- 71-8000 - Invitrogen Antibodies MET antibody

Submitted references Cabozantinib inhibits AXL- and MET-dependent cancer cell migration induced by growth-arrest-specific 6 and hepatocyte growth factor.

Hara T, Kimura A, Miyazaki T, Tanaka H, Morimoto M, Nakai K, Soeda J
Biochemistry and biophysics reports 2020 Mar;21:100726

Oncogene-dependent function of BRG1 in hepatocarcinogenesis.

Wang P, Song X, Cao D, Cui K, Wang J, Utpatel K, Shang R, Wang H, Che L, Evert M, Zhao K, Calvisi DF, Chen X
Cell death & disease 2020 Feb 4;11(2):91

Absent and abundant MET immunoreactivity is associated with poor prognosis of patients with oral and oropharyngeal squamous cell carcinoma.

De Herdt MJ, Willems SM, van der Steen B, Noorlag R, Verhoef EI, van Leenders GJ, van Es RJ, KoljenoviÄ S, Baatenburg de Jong RJ, Looijenga LH
Oncotarget 2016 Mar 15;7(11):13167-81

Ovarian cancer ascites enhance the migration of patient-derived peritoneal mesothelial cells via cMet pathway through HGF-dependent and -independent mechanisms.

Matte I, Lane D, Laplante C, Garde-Granger P, Rancourt C, Piché A
International journal of cancer 2015 Jul 15;137(2):289-98

p38 MAPK signaling underlies a cell-autonomous loss of stem cell self-renewal in skeletal muscle of aged mice.

Bernet JD, Doles JD, Hall JK, Kelly Tanaka K, Carter TA, Olwin BB
Nature medicine 2014 Mar;20(3):265-71

Satellite cell number and cell cycle kinetics in response to acute myotrauma in humans: immunohistochemistry versus flow cytometry.

McKay BR, Toth KG, Tarnopolsky MA, Parise G
The Journal of physiology 2010 Sep 1;588(Pt 17):3307-20

Normalization of wound healing and diabetic markers in organ cultured human diabetic corneas by adenoviral delivery of c-Met gene.

Saghizadeh M, Kramerov AA, Yu FS, Castro MG, Ljubimov AV
Investigative ophthalmology & visual science 2010 Apr;51(4):1970-80

Acquisition of biologically relevant gene expression data by Affymetrix microarray analysis of archival formalin-fixed paraffin-embedded tumours.

Linton KM, Hey Y, Saunders E, Jeziorska M, Denton J, Wilson CL, Swindell R, Dibben S, Miller CJ, Pepper SD, Radford JA, Freemont AJ
British journal of cancer 2008 Apr 22;98(8):1403-14

c-MET expression level in primary colon cancer: a predictor of tumor invasion and lymph node metastases.

Takeuchi H, Bilchik A, Saha S, Turner R, Wiese D, Tanaka M, Kuo C, Wang HJ, Hoon DS
Clinical cancer research : an official journal of the American Association for Cancer Research 2003 Apr;9(4):1480-8

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Supportive validation

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Experimental details: Immunohistochemistry analysis of c-Met showing staining in the cytoplasm and membrane of paraffin-embedded human lung adenocarcinoma (right) compared to a negative control without primary antibody (left). To expose target proteins, antigen retrieval was performed using 10mM sodium citrate (pH 6.0), microwaved for 8-15 min. Following antigen retrieval, tissues were blocked in 3% H2O2-methanol for 15 min at room temperature, washed with ddH2O and PBS, and then probed with a c-Met Rabbit Polyclonal Antibody (Product # 71-8000) diluted in 3% BSA-PBS at a dilution of 1:20 overnight at 4°C in a humidified chamber. Tissues were washed extensively in PBST and detection was performed using an HRP-conjugated secondary antibody followed by colorimetric detection using a DAB kit. Tissues were counterstained with hematoxylin and dehydrated with ethanol and xylene to prep for mounting.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Immunohistochemistry analysis of c-Met showing staining in the cytoplasm and membrane of paraffin-embedded human liver tissue (right) compared to a negative control without primary antibody (left). To expose target proteins, antigen retrieval was performed using 10mM sodium citrate (pH 6.0), microwaved for 8-15 min. Following antigen retrieval, tissues were blocked in 3% H2O2-methanol for 15 min at room temperature, washed with ddH2O and PBS, and then probed with a c-Met Rabbit Polyclonal Antibody (Product # 71-8000) diluted in 3% BSA-PBS at a dilution of 1:20 overnight at 4°C in a humidified chamber. Tissues were washed extensively in PBST and detection was performed using an HRP-conjugated secondary antibody followed by colorimetric detection using a DAB kit. Tissues were counterstained with hematoxylin and dehydrated with ethanol and xylene to prep for mounting.

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Flow cytometry analysis of c-Met was done on A549 cells. Cells were fixed with 70% ethanol for 10 minutes, permeabilized with 0.25% Tritonª X-100 for 20 minutes, and blocked with 5% BSA for 30 minutes at room temperature. Cells were labeled with ABfinityª c-Met Recombinant Rabbit Polyclonal Antibody (718000, red histogram) or with rabbit isotype control (pink histogram) at 3-5 µg/million cells in 2.5% BSA. After incubation at room temperature for 2 hours, the cells were labeled with Alexa Fluor¨ 488 Goat Anti-Rabbit Secondary Antibody (A11008) at a dilution of 1:400 for 30 minutes at room temperature. The representative 10,000 cells were acquired and analyzed for each sample using an Attune¨ Acoustic Focusing Cytometer. The purple histogram represents unstained control cells and the green histogram represents no-primary-antibody control.

Supportive validation

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Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: NULL

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 4 Illustration of cmet immunostaining and computerised image analysis detection of immunostained features in a case of synovial sarcoma. ( A ) Immunopositive areas are dark grey (SG chromogen) and background is light grey, ( B ) computer detected features are marked with blue overlay, which confirms excellent detection of immunopositive areas shown in A.

Supportive validation

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Experimental details: Figure 6 Partial p38alphabeta MAPK inhibition rescues aged SC engraftment ( a-c ) ( a ) Schematic for heterochronic myofiber transplantation into young host muscles after overnight treatment with 10 muM SB203580 or FGF-2 (control). ( b ) Images of donor-derived SCs (^ = GFP + /c-Met + ) in muscle sections 30 d post-transplantation. Scale bar, 5 mum. ( c ) Average number of donor-derived SCs per field (Mean +- s.e.m. n = 3 transplant recipients. * P < 0.05 for Aged Control vs.SB treated, Young vs. Aged Control, two-way ANOVA). ( d ) Model. Asymmetric p38alphabeta MAPK activation promotes self-renewal in young SCs generating a quiescent daughter and a lineage committed daughter cell. Elevated pp38 in aged cells prevents asymmetric p38alphabeta MAPK signal transduction generating two lineage committed daughter cells. Partial inhibition of p38alphabeta MAPK permits asymmetric p38alphabeta MAPK activation, restoring self-renewal in aged SCs. Ectopic activation of constitutively expressed iFR1 re-localizes iFR1 into an asymmetric signaling complex promoting asymmetric localization of active iFR1, resulting in asymmetric activation of p38alphabeta MAPK and self-renewal.

Supportive validation

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Experimental details: Supplementary Figure 12

Supportive validation

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Experimental details: Fig. 2 GAS6- and HGF-induced migration depends on AXL and MET, respectively, in SKOV3 cells. A. Phosphorylation of AXL and MET was induced by GAS6 and HGF, respectively, in SKOV3 cells. Cells were treated with GAS6 (100 ng/mL) or HGF (100 ng/mL) for 10 and 30 min after serum starvation overnight. AXL, pAXL, MET, and pMET levels were determined via immunoblot analysis. B. Knockdown of AXL and MET via siRNA in SKOV3 cells. Cells were treated with siRNAs against AXL, or MET, or AXL and MET together for 72 h and AXL, pAXL, MET, and pMET levels were determined via immunoblot analysis. C. KD of AXL or MET individually and in combination suppressed GAS6-, HGF-, and combinatorial GAS6- and HGF-induced cell migration to baseline levels, respectively. Cells were treated with siRNA via reverse transfection for 24 h, followed by an additional 24 h of serum starvation. Thereafter, cells were plated into the upper chambers of Boyden chambers in serum-free medium, with GAS6 (100 ng/mL), HGF (100 ng/mL), or both GAS6 (100 ng/mL) and HGF (100 ng/mL) in serum-free medium in the lower chambers. After 24 h, the cells that had migrated to the lower chambers were enumerated as described in the Materials and Methods. The data represent the mean values. Bars, +SE. n = 4. **, P < 0.01; ***, P < 0.001 vs siNC (negative control), unless otherwise indicated, by Dunnett's test. Fig. 2

Supportive validation

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Experimental details: Fig. 3 GAS6- and HGF-induced migration was inhibited by cabozantinib in SKOV3 cells. A. Cells were serum-starved overnight and then treated with cabozantinib (0.1, 1, and 10 muM) or capmatinib (0.1, 1, and 10 muM) for 10 min, followed by treatment with GAS6 (100 ng/mL) and HGF (100 ng/mL) together for 10 min. AXL, pAXL, MET, pMET, AKT, pAKT, SRC, pSRC, ERK, and pERK levels were determined via immunoblot analysis. B -D. Cells were serum-starved overnight and then seeded into the upper Boyden chambers in serum-free medium with serum-free medium, GAS6 (100 ng/mL) (B), HGF (100 ng/mL) (C), or both GAS6 (100 ng/mL) and HGF (100 ng/mL) (D) in the lower chambers. DMSO, cabozantinib (0.1 and 1 muM) or capmatinib (0.1 and 1 muM) were added to both the upper and lower chambers. After 24 h, cells that had migrated to the lower chambers were enumerated as described in the Materials and Methods. The data represent the mean values. Bars, +SE. n = 3-4. **, P < 0.01; ***, P < 0.001 vs DMSO control by Dunnett's test. ##, P < 0.01; ###, P < 0.001 vs GAS6/HGF (-) control by Student t -test. Fig. 3

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