Rabbit anti erk

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Rabbit anti-ERK is a primary antibody that specifically binds to the extracellular signal-regulated kinase (ERK) protein. ERK is a key regulator of cellular processes such as proliferation, differentiation, and survival. This antibody can be used to detect and analyze the expression and activation of ERK in various biological samples.

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Close spelling variants of this product

Anti-ERK (116 citations) Rabbit anti-TM (2 citations) Rabbit anti-phospho ERK (2 citations) Rabbit anti-total ERK (2 citations)

13 protocols using rabbit anti erk

Western Blot Analysis of Cell Signaling

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Immunoblot analysis was performed
as previously described^{58 (link)−60 (link)} using mouse anti-β-Actin,
mouse anti-p-ERK, rabbit anti-ERK, mouse anti-p-EGFR (Y1045), mouse
anti-p-EGFR (Y1148), mouse anti-p-EGFR (Y1173), mouse anti-CCND1,
mouse anti-CDK4, mouse anti-CCNB1, rabbit anti-c-MYC, mouse anti-BCL2,
mouse anti-BCL-XL, mouse anti-BAD, rabbit anti-CYCS, mouse anti-p-ERK
(44/42), and rabbit anti-ERK antibodies were procured from Santa Cruz
Biotechnology, CA. Mouse anti-CDH1, mouse anti-CDH2, rabbit anti-OCLN,
rabbit anti-pSTAT3, and mouse anti-STAT3 antibodies were obtained
from Abcam, Cambridge, MA. Rabbit anti-p-EGFR (Y992) and rabbit anti-p-CDK2
antibodies were obtained from Cell Signaling. Cell extracts were resolved
on SDS-PAGE and immunoblotted, with the appropriate and respective
antibodies. β-Actin was used as input control for cell lysate.
The sizes of the detected protein bands are shown in kilodaltons on
the left side.

Sebastian A., Pandey V., Mohan C.D., Chia Y.T., Rangappa S., Mathai J., Baburajeev C.P., Paricharak S., Mervin L.H., Bulusu K.C., Fuchs J.E., Bender A., Yamada S., B.a.s.a.p.p.a., Lobie P.E, & Rangappa K.S. (2016). Novel Adamantanyl-Based Thiadiazolyl Pyrazoles Targeting EGFR in Triple-Negative Breast Cancer. ACS Omega, 1(6), 1412-1424.

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Western Blot Analysis of ERK and STAT3 Signaling

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Proteins were separated by electrophoresis and then transferred to a nitrocellulose membrane (TCM) and blocked in 1% nonfat milk 1% BSA/Tris-buffered saline containing 0.10% Tween-20 (TBS-T pH 7.4) for 1 h at room temperature. Subsequently, the membranes were incubated overnight at 4 °C with the appropriate primary antibodies rabbit anti-ERK (Santa Cruz, sc-153) and mouse anti-pERK (Cell Signaling Technology, Danvers, MA, USA, #9106S), mouse anti-STAT3 (MA1-13,042), and rabbit anti-pSTAT3(Tyr705) (# 44-380G) (Invitrogen-Thermo Fisher Scientific, Milan, Italy) diluted 1:1000 in the blocking solution. Membranes were then incubated with an anti-mouse IgG HRP-linked secondary antibody. The immunoreactive signals were visualized using an enhanced chemiluminescence system [12 (link)].

Lattanzi R., Maftei D., Vincenzi M., Fullone M.R, & Miele R. (2022). Identification and Characterization of a New Splicing Variant of Prokineticin 2. Life, 12(2), 248.

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Protein Expression Analysis in Mouse Tissues

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Mouse tissues and cells for protein lysates were lysed in RIPA buffer, homogenized by a Tissue LyserII (Qiagen, Venlo, Netherlands) and quantified using the BCA Protein Assay Kit (Thermo Fisher Scientific). Lysates were subjected to 8% or 10% SDS-PAGE and transferred to a PVDF membrane. Protein expression was analyzed using rabbit anti-ASAP1 (ab12423, 1:2500, Abcam, Cambridge, UK), rabbit anti-FAK (06–543, 1:1000, Merck Milipore, Darmstadt, Germany), rabbit anti-phospho FAK Y397 (44-624G, 1:1000, Thermofisher), rabbit anti-Src (ab47405, 1:1000, abcam), rabbit anti-phospho Src Y416 (#6943, 1:1000, Cell Signaling), rabbit anti-phospho AKT T308 (#9275, 1:1000, Cell Signaling), rabbit anti-AKT (sc-8312, 1, 1:200, Santa Cruz), rabbit anti-ERK (sc-93, 1:200, Santa Cruz), mouse anti-phospho ERK (#9106, 1:1000, Cell Signaling), rabbit anti-p38 (sc535, 1:200, Santa Cruz), rabbit anti-phospho p38 (#4511, 1:1000, Cell Signaling). Probing the membranes with mouse anti-vinculin antibodies (V4139, 1:5000, Sigma) served as a loading control.

Schreiber C., Saraswati S., Harkins S., Gruber A., Cremers N., Thiele W., Rothley M., Plaumann D., Korn C., Armant O., Augustin H.G, & Sleeman J.P. (2019). Loss of ASAP1 in mice impairs adipogenic and osteogenic differentiation of mesenchymal progenitor cells through dysregulation of FAK/Src and AKT signaling. PLoS Genetics, 15(6), e1008216.

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Immunochemical Analysis of Neuroinflammation

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The following primary antibodies were used throughout this study: rat anti-mouse CD11b (1:400, Abcam), rabbit anti-F-actin (1:1000, Abcam), rabbit anti-COX-2 (1:1000, Abcam), rabbit anti-IL-1β (1:200, Abcam), rabbit anti-GFAP (1:5000, Neuromics), rabbit anti-Iba-1 (1:1000, Wako), goat anti-Iba-1 (1:500, Wako), rabbit anti-AKT (1:1000, Santa Cruz), rabbit anti-p-AKT (Ser473, Thr308) (1:1000, Cell Signaling), rabbit anti-ERK (1:1000, Santa Cruz), rabbit anti-p-ERK (Thr42/44) (1:1000, Cell Signaling), rabbit anti-STAT3 (1:1000, Cell Signaling), rabbit anti-p-STAT3 (Ser727, Abcam), mouse anti-PCNA (1:1000, Santa Cruz), rabbit anti-D2R (1:1000, Abcam), and rabbit anti-D1R (1:1000, Millipore) antibodies. We used the following small molecules: D1R antagonists (LE300, 10 μM, Sigma-Aldrich; SCH23390, 30 μM, Tocris), D1R agonist (A77636 hydrochloride, 10 nM, Tocris), D2R antagonist (eticlopride hydrochloride, 100 nM, Sigma-Aldrich), a STAT3 inhibitor (S3I-201, 50 μM, Sigma-Aldrich), and an ERK inhibitor (PD98059, 10 μM, Millipore).

Lee J.Y., Nam J.H., Nam Y., Nam H.Y., Yoon G., Ko E., Kim S.B., Bautista M.R., Capule C.C., Koyanagi T., Leriche G., Choi H.G., Yang J., Kim J, & Hoe H.S. (2018). The small molecule CA140 inhibits the neuroinflammatory response in wild-type mice and a mouse model of AD. Journal of Neuroinflammation, 15, 286.

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Comprehensive Antibody Immunostaining Protocol

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The primary antibodies used were mouse anti-GFP (Invitrogen—1:1000), rabbit anti-GFP (Abcam—1:5000), chicken anti-GFP (Millipore—1:1000), mouse anti-SatB2 (Abcam—1:400), mouse anti-βIII-tubulin (Covance—1:1000), rabbit anti-βIII-tubulin (Covance—1:1000), rabbit anti-Pax6 (Covance—1:2000), mouse anti-Pax6 (Abcam—1:250), rabbit anti-GAPDH (Sigma—1:1000), rabbit anti-Tbr2 (Abcam—1:500), rabbit anti-Erk (Santa Cruz Biotechnology—1:1000), rabbit anti-Notch1 (Abcam—1:250), rabbit anti-RFP (MBL—1:1000), mouse anti-Actin (Sigma—1:2000), mouse anti-MG-H1 (Cell Biolabs—1:50), mouse anti-GAPDH (Abcam—1:1000), rabbit anti-GLO1 (Abcam 1:500), mouse anti-puromycin (Kerafast—1:1000). The donkey anti-mouse and anti-rabbit Alexa 488, 555 and 647-conjugated secondary antibodies were obtained from ThermoFisher and used at 1:500 dilutions. HRP-conjugated goat anti-mouse, anti-rabbit or anti-chicken secondary antibodies were purchased from ThermoFisher and used at 1:5000 dilutions. NIR-conjugated goat anti-mouse and anti-rabbit secondary antibodies were acquired from LI-COR and used at 1:25,000 dilutions.

Rodrigues D.C., Harvey E.M., Suraj R., Erickson S.L., Mohammad L., Ren M., Liu H., He G., Kaplan D.R., Ellis J, & Yang G. (2020). Methylglyoxal couples metabolic and translational control of Notch signalling in mammalian neural stem cells. Nature Communications, 11, 2018.

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Detailed Western Blot Procedure

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Western blot was performed as reported in Fullone et al. 2022 [5 (link)]. The following primary antibodies were used at a dilution of 1:1000 in the blocking solution: rabbit anti-ERK (Santa Cruz Biotechnology, Dallas, TX, USA, sc-153), mouse anti-p-ERK (Cell Signaling Technology, Danvers, MA, USA, 9106S), monoclonal anti polyhistidine peroxidase (Sigma-Aldrich, MERCK, Darmstadt, Germany A7058), rabbit anti-MRAP2 polyclonal antibody (Invitrogen-Thermo Fisher Scientific, Waltham, MA, USA, PA5-113283), mouse anti-PKR2 polyclonal antibody (Santa Cruz Biotechnology, Dallas, TX, USA, sc-365696), mouse anti-STAT3, and rabbit anti-pSTAT3 (Tyr705) (1:1000, Invitrogen, Thermo Fisher Scientific, Waltham, MA, USA). After extensive washing with T-TBS, membranes were incubated with the appropriate IgG HRP-linked secondary antibody for 1 h at room temperature. The immunoreactive signals were visualized using an enhanced chemiluminescence system.

Fullone M.R., Maftei D., Vincenzi M., Lattanzi R, & Miele R. (2022). Arginine 125 Is an Essential Residue for the Function of MRAP2. International Journal of Molecular Sciences, 23(17), 9853.

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Bladder Cancer Cell Lines and ERK Pathway Inhibition

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The RT-4, BI-87,253 J, SV-HUC-1, T24 and J82 human bladder tumor cell lines were purchased from China Academia Sinica Cell Repository (Shanghai, China; www.cellbank.org.cn). T24, RT-4, and 253 J cells were cultured in RPMI 1640 (cat. no. 22400-089; Gibco; Thermo Fisher Scientific, Inc., Waltham, MA, USA) supplemented with 10% fetal calf serum (Gibco; Thermo Fisher Scientific, Inc.). J82 cells were maintained in Opti-Minimal Essential Medium^® I (cat. no. 51985-042; Gibco; Thermo Fisher Scientific, Inc.) containing 10% fetal calf serum (Gibco; Thermo Fisher Scientific, Inc.). SV-HUC-1 cells were cultured in F12K medium (cat. no. N3520; Sigma-Aldrich; Merck Millipore) supplemented with 10% fetal calf serum (Gibco; Thermo Fisher Scientific, Inc.) All cells were cultured in a humidified incubator at 37°C and 5% CO₂. The following antibodies were used: Anti-B23 (cat. no. 10306-1-AP; Proteintech Group, Inc., Rosemont, USA), mouse anti-GAPDH (cat. no. sc-32233; Santa Cruz Biotechnology, Inc., Dallas, TX, USA), rabbit anti-ERK (cat. no. 4372S; Cell Signaling Technology, Inc., Danvers, MA, USA) and rabbit anti-phosphorylated (p)-ERK1/2 (cat. no. 4370S; Cell Signaling Technology, Inc.). U0126 (cat. no. 9903; Cell Signaling Technology, Inc.) was selected as the mitogen activated protein kinase (MAPK)/ERK inhibitor and the cells were treated with 2 µM U0126 for 1, 2, 3 days at 37°C.

Wang H., Yuan G., Zhao B., Zhao Y, & Qiu Y. (2016). High expression of B23 is associated with tumorigenesis and poor prognosis in bladder urothelial carcinoma. Molecular Medicine Reports, 15(2), 743-749.

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Platelet Activation Signaling Proteins

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Bovine thrombin and bovine serum albumin (BSA) were purchased from Sigma (St. Louis, MO, USA). Mouse anti-p-ERK, rabbit anti-ERK, goat anti-AKT1/2, and rabbit anti-p-AKT1 antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Rabbit anti-CD41 antibody was obtained from Abcam (Cambs., UK). Horseradish peroxidase- (HRP-) labeled goat anti-mouse immunoglobulin G (IgG), goat anti-rabbit IgG, and rabbit anti-goat IgG antibodies were obtained from Jackson Immuno Research (West Grove, PA, USA). R-phycoerythrin- (R-PE-) conjugated goat anti-rabbit IgG (H + L) was acquired from Proteintech (Chicago, USA). Fluorescein isothiocyanate- (FITC-) conjugated anti-CD61 antibody was purchased from eBioscience (CA, USA).

Yang X.L., Ge M.K., Mao D.K., Lv Y.T., Sun S.Y, & Yu A.P. (2016). Thrombin Maybe Plays an Important Role in MK Differentiation into Platelets. BioMed Research International, 2016, 9313269.

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Murine Lung Protein Signaling Analysis

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Murine lung explants were lysed in buffer containing 50 mM Tris-HCl, 150 mM NaCl, 1% Nonidet P40, 1 mM sodium vanadate, 1 mM sodium molybdate, 10 mM sodium fluoride, 40 µg/ml PMSF, 0.7 µg/ml pepstatin A, 10 µg/ml aprotinin, 10 µg/ml leupeptin and 10 µg/ml soybean trypsin inhibitor. Samples were then diluted in sample buffer containing 5% β-mercaptoethanol, boiled, and separated by electrophoresis on a 10% SDS–PAGE gel. Proteins were subsequently transferred to a nitrocellulose membrane and probed with either rabbit anti-phospho-Akt (Ser473) (Cat No: 4060S; Cell Signaling), rabbit anti phospho-S6 ribosomal protein (Ser235/236)(Cat No: 2211S; Cell Signaling), rabbit anti-Akt (Cat No: 9272; Cell Signaling) or rabbit anti-ERK (Cat No: SC-93; Santa Cruz, Middlesex, UK). Membranes were then incubated in an HRP-conjugated goat anti-rabbit secondary antibody (DAKO) before bands were visualised using an EZ-ECL chemiluminescence detection kit (Geneflow, Staffordshire, UK) with an ImageQuant developer (GE healthcare, Buckinghamshire, UK).

Carter E., Miron-Buchacra G., Goldoni S., Danahay H., Westwick J., Watson M.L., Tosh D, & Ward S.G. (2014). Phosphoinositide 3-Kinase Alpha-Dependent Regulation of Branching Morphogenesis in Murine Embryonic Lung: Evidence for a Role in Determining Morphogenic Properties of FGF7. PLoS ONE, 9(12), e113555.

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Immunoblotting Assay for Rac1 Activation

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The following primary Abs were used: mouse anti-Rac1 (Millipore), mouse anti-active Rac (NewEast Biosciences), rabbit anti–pY507-Lyn (Epitomics), rabbit anti–pY416-Src (Cell Signaling Technology; cross reacts with pY396-Lyn), rabbit anti–pY527-Src (Cell Signaling Technology; cross reacts with pY528-Fyn), anti-Fyn (Santa Cruz Biotechnology), rabbit anti-Vav1 (C-14; Santa Cruz Biotechnology), rabbit anti-ERK (Santa Cruz Biotechnology), mouse anti–β-actin (Santa Cruz Biotechnology), anti-tubulin (Sigma-Aldrich), mouse anti-pY99 (Santa Cruz Biotechnology), rabbit anti-SHP2 (Santa Cruz Biotechnology), and rabbit anti-Lyn (Santa Cruz Biotechnology). Secondary Abs were Alexa Fluor 488–conjugated goat anti-mouse IgG (Invitrogen) and Alexa Fluor 568–conjugated goat anti-rabbit IgG (Invitrogen). Other reagents included the following: recombinant murine SCF (PeproTech), CellTracker Green and CellTracker Orange (Invitrogen), bovine fibronectin (Roche Diagnostics), and tetramethylrhodamine isothiocyanate (TRITC)– and Alexa Flour 488–conjugated phalloidin (Invitrogen).

Sharma N., Everingham S., Ramdas B., Kapur R, & Craig A.W. (2014). SHP2 Phosphatase Promotes Mast Cell Chemotaxis toward Stem Cell Factor via Enhancing Activation of the Lyn/Vav/Rac Signaling Axis. Journal of immunology (Baltimore, Md. : 1950), 192(10), 4859-4866.

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