Xcell surelock mini cell

Manufactured by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Spain

The XCell SureLock Mini-Cell is a compact, self-contained electrophoresis system designed for small-scale protein or nucleic acid separation. It features a pre-assembled tank and lid for easy setup and operation. The system accommodates mini-gels up to 8.6 cm x 6.8 cm in size.

Automatically generated - may contain errors

Lab products found in correlation

Close spelling variants of this product

XCell SureLock Mini-Cell Electrophoresis System (55 citations) XCell SureLock Mini-Cell system (53 citations) XCell SureLock (23 citations) Novex XCell SureLock Mini-Cell system (5 citations) XCell SureLock Mini-Cell apparatus (3 citations) XCell SureLock Mini-Cell Units (3 citations) XCell SureLock Mini-Cell PowerEase 200 system (2 citations) XCell Surelock Novex Mini- Cell (2 citations) XCell SureLock® Mini-Cell precast system (2 citations) XCell Surelock Mini-Cell gel tank (2 citations)

102 protocols using xcell surelock mini cell

Analytical Characterization of Antibody Charge Isoforms

Check if the same lab product or an alternative is used in the 5 most similar protocols

EXAMPLE 6

Analytical Cation Exchange Analysis to characterize and determine proportion of charged isoforms was carried out on a MabPac SCX-10 3 μm, 4×50 mm, column (Thermofisher) at 0.5 ml min⁻¹with MES pH 5.6 buffer using salt gradient elution on an Ultimate 3000 HPLC (Dionex) with detection by UV at 280 nm.

Isoelectric Focusing was carried out using non-equilibrium pH gel electrophoresis using IEF 3-10 precast gels (Serva) run in a XCell Surelock Mini-Cell (Invitrogen) with BIO-RAD Power Pac HV and stained with SimplyBlue SafeStain (Invitrogen)

SDS PAGE was carried out on NuPAGE Novex Bis-Tris 4-12% gels (Invitrogen) run in a XCell Surelock™ Mini-Cell (Invitrogen) with BIO-RAD Power Pac HV, MOPs buffer, and stained with SimplyBlue™ SafeStain (Invitrogen). For analysis samples were diluted with loading buffer, NuPAGE LDS (Invitrogen) and for reducing SDS PAGE additionally reduced with DTT.

For Western Blots sample are first separated by non-reducing SDS PAGE, NuPAGE Novex Bis-Tris 4-12% gels (Invitrogen) run in a XCell Surelock Mini-Cell (Invitrogen) with BIO-RAD Power Pac HV, MOPs buffer, transferred to a PVDF membrane and detected using anti-human Kappa light chain AP; e.g. Sigma, Cat. No. K4377. Bound detection antibody is developed using a AP conjugate kit, Cat. No. 170-6432, Biorad.

US10941207B2. Fusion protein comprising three binding domains to 5T4 and CD3 (2021-03-09). BIOTECNOL LIMITED [GB]. Inventors: Nico Mertens [BE], Philip Jeffrey Cunnah [PT], Ana Rita Da Fonseca Ricardo [PT].

+ Open protocol

+ Expand

Northern Blot Analysis of Bacterial RNA

Check if the same lab product or an alternative is used in the 5 most similar protocols

Total RNA (1 µg, originated from 2 × 10⁶ CFU) was separated on a 6% denaturing polyacrylamide gel (Novex precast 6% TBE‐Urea polyacrylamide gel, Invitrogen™) run in a XCell SureLock™ Mini‐Cell (Invitrogen™) according to manufacturer's protocols. Prestained molecular weight markers (DynaMarker DM270; BioDynamics Laboratory Inc.) were separated alongside Mk total RNA and the 100‐bp hybridization probe fragment (see below), which was used as reference for maker size calibration. After electrophoresis, the gel was electroblotted onto a nylon membrane (Amersham Hybond N+; GE Healthcare Life Sciences) using a XCell SureLock™ Mini‐Cell Blot Module (Invitrogen™) in the XCell SureLock™ Mini‐Cell according to manufacturer's instructions and subsequently baked for 2 hr at 80°C. An Mk B11‐specific DIG‐labeled hybridization probe (100 bp; genome coordinates 2810109–2810208) was generated by PCR amplification using primers CB9c3 and CB8c and a PCR DIG‐labeled probe synthesis kit (F. Hoffmann‐La Roche, Ltd.) according to manufacturer's instructions. The probe was used for the hybridization analysis following reported protocols (Quadri et al., 1994; Sambrook & Russell, 2001) and visualized by chromogenic detection using a DIG‐labeled nucleic acid detection kit (F. Hoffmann‐La Roche, Ltd.) according to the DIG Application manual (F. Hoffmann‐La Roche, Ltd.).

Budell W.C., Germain G.A., Janisch N., McKie‐Krisberg Z., Jayaprakash A.D., Resnick A.E, & Quadri L.E. (2020). Transposon mutagenesis in Mycobacterium kansasii links a small RNA gene to colony morphology and biofilm formation and identifies 9,885 intragenic insertions that do not compromise colony outgrowth. MicrobiologyOpen, 9(4), e988.

+ Open protocol

+ Expand

1-DE Analysis of Vipera Venoms

Check if the same lab product or an alternative is used in the 5 most similar protocols

1-DE analysis of V. ursinii ssp. and V. a. ammodytes venoms was performed on 4–12% Bis-Tris precast gels with MES as running buffer, under both reducing and non-reducing conditions at 180 V for 50 min in an Xcell SureLock Mini-Cell, according to the manufacturer’s instructions (Invitrogen, Carlsbad, CA, USA). A total of 40 µg of respective venom was applied in each well. Molecular mass standards were from Invitrogen. Protein staining was carried out with CBB R250. For Western blots (WB) following SDS-PAGE analysis, venoms were electro-blotted to the PVDF membrane (GE Healthcare, Buckinghamshire, UK) in an Xcell Sure Lock Mini Cell according to the manufacturer’s procedure (Invitrogen, Carlsbad, CA, USA). The blocking was performed with 2% (m/v) BSA in PBS/T buffer at +4 °C overnight. The blotted membrane was incubated first with anti-Atx serum (diluted 20,000-fold) and then with HRP-anti-rabbit IgG (diluted 10,000-fold) at 37 °C for 1 h. The Enhanced ChemiLuminescence (ECL) plus Western Blotting Detection System was used for detection, according to the manufacturer’s instructions (GE Healthcare, Buckinghamshire, UK).

Lang Balija M., Leonardi A., Brgles M., Sviben D., Kurtović T., Halassy B, & Križaj I. (2020). Biological Activities and Proteomic Profile of the Venom of Vipera ursinii ssp., a very Rare Karst Viper from Croatia. Toxins, 12(3), 187.

+ Open protocol

+ Expand

Protein Gel Electrophoresis and Western Blotting

Check if the same lab product or an alternative is used in the 5 most similar protocols

Protein gel electrophoresis was routinely conducted using NuPAGE Novex Pre-Cast Bis-Tris gels (generally 4–12% gels, 1.5 mm, 10 wells) and the XCell SureLock Mini-Cell (both Invitrogen) if not stated otherwise. Protein detection was after transfer to nitrocellulose with appropriate antibodies and SuperSignal West Dura Extended Duration Chemiluminescent Substrate (Pierce) according to the supplier’s instructions. Signals were detected using the Molecular Imager ChemiDoc XRS System (BioRad; CCD camera detection) evaluated/quantified with the ImageLab software (BioRad). Rabbit polyclonal sera against prepro alpha factor, CPY, Sec61p N-terminus & Sec61p C-terminus had been raised in our lab, and were used at 1:2000; anti-FLAG M2 monoclonal mouse (Sigma) and polyclonal rabbit (Sigma) were used at 1:2000; polyclonal rabbit anti-HA (Sigma) at 1:5000; goat anti-rabbit HRP (Rockland) as secondary antibody 1:20,000 using chemiluminescence reagents (Pierce).

Kaiser M.L, & Römisch K. (2015). Proteasome 19S RP Binding to the Sec61 Channel Plays a Key Role in ERAD. PLoS ONE, 10(2), e0117260.

+ Open protocol

+ Expand

Western Blot Protein Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

Total cellular proteins were obtained by detergent lysis. Samples (50 μg) were boiled in an equal volume of sample buffer (20% glycerol, 4% SDS, 0.2% Bromophenol Blue, 125 mM Tris-HCl (pH 7.5), and 640 mM 2-mercaptoethanol) and separated on pre-casted Tris-glycine polyacrylamide gels (6–10%) using the XCell Surelock^™ Mini-Cell, in Tris-Glycine SDS running buffer, all from Novex (Invitrogen, Carlsbad, CA). Proteins resolved on the gels were transferred to nitrocellulose membranes, which were then probed with protein specific antibody or anti-β-actin antibody as loading control. Immune complexes were visualized by chemiluminescence. Protein band densities were analyzed using the NIH/Scion image analysis software and normalized to the corresponding β-actin band densities.

Gao X., Liu Y., Deeb D., Arbab A.S, & Gautam S.C. (2014). Anticancer activity of pristimerin in ovarian carcinoma cells is mediated through the inhibition of prosurvival Akt/NF-κB/mTOR Signaling. Journal of experimental therapeutics & oncology, 10(4), 275-283.

+ Open protocol

+ Expand

Phosphatase Assay with Phos-tag SDS-PAGE

Check if the same lab product or an alternative is used in the 5 most similar protocols

SDS-PAGE gels (7%) were supplemented with Phos-tag AAL solution (Wako) according to manufacturer’s recommendations. Gels were run at 100V in an XCELL SureLOCK Mini-Cell (Invitrogen) until the dye front completely exited the gel. Gels were incubated in transfer buffer supplemented with 1 mM EDTA for 10 minutes. Gels were then soaked in normal transfer buffer for 10 minutes. Proteins were transferred to a nitrocellulose membrane and standard western blotting procedures were subsequently followed.
For lambda phosphatase treatments, lysates were generated as described in the co-immunoprecipitation assays. 50 μL of lysate was mixed with 10X MnCl₂ buffer and 10X reaction buffer provided with the lambda protein phosphatase kit (NEB). Samples treated with enzyme received 1 μL of purified lambda protein phosphatase. Incubations were performed for 45 minutes at 30°C, and samples were subjected to chloroform-methanol precipitation⁴¹ prior to phos-tag electrophoresis.

Golden R.J., Chen B., Li T., Braun J., Manjunath H., Chen X., Wu J., Schmid V., Chang T.C., Kopp F., Ramirez-Martinez A., Tagliabracci V.S., Chen Z.J., Xie Y, & Mendell J.T. (2017). An Argonaute phosphorylation cycle promotes microRNA-mediated silencing. Nature, 542(7640), 197-202.

+ Open protocol

+ Expand

Western Blotting for OXPHOS and GAPDH

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Western blotting was performed as previously described (17 (link),20 (link)). The cells were lysed in lysis buffer (20 mM Tris-HCl, 150 mM NaCl, 2 mM EDTA and 1% Triton X-100) containing a protease inhibitor cocktail (Sigma-Aldrich; Merck KGaA). The total protein concentrations were measured by a BCA Protein Assay kit (Sigma-Aldrich; Merck KGaA). After heat-denaturing, equal quantities of proteins (20 µg) were separated by NuPAGE Novex 12% Bis-Tris Gel and electrophoresed in the XCell SureLock™ Mini-Cell (both from Invitrogen; Thermo Fisher Scientific, Inc.), and then transferred to polyvinylidene difluoride membranes and blocked with 5% non-fat milk in Tris-buffered saline (TBS) for 1.5 h at the room temperature. The membranes were incubated with primary antibodies against OXPHOS (ab110413; 1:1,000; Abcam, Cambridge, UK) or GAPDH (AB2302; 1:1,000; EMD Millipore, Billerica, MA, USA) overnight at 4°C. After washing three times with 1X TBS, the membranes were incubated with secondary antibodies [anti-mouse (AP181R) and anti-rabbit antibodies (AP187R); 1:10,333; EMD Millipore] for 1.5 h at room temperature. After washing steps, immunoreactive binding was detected with ECL detection reagent (Amersham Biosciences, Piscataway, NJ, USA) with MicroChemi 4.2. The band intensity was quantified using ImageJ 1.47 software.

Chang Y., Li Y., Ye N., Guo X., Li Z., Sun G, & Sun Y. (2017). Atorvastatin protects the proliferative ability of human umbilical vein endothelial cells inhibited by angiotensin II by changing mitochondrial energy metabolism. International Journal of Molecular Medicine, 41(1), 33-42.

+ Open protocol

+ Expand

Fluorescent Glycated Protein Quantification

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Glycated proteins were identified as previously described13 (link). Briefly, brain homogenates were incubated with 0.5 mM fluorescent boronic acid at room temperature for one hour. Gel electrophoresis was performed using an Xcell surelock mini-cell (Invitrogen), separating proteins on 15% tris-glycine gels. Glycation was visualised prior to protein staining with a Dark Reader^® (Clare Chemicals Research Inc.; 420–520 nm, with 530 or 595 nm filter). Gels were then stained with coomassie to visualise total protein content. Samples where only SDS-PAGE was required skipped the boronic acid incubation and visualisation stages. Quantification of protein band fluorescence and coomassie stain intensity was performed using Fusion software (Vilber Lourmat).

Kassaar O., Pereira Morais M., Xu S., Adam E.L., Chamberlain R.C., Jenkins B., James T., Francis P.T., Ward S., Williams R.J, & van den Elsen J. (2017). Macrophage Migration Inhibitory Factor is subjected to glucose modification and oxidation in Alzheimer’s Disease. Scientific Reports, 7, 42874.

+ Open protocol

+ Expand

Recombinant Disintegrins Purification

Cited 2 times

Check if the same lab product or an alternative is used in the 5 most similar protocols

r-Mojastin 1 and r-viridistatin 2 were expressed in E.coli and further purified by two-step chromatography, using the method of Sánchez et al. (2010) (link) and Lucena et al. (2012) (link), respectively. Briefly, E. coli BL21 cells were grown, induced by 0.5 mM of isopropyl β-D thiogalactoside (IPTG) and centrifuged. After bacterial cell disruption with a Branson Sonifier 450 (Danbury, CT), the cell debris was removed by centrifugation and the crude lysate was incubated with glutathione Sepharose 4B (GS4B) (Amersham Biosciences). Recombinant disintegrins peptides were cleaved and eluted from glutathione S-transferase (GST) bound to GS4B by thrombin (80 U/mL, GE Healthcare Life Sciences, USA). thrombin was removed from r-mojastin 1 and r-viridistatin 2 using a 5 mL HiTrap^™ Benzamidine Sepharose 4 Fast Flow column (Amersham Biosciences). Purity of recombinant disintegrins was determined by using a 10–20% Tricine gel (Schägger and von Jagow, 1987 (link)) in an XCell SureLock Mini-Cell (Invitrogen Life Technologies, USA).

Lucena S., Castro R., Lundin C., Hofstetter A., Alaniz A., Suntravat M, & Sánchez E.E. (2014). Inhibition of pancreatic tumoral cells by snake venom disintegrins. Toxicon : official journal of the International Society on Toxinology, 93, 136-143.

+ Open protocol

+ Expand

Native Gel Electrophoresis of Hsp60 and GroEL Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols

Native gel electrophoresis was performed using NativePAGE Bis-Tris Gels according to the manufacturer's instructions (Invitrogen, Carlsbad, CA, USA). Hsp60 and GroEL protein samples were diluted in NativePAGE Sample Buffer (1x) containing 1% digitonin and 0.5% n-dodecyl-β-D-maltoside (DDM) detergent solutions at pH 7.2. Samples and molecular weight marker (NativeMark Unstained Protein Standard-Invitrogen) were loaded on precasted 4–16% Novex NativePAGE Bis-Tris Gels that resolve proteins in the molecular weight range of 15–1,000 kDa. lectrophoresis was performed at 150 V constant voltage for 120 min, using XCell SureLock Mini-Cell (Invitrogen). Gels were stained by Coomassie G-250 staining. Gels were destained in 8% acetic acid until the desired background was obtained and scanned, using Gel Doc XR (Bio-Rad) molecular imager. Protein molecular weights were determined by the Quantity One software (Bio-Rad).

Vilasi S., Carrotta R., Mangione M.R., Campanella C., Librizzi F., Randazzo L., Martorana V., Marino Gammazza A., Ortore M.G., Vilasi A., Pocsfalvi G., Burgio G., Corona D., Palumbo Piccionello A., Zummo G., Bulone D., Conway de Macario E., Macario A.J., San Biagio P.L, & Cappello F. (2014). Human Hsp60 with Its Mitochondrial Import Signal Occurs in Solution as Heptamers and Tetradecamers Remarkably Stable over a Wide Range of Concentrations. PLoS ONE, 9(5), e97657.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!