The following antibodies were obtained from Cell Signaling (Boston, MA, USA): c-Myc (D84C12, #12189); cleaved-caspase-3 (D3E9, #8172); cleaved-PARP (D64E10, #5625); cyclin D (92G2, #2978); E-cadherin (#3195); N-cadherin (D4R1H, #13116); MMP2 (D8N9Y, #13132); MMP9 (D6O3H, #13667); and GAPDH (D16H11, #5174). The following reagents were utilized: Lipofectamine 3000 transfection reagent (Lot. 11668-027 Invitrogen, Carlsbad, CA, USA) and RIPA lysis buffer (Lot. 89901, Thermo Scientific, USA). The pcDNA3.1-OTUB1-isoform 2 construct was constructed by Hanhen Co. Ltd. (Shanghai, China).
Mmp2 d8n9y
Manufactured by Cell Signaling Technology
Sourced in United States
MMP2 (D8N9Y) is a recombinant protein product from Cell Signaling Technology. It is a member of the matrix metalloproteinase (MMP) family and is involved in the breakdown of extracellular matrix components.
Automatically generated - may contain errors
Lab products found in correlation
Ripa lysis buffer, by Thermo Fisher Scientific (1 mentions)
Cleaved caspase 3 d3e9, by Cell Signaling Technology (1 mentions)
Gapdh, by Cell Signaling Technology (1 mentions)
E cadherin, by Cell Signaling Technology (1 mentions)
Lipofectamine 3000 transfection reagent, by Thermo Fisher Scientific (1 mentions)
Cleaved parp d64e10, by Cell Signaling Technology (1 mentions)
C myc d84c12, by Cell Signaling Technology (1 mentions)
N cadherin d4r1h, by Cell Signaling Technology (1 mentions)
Pvdf membrane, by Thermo Fisher Scientific (1 mentions)
Nupage, by Thermo Fisher Scientific (1 mentions)
Anti β actin, by Cell Signaling Technology (1 mentions)
Anti α tubulin, by Cell Signaling Technology (1 mentions)
2 protocols using mmp2 d8n9y
1
OTUB1-Mediated Apoptosis Regulation
2
Western Blot Analysis of MMP-2 Expression
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Culture dishes were harvested for protein analysis as previously described [9] (link). Protein from cell lysates were separated by NuPAGE (Bis-Tris) gels and transferred to PVDF membranes (Invitrogen), blocked with 5% nonfat dry milk dissolved in Tris-Buffered saline, and incubated overnight with primary antibodies at 4°C. Immunoreactive proteins were detected by chemiluminescence with Thermo Scientific SuperSignal (Pierce Biotechnology; IL, USA). Primary antibodies included MMP-2 (D8N9Y) and housekeeping genes anti-b-actin, and anti-a-tubulin (Cell Signaling Technologies; Danvers, MA, USA). Densitometric analyses of protein was completed using the ImageJ software (NIH). Band intensity of proteins were divided by the band intensity of their internal control for normalization. Data are expressed as relative protein expression (fold change Δ; mean ± SEM) and AA HUVEC data are compared to basal expression of CA HUVEC (referent control).
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