Anti gapdh d16h11

Manufactured by Cell Signaling Technology

Sourced in United States

Anti-GAPDH (D16H11) is a monoclonal antibody that recognizes the GAPDH protein. GAPDH is a ubiquitously expressed enzyme involved in glycolysis. The antibody can be used to detect GAPDH expression levels in various sample types.

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Lab products found in correlation

Anti β actin 8h10d10, by Cell Signaling Technology (2 mentions) Anti iκbα l35a5, by Cell Signaling Technology (2 mentions) Anti lamin b1 d9v6h, by Cell Signaling Technology (2 mentions) Anti gfp a 11122, by Thermo Fisher Scientific (2 mentions) Mouse monoclonal anti flag f3165, by Merck Group (2 mentions) Clarity western ecl substrate, by Bio-Rad (2 mentions) Fusion fx documentation system, by Vilber (2 mentions) Hrp conjugated appropriate secondary antibodies, by Cell Signaling Technology (2 mentions) Enhanced chemiluminescent detection, by Thermo Fisher Scientific (2 mentions) Protease inhibitor, by Biosharp (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by Santa Cruz Biotechnology (1 mentions) Anti ve cadherin f 8, by Santa Cruz Biotechnology (1 mentions) Anti ki67 ab15580, by Abcam (1 mentions) Anti gm130 clone 35, by BD (1 mentions) Anti gfp d5, by Cell Signaling Technology (1 mentions) Semaxanib, by Selleck Chemicals (1 mentions) Anti β tubulin ab6046, by Abcam (1 mentions) Anti e cadherin ab1416, by Abcam (1 mentions) Rhodamine phalloidin, by Thermo Fisher Scientific (1 mentions) Recombinant human tgf β1 protein, by R&D Systems (1 mentions)

Spelling variants of this product

GAPDH (5572 citations) Anti-GAPDH (1707 citations) GAPDH (D16H11) (66 citations) Anti-GAPDH (clone D16H11) (6 citations) Rabbit anti-GAPDH (D16H11) (3 citations) GAPDH (Rabbit Anti-GAPDH (D16H11) mAb, (2 citations) Anti-GAPDH D16H11 XP (2 citations) Anti-Gapdh antibody (D16H11) (2 citations)

22 protocols using anti gapdh d16h11

Protein Expression Analysis via Western Blot

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Cell lysate was prepared with RIPA lysis buffer supplemented with 1 × protease inhibitor (70090050, Biosharp, China) and 1 × phosphatase inhibitor (70080020, Biosharp, China) at 4 °C. Western blot was performed according to the common protocol. The primary antibodies used were anti-cyclin D1 antibody (92G2, Cell Signaling Technology), anti-NRP2 antibody (D39A5, Cell Signaling Technology), anti-p21 antibody (12D1, Cell Signaling Technology) and anti-GAPDH (D16H11, Cell Signaling Technology) with a dilution of 1:1000. Anti-rabbit secondary antibody (7074S, Cell Signaling Technology) was used with a dilution of 1:3000.

Li P., Zeng Y., Chen Y., Huang P., Chen X, & Zheng W. (2022). LRP11-AS1 promotes the proliferation and migration of triple negative breast cancer cells via the miR-149-3p/NRP2 axis. Cancer Cell International, 22, 116.

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Comprehensive Immunofluorescence Staining Protocol

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Anti-VE-cadherin (F-8, 1 µg/ml) and DAPI were from Santa Cruz Biotechnology. Anti-E-cadherin (ab1416, 1 µg/ml), anti-Ki67 (ab15580, 0.25 µg/ml), and anti-β tubulin (ab6046, 0.25 µg/ml) were from Abcam. Anti-GM130 (clone 35, 2 µg/ml) was from BD Biosciences. Anti-VEGFA (VG-1, 2 µg/ml), anti-ZO-1 (40-2200, 1 µg/ml), rhodamine phalloidin (1 µg/ml), 70 kDa FITC-dextran and AlexaFluor 647 conjugated goat secondary antibodies were from Life Technologies. Anti-α6 integrin (MA6, 1 µg/ml) was from Millipore. Anti-HA (6E2, 0.5 µg/ml), anti-GFP (D5.1, 0.5 µg/ml), and anti-GAPDH (D16H11, 0.25 µg/ml) were from Cell Signaling Technologies. HRP-conjugated donkey anti-mouse and rabbit IgG secondary antibodies (1: 0.25 µg/ml) were purchased from Fitzgerald. Recombinant human IL-6 protein (7270-IL, 200 ng/ml), recombinant human TGFβ1 protein (240-B, 5 ng/ml), recombinant human FGF2 protein 2 (33-FB, 3 nM), anti-IL-6 (6708, 1 µg/ml), anti-IL-6Rα (MAB227, 0.5 µg/ml), and Proteome Profiler Human Cytokine Array Kit were purchased from R&D Systems. Semaxanib was purchased from Selleckchem.

Kutys M.L., Polacheck W.J., Welch M.K., Gagnon K.A., Koorman T., Kim S., Li L., McClatchey A.I, & Chen C.S. (2020). Uncovering mutation-specific morphogenic phenotypes and paracrine-mediated vessel dysfunction in a biomimetic vascularized mammary duct platform. Nature Communications, 11, 3377.

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Regulation of ACE2 Expression by Exosomes

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Immature DCs or mouse primary tracheal/bronchial epithelium cells (PTBECs) were incubated with and without 10⁸/ml EXO regDCs EXO, iDCs EXO in the presence or absence of TGFβ1R blocker (SB 431542, R and D, USA, endocytosis inhibitor Cytochalasin D (C8273, Sigma Aldrich, USA) and free TGFβ1 (with dose approximately matching that in regDCs EXO) for 1 h and 24 hrs. Cells were harvested and ACE2 mRNA were measured by polymerase chain reaction (PCR) while ACE2 surface markers levels were measured by flow cytometry. Phosphorylation of TGβ1 transcription factors was assessed by western blot using anti PSMAD2/3 (D6G10), anti SMAD2/3 (D7G7), with anti-GAPDH (D16H11) or anti-Beta-actin (8H10D10) as loading control (Cell Signaling Technology, Danvers, MA, USA).

Elashiry M., Elsayed R., Elashiry M.M., Rashid M.H., Ara R., Arbab A.S., Elawady A.R., Hamrick M., Liu Y., Zhi W., Lucas R., Vazquez J, & Cutler C.W. (2021). Proteomic Characterization, Biodistribution, and Functional Studies of Immune-Therapeutic Exosomes: Implications for Inflammatory Lung Diseases. Frontiers in Immunology, 12, 636222.

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PTEN Plasmid Engineering and Expression

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Human wild type (Wt), N-terminal myristoylated (myr)-tagged, and C-terminal NLS-tagged PTEN complementary DNA (cDNA) sequences were subcloned from pCDNA3-PTEN into pTRIPZ vector (Addgene, Watertown, MA, USA) with AgeI and MluI to generate PTEN expression plasmid. All plasmid constructs were confirmed by sequencing. Ampicillin, puromycin, and doxycycline were purchased from Sigma-Aldrich (St. Louis, MO, USA). Polyethylenimine (PEI) was purchased from Polysciences (Warrington, PA, USA), while RPMI, DMEM, Opti-MEM reduced serum media, and fetal bovine serum (FBS) were purchased from Thermo Fisher Scientific (Waltham, MA, USA), and Protein G Sepharose 4 Fast Flow beads were purchased from Cytiva (Malborough, MA, USA). The antibodies for Western blotting were as follows: anti-PTEN (138G6, 1:1000), anti-p-AKT (9271, 1:1000), anti-AKT (9272, 1:1000), anti-GAPDH (D16H11, 1:4000), anti-Lamin B1 (D4Q4Z, 1:1000), anti-β-Tubulin (9F3, 1:1000), and anti-EGFR (D3871, 1:1000) antibodies, all purchased from Cell Signaling Technology (Danvers, MA, USA). Anti-HSP90 (610418, 1:4000) was purchased from BD Bioscience (Franklin Lakes, NJ, USA).

Loh Z.N., Wang M.E., Wan C., Asara J.M., Ji Z, & Chen M. (2023). Nuclear PTEN Regulates Thymidylate Biosynthesis in Human Prostate Cancer Cell Lines. Metabolites, 13(8), 939.

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Western Blot Analysis of Protein Targets

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Cells were lysed in Laemmli buffer, proteins were separated on SDS-PAGE, and transferred to polyvinylidene fluoride membranes (Bio-Rad). Primary antibodies used were anti-FLAG (2368; NEB; 1:1000 dilution), anti-HA (3724; NEB; 1:1000 dilution), anti-mTOR (7C10; Cell Signaling; 1:1000 dilution), anti-DEPTOR (D9F5; Cell Signaling; 1:1000 dilution), anti-S6 (54D2; Cell Signaling; 1:1000 dilution), anti-phospho-S6^S240/244 (2215; Cell Signaling; 1:1000 dilution), anti-pan-AKT (C67E7; Cell Signaling; 1:1000), antiphospho-AKT^S473 (D9E; Cell Signaling; 1:1000 dilution), anti-ACTIN (D6A8; Cell Signaling; 1:2000 dilution) and anti-GAPDH (D16H11; Cell Signaling; 1:2000 dilution), anti-4G10 (05-321; Millipore–Sigma; 1:1000 dilution), anti-GFP (2956; Cell Signaling; 1:1000 dilution), antiubiquitin P4D1 (sc-8017; Santa Cruz; 1:1000 dilution), anti-EPHB2 D2X2I (83029; Cell Signaling; 1:1000 dilution), anti-EPHB2 (AF467; R&D Systems; 1:200 dilution), and anti-SYK D3ZE1 (13198; Cell Signaling; 1:500 dilution).

M. Gagné L., Morin N., Lavoie N., Bisson N., Lambert J.P., Mallette F.A, & Huot M.É. (2021). Tyrosine phosphorylation of DEPTOR functions as a molecular switch to activate mTOR signaling. The Journal of Biological Chemistry, 297(5), 101291.

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Western Blot Analysis of Protein Expression

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Cells modified with SB transposons were seeded in 12‐well plates. 24 h after transfection protein expression was induced by doxycycline (1 μg/mL). Next day cells were lysed in SDS Loading Buffer (0.35 M Tris·HCl, 35% (v/v) glycerol, 10% (w/v) SDS, 3.6 M β‐mercaptoethanol, 0.12 g/mL bromophenol blue) and denatured in 95°C for 7 min. Protein extracts were analyzed by Western blot. Following antibodies were used: mouse monoclonal anti‐FLAG (F3165, Merck), anti‐HA‐Tag (C29F4, Cell Signaling Technology), anti‐Lamin B1 (D9V6H, Cell Signaling Technology), anti‐GAPDH (D16H11, Cell Signaling Technology), anti‐IκBα (L35A5, Cell Signaling Technology), anti‐β‐actin (8H10D10, Cell Signaling Technology), anti‐GFP (A‐11122, Invitrogen) anti‐mouseHRP (#7076), and anti‐rabbit HRP (#7074) (Cell Signaling). Luminescence was detected using the Clarity Western ECL Substrate (Bio‐Rad) and recorded using the Fusion‐Fx documentation system (Vilber Lourmat).

Sowinska W., Wawro M., Biswas D.D., Kochan J., Pustelny K., Solecka A., Gupta A.S., Mockenhaupt K., Polak J., Kwinta B., Kordula T, & Kasza A. (2023). The homeostatic function of Regnase‐2 restricts neuroinflammation. The FASEB Journal, 37(3), e22798.

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Rad51d Knockout Impacts DNA Damage Response

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Immortalized Rad51d^+/+, Rad51d^−/−, and Rad51d^−/− Mlh1^−/− MEFs were plated in a 6-well dish at a concentration of 6 × 10⁴ cells per well and, after 24 h, treated with 50 or 100 nM 6TG (Sigma Aldrich, St. Louis, MO USA) for 48 and 72 h. Following treatment, cells were trypsinized and proteins extracted in 1X cell lysis buffer (20 mM Tris, 150 mM NaCl, 1 mM EDTA, 1 mM EGTA, 1 mM PMSF, 1% Triton X-100) containing protease inhibitor cocktail (Thermo Fisher, Waltham, MA USA). Thirty μg of whole-cell protein extracts were separated using a 4–20% gradient gel (Bio-Rad, Hercules, CA USA). Western blot analysis was performed using rabbit polyclonal anti-γ-H2AX (A300-081, Bethyl, Montgomery, TX USA) or rabbit monoclonal anti-GAPDH (D16H11, Cell Signaling, Danvers, MA USA). Primary incubations were followed with species specific IR Dye 800CW secondary antibody (Licor, Lincoln, NE USA), and signal detection was performed using a Licor Odyssey Sa Imaging System. Quantitative analysis of band intensity was performed using Image Studio software (LiCor, version 4.0, Lincoln NE, USA).

Wyatt M.D., Reilly N.M., Patel S., Rajesh P., Schools G.P., Smiraldo P.G, & Pittman D.L. (2017). Thiopurine-induced mitotic catastrophe in Rad51d-deficient mammalian cells. Environmental and molecular mutagenesis, 59(1), 38-48.

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Proliferation and Migration Assay Kit

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The EdU cell proliferation detection kit assay was purchased from RiboBio Co., Ltd. (Guangzhou, China). Cell Counting Kit-8 (CCK-8) was purchased from KeyGen Biotech Co., Ltd (Nanjing, China). LDHD protein primary antibody (K008489P) was purchased from Solarbio (Beijing, China). Anti-GAPDH (D16H11) and anti-p-Akt (Ser473) antibodies were purchased from Cell Signaling Technology (Beverly, MA, USA). The antibodies against E-cadherin (A20798), N-cadherin (A19083), MMP-9 (A0289), and MMP-2 (A6247) were the products of ABclonal Biotechnology (Wuhan, China). Horseradish peroxidase-linked anti-mouse IgG and anti-rabbit IgG secondary antibodies were purchased from Cell Signaling Technology (Beverly, MA, USA).

Wang S., Wu X., Wu X., Cheng J., Chen Q, & Qi Z. (2024). Systematic analysis of the role of LDHs subtype in pan-cancer demonstrates the importance of LDHD in the prognosis of hepatocellular carcinoma patients. BMC Cancer, 24, 156.

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Immunoblot Analysis of Apoptosis Signaling

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Following treatments, cells were washed with ice-cold PBS and lysed with RIPA buffer. For immunoblot analysis, 30 μg of each protein sample was subjected to SDS-PAGE and transferred onto a nitrocellulose membrane. Blots were exposed to anti-c-CBL (D4E10), cleaved caspase 8 (18C8), caspase 9 (C9), PLC-g1 (D9H10) and phospho-PLC-g1 (Tyr 783) primary antibodies (Cell Signaling; Beverly, MA) and HRP conjugated appropriate secondary antibodies (Cell Signaling; Danvers, MA), followed by enhanced chemiluminescent detection (Thermo Fisher Scientific, Inc., Rockford, IL) using the Fotodyne digital imaging system (Fotodyne, Hartland, WI). Loading control antibody was anti-GAPDH (D16H11; Cell Signaling; Beverly, MA). Numbers in immunoblot lanes represent scanning densitometry relative to controls.

Wu J., Salva K.A, & Wood G.S. (2014). c-CBL E3 Ubiquitin Ligase is Over-Expressed in Cutaneous T-Cell Lymphoma: Its Inhibition Promotes Activation Induced Cell Death. The Journal of investigative dermatology, 135(3), 861-868.

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Fractionation and Western Blotting Protocol

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For fractionation assays, NIH-3T3 cells were collected in ice-cold PBS, and fractionated into nuclear, cytoplasmic, and whole cell extracts by the Rapid, Efficient, and Practical (REAP) method (47). Cellular and viral proteins were detected by Western blots. Polyclonal goat anti-MLV antibody (NCI Repository) (34), anti-GAPDH (D16H11, Cell Signaling Technology/CST), anti-α-tubulin (T6074, Sigma-Aldrich), anti-lamin B1 (D4Q4Z, CST), horseradish peroxidase (HRP)-conjugated anti-rabbit (7074, CST), and (HRP)-conjugated anti-goat (A8919, Sigma-Aldrich) were used for detection, using Pierce ECL Western blotting substrate (Thermo Fisher Scientific, 32209).

Salas-Briceno K., Zhao W, & Ross S.R. (2024). Murine leukemia virus infection of non-dividing dendritic cells is dependent on nucleoporins. PLOS Pathogens, 20(1), e1011640.

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