technology), rabbit anti-Akt3 (4059, Cell Signaling Technology), rabbit anti-ERK1/2 (137F5, 4695, Cell Signaling Technology), rabbit anti-pERK1/2 T202/Y204 (D13.14.4E, 4370, Cell Signaling Technology), rabbit anti-p38 (9212, Cell Signaling Technology), rabbit anti-p-p38 T180/Y182 (D3F9, 4511, Cell Signaling Technology), rabbit anti-podocin (PO372, Sigma), mouse anti-β-actin (AC15, A1978, Sigma), rabbit anti-cadherin (ab16505, Abcam, Cambridge, UK), and rabbit anti-ERβ (H-150, SC-8974, Santa Cruz). Rabbit anti-nephrin was described previously.^{44 (link)} Phospho-specific anti-nephrin antibodies were generated and validated previously.^{45 (link)} All primary antibodies were used at 1:1000 except for podocin and β-actin, which were used at 1:5000. Secondary horseradish peroxidase-conjugated goat anti-mouse (170-6516, BioRad, Hercules, CA) and goat anti-rabbit (170-6515, BioRad) antibodies were used at 1:5000 for immunoblot detection.

Mahesaniya A., Williamson C.R., Keyvani Chahi A., Martin C.E., Mitro A.E., Lu P., New L.A., Watson K.L., Moorehead R.A, & Jones N. (2022). Sex Differences in Glomerular Protein Expression and Effects of Soy-Based Diet on Podocyte Signaling. Canadian Journal of Kidney Health and Disease, 9, 20543581221121636.

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Indirect Immunofluorescence of Cell Markers

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Indirect immunofluorescence was performed as reported [25 (link)]. Following primary antibodies were used: rabbit polyclonal antibodies against pan-cadherin (ab16505; Abcam, Cambridge, UK) and against β-hCG (SAB4500168; Sigma-Aldrich, Taufkirchen, Germany), and mouse monoclonal antibody against acetylated α-tubulin (6-11B1, T7451; Sigma-Aldrich, Taufkirchen, Germany). Cy3-conjugated secondary antibodies were obtained from Jackson Immunoresearch (Cambridgeshire, UK). DAPI (4’,6-diamidino-2-phenylindole-dihydrochloride; Roche, Mannheim, Germany) was used to stain the DNA content. All slides were examined with an AxioObserver.Z1 microscope (Zeiss, Göttingen, Germany) equipped with an AxioCam MRm camera (Zeiss, Göttingen, Germany). The immunofluorescence stained slides were further imaged with an confocal laser scanning microscopy (CLSM) as described [30 (link)].

Wildner J.M., Friemel A., Jennewein L., Roth S., Ritter A., Schüttler C., Chen Q., Louwen F., Yuan J, & Kreis N.N. (2019). RITA Is Expressed in Trophoblastic Cells and Is Involved in Differentiation Processes of the Placenta. Cells, 8(12), 1484.

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Immunohistochemical Characterization of PTPRζ

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Most chemicals were purchased from Sigma or Wako Chemicals. The following antibodies were purchased: mouse IgM anti-PTPRζ (sc-33664; Santa Cruz Biotechnology), hereinafter referred to as “anti-PTPRZ (Santa Cruz),” mouse IgM anti-chondroitin sulfate proteoglycan (MAB1581; Merck Millipore), referred to by its clone name, as “Cat-315,” mouse monoclonal anti-aggrecan (6-B-4; Abcam), rabbit polyclonal anti-PTPRZ1(HPA015103; Sigma), hereinafter referred to as “anti-PTPRZ1 (Sigma),” anti-pan cadherin (ab16505; Abcam), polyclonal sheep anti-transthyretin (ab9015; Abcam), referred to as “TTR,” horseradish peroxidase (HRP)-conjugated goat anti-mouse IgM (SAB-110; Stressgen), goat anti-rabbit IgG (NA934; GE Healthcare), and donkey anti-sheep IgG-HRP (A16041; Thermo Fisher Scientific).

Yamanoi Y., Fujii M., Murakami Y., Nagai K., Hoshi K., Hashimoto Y., Honda T., Saito K, & Kitazume S. (2020). Soluble protein tyrosine phosphatase receptor type Z (PTPRZ) in cerebrospinal fluid is a potential diagnostic marker for glioma. Neuro-oncology Advances, 2(1), vdaa055.

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Evaluating PLAUR Variant Effects

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We generated the PLAUR variants rs2302524 and rs4760 (Supplemental Figure 19) using the GeneArt site-directed mutagenesis system (Thermo Scientific) and WT PLAUR (NCBI’s RefSeqGene LRG_637 and RefSeq NG_032898.1) cloned into a pCMV6-entry vector (Origene).
Equal amounts (12 μg) of plasmid DNA encoding vector control, human reference, or the PLAUR missense variants were transfected into HEK293T cells (CRL-3216; ATCC) using the FuGENE 6 transfection reagent (E2691; Promega). The conditioned media and cells from each plate were harvested 48 hours after transfection for performing the following: (a) assess uPAR distribution with immunofluorescence staining of cells using monoclonal uPAR antibody to uPAR domain 2 (NBP2-62800, 1:400, Novusbio) and membrane marker P-cadherin (ab16505; 1:100, Abcam); (b) quantification of gene expression using real-time quantitative PCR testing; and (c) suPAR measurement in the supernatant using the Human uPAR Quantikine ELISA Kit (DUP00; R&D Systems).
We performed hydrodynamic tail-vein injection of plasmid DNA encoding reference human PLAUR (n = 5), PLAUR variant rs2302524 (n = 9), and PLAUR variant rs4760 (n = 7) in 8-week-old C57BL/6J female mice and measured serum suPAR levels 24 hours after injection using the Human uPAR Quantikine ELISA Kit.

Hindy G., Tyrrell D.J., Vasbinder A., Wei C., Presswalla F., Wang H., Blakely P., Ozel A.B., Graham S., Holton G.H., Dowsett J., Fahed A.C., Amadi K.M., Erne G.K., Tekmulla A., Ismail A., Launius C., Sotoodehnia N., Pankow J.S., Thørner L.W., Erikstrup C., Pedersen O.B., Banasik K., Brunak S., Ullum H., Eugen-Olsen J., Ostrowski S.R., Haas M.E., Nielsen J.B., Lotta L.A., Engström G., Melander O., Orho-Melander M., Zhao L., Murthy V.L., Pinsky D.J., Willer C.J., Heckbert S.R., Reiser J., Goldstein D.R., Desch K.C, & Hayek S.S. (2022). Increased soluble urokinase plasminogen activator levels modulate monocyte function to promote atherosclerosis. The Journal of Clinical Investigation, 132(24), e158788.

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Western Blot Analysis of Liver Proteins

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Protein from human liver whole cell lysates (80 μg/sample) was
separated in 10% SDS-PAGE gels and transferred to polyvinylidene
difluoride membranes. Membrane blocking and antibody application was
accomplished using 5% non-fat dry milk dissolved in phosphate-buffered
saline with 0.1% Tween-20. Primary antibodies for HNF3A/B (sc-377033)
and HNF1A (sc-10791) were acquired from Santa Cruz Biotechnology (Santa Cruz,
CA) while those for LXRα/β (ab24532) and Pan-Cadherin (ab16505)
were purchased from Abcam (Cambridge, MA). Immunoblots were imaged using
Supersignal West Femto chemiluminescent substrate (Fisher Scientific, Rockford,
IL). Densitometry was performed using ImageJ software (NIH, Bethesda, MD).

Lake A.D., Chaput A.L., Novak P., Cherrington N.J, & Smith C.L. (2016). TRANSCRIPTION FACTOR BINDING SITE ENRICHMENT ANALYSIS PREDICTS DRIVERS OF ALTERED GENE EXPRESSION IN NONALCOHOLIC STEATOHEPATITIS. Biochemical pharmacology, 122, 62-71.

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Zebrafish Protein Extraction and Immunoblotting

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Protein extraction of embryonic zebrafish and immunoblotting was carried out as described [16 (link),17 (link)]. For immunoblotting following primary antibodies were used: rabbit anti-Hdac1 (1:500, Abcam #ab33278), rabbit anti-acetyl-Histone H3 (1:1000, Millipore #06–599) rabbit anti-acetyl Histone H4 (1:1000, Abcam #ab177790). For loading control rabbit anti-Histone H3 (1:2500,Sigma/ #H0164), rabbit anti-Pan Cadherin (1:10000, Abcam #ab16505), or rabbit anti-LaminB1 (1:1000; Abcam #16048) were used. Signals were detected by chemiluminescence (anti-mouse IgG HRP-linked, anti-rabbit IgG HRP-linked, Cell Signaling #7076/#7074) using a Luminescent image analyzer (Image Quant LAS4000mini, D-79111 Freiburg, Germany).

Bühler A., Gahr B.M., Park D.D., Bertozzi A., Boos A., Dalvoy M., Pott A., Oswald F., Kovall R.A., Kühn B., Weidinger G., Rottbauer W, & Just S. (2021). Histone deacetylase 1 controls cardiomyocyte proliferation during embryonic heart development and cardiac regeneration in zebrafish. PLoS Genetics, 17(11), e1009890.

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Immunohistochemical Profiling of HCC

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After conventional paraffin embedding and sectioning (4 μm), HCC tissue samples were dewaxed with xylene, hydrated with gradient alcohol, and inactivated with 3% H₂O₂ for 10 min. 0.01 mol/L citrate sodium buffer was applied for microwave repair (pH = 6.0, 15 min). After the sections were blocked with 5% bovine serum albumin (BSA) for 20 min, they were incubated with the antibodies of anti-GRIM-19 (ab110240, Abcam, MA, USA), anti-Ki67 (ab15580, Abcam, MA, USA), anti-E-cadherin (ab16505, Abcam, MA, USA), and anti-Vimentin (ab92547, Abcam, MA, USA) at 4 ℃ overnight. The next day, the goat-anti-rabbit IgG was added and incubated at RT for 20 min. After washing with PBS, DAB was used for color development. After hematoxylin restaining, the sections were dehydrated, transparentized, mounted, and examined under a microscope. Image-Pro Plus (Media Cybem etics, America) was applied for analysis.

Huang J., Yang Y., Zhao F., Zhang Z., Deng J., Lu W, & Jiang X. (2023). LncRNA SATB2-AS1 overexpression represses the development of hepatocellular carcinoma through regulating the miR-3678-3p/GRIM-19 axis. Cancer Cell International, 23, 82.

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Immunoblotting of Membrane Transporters

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Membrane proteins (40 μg/well) or whole cell lysates (55 μg/well) were separated by SDS-PAGE and transferred to polyvinylidene difluoride membranes. Organic anion transporting polypeptide-1B1 (OATP1B1) (Progen mESL clone), OATP1B3 (gift from Dr. Bruno Hagenbuch KUMC), OATP2B1 (Santa Cruz Biotechnology sc-135099), and Sodium/Taurocholate Co-transporting Polypeptide (NTCP) (Santa Cruz Biotechnology sc-98484) antibodies were used to probe membrane proteins and MRP2 (Kamiya Biomedical Company M₂III-5 clone) antibody was used to probe whole cell lysates. Densitometry was performed using Image Lab software (Bio-Rad Laboratories). Proteins were normalized to pan-cadherin levels (Abcam ab16505).

Clarke J.D., Novak P., Lake A.D., Hardwick R.N, & Cherrington N.J. (2017). Impaired N-linked Glycosylation of Uptake and Efflux Transporters in Human Nonalcoholic Fatty Liver Disease. Liver international : official journal of the International Association for the Study of the Liver, 37(7), 1074-1081.

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Zebrafish Protein Extraction and Immunoblotting

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Protein extraction of embryonic zebrafish and immunoblotting was performed as described [47 (link)] using following primary antibodies: anti-Atrogin-1 (1:1000), mouse anti-ubiquitin (P4D1) (1:1000, cell signaling #3936S, Danvers, MA 01923, USA) monoclonal rabbit anti-p62 (1:2000, Abcam ab109012), rabbit anti-LC3 (1:2000, novusbio NB100-2331) and mouse anti-Myc (1:10000; cell signaling #2276S). For loading control mouse anti-β-actin (1:1000; Sigma-Aldrich #A5441) and rabbit anti- pan-cadherin (1:50000; Abcam #ab16505, 330 Cambridge, CB4 0FL, UK) were used. Signals were detected by chemiluminescence (anti-mouse IgG HRP-linked, anti-rabbit IgG HRP-linked, Cell signaling #7076/#7074) using a Luminescent image analyzer (Image Quant LAS4000mini, D-79111 Freiburg, Germany). Protein levels were compared by measuring the mean gray values, LC3-II and p62 protein levels of MO1-control injected embryos were normalized to 1.

Bühler A., Kustermann M., Bummer T., Rottbauer W., Sandri M, & Just S. (2016). Atrogin-1 Deficiency Leads to Myopathy and Heart Failure in Zebrafish. International Journal of Molecular Sciences, 17(2), 187.

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Membrane Protein Quantification in Mouse Liver

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Whole cell protein lysates were prepared from mouse livers as previously described [16 (link)]. Portions of the whole cell lysates were subjected to ultracentrifugation at 100,000 × g for one h to collect a membrane enriched fraction. Sixty micrograms of whole cell lysate or 30 μg of membrane preparation were separated on 7.5% SDS-PAGE gels and transferred to polyvinylidene difluoride (PVDF) membranes. The following antibodies were used for each protein: Oatp1a1, Santa Cruz Biotechnology (Santa Cruz, CA) sc-47265; Oatp1a4, sc-18436; Oatp1b2, sc-47270; Mrp2, M₂III-5 clone Kamiya Biomedical Company (Seattle, WA) MC-267; Mrp3, sc-5775; Mrp4, M₄I-10 clone generated by George L. Scheffer (Amsterdam, The Netherlands); OATP1B1, Progen Biotech (Heidelberg, Germany); OATP1B3, gift from Dr. Bruno Hagenbuch (University of Kansas Medical Center); Oatp2b1/OATP2B1 sc-135099. Relative protein levels were measured using Image J software from the National Institutes of Health (Bethesda, MD) and each protein was normalized to either Erk-2 (sc-154) or pan-cadherin (Abcam, Ab16505).

Clarke J.D., Hardwick R.N., Lake A.D., Lickteig A.J., Goedken M.J., Klaassen C.D, & Cherrington N.J. (2014). Synergistic interaction between genetics and disease on pravastatin disposition. Journal of hepatology, 61(1), 139-147.

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