Quickgel chamber

Manufactured by Helena Laboratories

The QuickGel Chamber is a laboratory equipment designed for electrophoresis applications. It provides a controlled environment for the separation and analysis of various biomolecules, such as proteins or enzymes. The device ensures consistent and reliable results by maintaining the necessary conditions for the electrophoresis process.

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Lab products found in correlation

Quickgels, by Helena Laboratories (5 mentions) Microtainer tube, by BD (2 mentions) Prism 8, by GraphPad (1 mentions) Mouse igg isotype control, by Thermo Fisher Scientific (1 mentions) Easy titer mouse igg assay kit, by Thermo Fisher Scientific (1 mentions) Advia 120 hematology system, by Siemens (1 mentions)

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QuickGels (5 citations)

8 protocols using quickgel chamber

Serum Protein Electrophoresis in Mice

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Mice blood samples were collected at time of euthanasia. Samples were allowed to coagulate at room temperature and spun at 3000 × G for 10 min; 0.5 μl of sera were loaded in precast QuickGels (Helena Laboratories, 3505T) and run on a QuickGel Chamber (Helena Laboratories, 1284) according to the manufacturer's instructions. Samples were analyzed in triplicate with M-spike positive samples visible in all three analyses.

McBride K.M., Kil H., Mu Y., Plummer J.B., Lee J., Zelazowski M.J., Sebastian M., Abba M.C, & Aldaz C.M. (2019). Wwox Deletion in Mouse B Cells Leads to Genomic Instability, Neoplastic Transformation, and Monoclonal Gammopathies. Frontiers in Oncology, 9, 517.

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Serum Protein Electrophoresis in Myeloma Mice

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Serum protein electrophoresis (SPEP) was performed to identify M-protein spikes in the WT 5TGM1-GFP and Itga4 KO 5TGM1-GFP myeloma mouse models used in this study. Blood samples were collected from the mice by cheek bleed technique in serum separating tubes. The serum was separated from samples by centrifuging at 1000 rpm for 10 min. These serum samples were analyzed on a QuickGel Chamber apparatus using pre-casted QuickGels (Helena laboratories) according to the manufacturer’s instructions. The % gamma globulin values were quantified from the bands using ImageJ software (Maryland, USA). The data is presented as mean + /− standard deviation using GraphPad Prism 8.0 (La Jolla, CA, USA).

Hathi D., Chanswangphuwana C., Cho N., Fontana F., Maji D., Ritchey J., O’Neal J., Ghai A., Duncan K., Akers W.J., Fiala M., Vij R., DiPersio J.F., Rettig M, & Shokeen M. (2022). Ablation of VLA4 in multiple myeloma cells redirects tumor spread and prolongs survival. Scientific Reports, 12, 30.

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Mouse Serum Protein Electrophoresis

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Blood was collected from mouse tail vein, followed by centrifugation and serum collection. Assay was conducted according to the manufacturer’s protocols. Briefly, serum was diluted 5-fold in PBS before loaded on a QuickGel SPE Gel (Helena Laboratories, catalog 3505T). Electrophoresis was run at 400 V for 5 minutes. Gels were dried with a QuickGel Chamber (Helena Laboratories, catalog 1284) for 15 minutes followed by staining with Acid Blue for 2 minutes and de-staining with Destain solution for 10 minutes.

Ma X., Xiao L., Liu L., Ye L., Su P., Bi E., Wang Q., Yang M., Qian J, & Yi Q. (2021). CD36-mediated ferroptosis dampens intratumoral CD8+ T-cell effector function and impairs their antitumor ability. Cell metabolism, 33(5), 1001-1012.e5.

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Serum Protein Analysis for Myeloma

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Blood was collected from mice periodically by cheek bleeding. About 100 μL of whole blood were collected into microtainer tubes (BD Biosciences), allowed to coagulate at room temperature, and spun for 10 minutes at 2,300 × g. Sera were diluted 1:2 in normal saline buffer and analyzed on a QuickGel Chamber apparatus using pre-casted QuickGels (Helena Laboratories) according to the manufacturer’s instruction. Densitometric analysis was then performed using the clinically certified Helena QuickScan 2000 workstation which allows a precise quantization of the various serum fractions, including the measurements of gamma/albumin (G/A) ratio. A G/A ratio between 0.5–2.0 corresponds to predominant M-spikes and suggest not only good multiple myeloma engraftment but also tumor response to treatments in similar factions as is done clinically [10 (link)].

Villa N.Y., Rahman M.M., Mamola J., Sharik M.E., de Matos A.L., Kilbourne J., Lowe K., Daggett-Vondras J., D'Isabella J., Goras E., Chesi M., Bergsagel P.L, & McFadden G. (2022). Transplantation of autologous bone marrow pre-loaded ex vivo with oncolytic myxoma virus is efficacious against drug-resistant Vk*MYC mouse myeloma. Oncotarget, 13, 490-504.

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Targeted Nanoparticle Therapy for Myeloma

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A KaLwRij myeloma mouse model was used as described (32 (link)). KaLwRij mice were inoculated intravenously with 1 × 10⁶ 5TGM1 cells and distributed into six groups of 6 to 8 mice, and treated intravenously (a) nontargeted (NT) or targeted (T), (b) drug-bearing (D) or no-drug (ND) PFC or micelle NPs. The following treatment cohorts were studied: (i) ND/NT 200 nm PFC NP; (ii) T/ND 200 nm PFC NP; (iii) T/D 200 nm PFC NP; (iv) NT/ND 20 nm micelles; (v) T/ND 20 nm micelles, and (vi) T/D 20 nm micelles. 5TGM1 cells were injected via tail vein on day 0. NPs were administered by tail vein injection on days 3, 5, 7, 10, 12, and 14 with 50 μL of MI1 (0.145 mg/mL) per mouse. Sera were collected on day 17, diluted 1:2 in PBS, and analyzed by serum protein electrophoresis (SPEP) on a QuickGel Chamber apparatus using precasted QuickGels (Helena Laboratories) according to the manufacturer's instruction. Densitometric analysis of the SPEP traces was performed using the clinically certified Helena QuickScan 2000 workstation, allowing a precise quantification of the various serum fractions, including the measurements of gamma/albumin ratio.

Soodgupta D., Pan D., Cui G., Senpan A., Yang X., Lu L., Weilbaecher K.N., Prochownik E.V., Lanza G.M, & Tomasson M.H. (2015). Small Molecule MYC Inhibitor Conjugated to Integrin-Targeted Nanoparticles Extends Survival in a Mouse Model of Disseminated Multiple Myeloma. Molecular cancer therapeutics, 14(6), 1286-1294.

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Comprehensive Blood Analysis Protocol

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A complete blood count (CBC) was determined using the Advia 120 Hematology System (Siemens Healthineers, Erlangen, Germany). To measure total serum IgG, blood was collected into Eppendorf tubes, allowed to coagulate at room temperature for 5 minutes, and centrifuged for 10 minutes at 850 g. Total IgG in serum was then determined by ELISA using the Easy- TiterMouse IgG Assay Kit and Mouse IgG Isotype Control (Thermo Fisher Scientific, Rockford, IL) according to the manufacturer’s protocol. For serum protein electrophoresis, sera were diluted 1:2 in normal saline buffer and then analyzed on a QuickGel Chamber apparatus using Precasted QuickGels (Helena Laboratories, Beaumont, TX) according to the manufacturer’s instructions.

Wang L., Kumar M., Deng Q., Wang X., Liu M., Gong Z., Zhang S., Ma X., Xu-Monette Z.Y., Xiao M., Yi Q., Young K.H., Ramos K.S, & Li Y. (2018). 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) Induces Peripheral Blood Abnormalities and Plasma Cell Neoplasms Resembling Multiple Myeloma in Mice. Cancer letters, 440-441, 135-144.

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Serum Protein Electrophoresis Protocol

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Serum samples were analyzed by SPEP on Quickgel Chamber apparatus using pre-casted quickGels (Helena Laboratories) according to manufacture’s instruction. Densitometric analysis of the SPEP traces was performed using the clinically certified Helena QuickScan 2000 workstation.

He Z., O’Neal J., Wilson W.C., Mahajan N., Luo J., Wang Y., Su M.Y., Lu L., Skeath J.B., Bhattacharya D, & Tomasson M.H. (2015). Deletion of Rb1 induces both hyperproliferation and cell death in murine germinal center B-cells. Experimental hematology, 44(3), 161-165.e4.

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Mouse Serum Protein Analysis

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Blood was collected from mice via submandibular venipuncture into Microtainer tubes (BD Biosciences, 365992), allowed to coagulate at room temperature, and spun for 10 minutes at 2,300 × g. Serum was diluted 1:2 in normal saline buffer and analyzed on a QuickGel Chamber apparatus using precasted QuickGels (Helena Laboratories, 1284), according to the manufacturer's instructions.

Sasine J.P., Kozlova N.Y., Valicente L., Dukov J., Tran D.H., Himburg H.A., Kumar S., Khorsandi S., Chan A., Grohe S., Li M., Kan J., Sehl M.E., Schiller G.J., Reinhardt B., Singh B.K., Ho R., Yue P., Pasquale E.B, & Chute J.P. (2024). Inhibition of Ephrin B2 Reverse Signaling Abolishes Multiple Myeloma Pathogenesis. Cancer Research, 84(6), 919-934.

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