Bortezomib

Manufactured by Enzo Life Sciences

Bortezomib is a proteasome inhibitor used in research applications. It functions by inhibiting the 26S proteasome, a large protein complex responsible for the degradation of most cellular proteins.

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Lab products found in correlation

Rapamycin, by Enzo Life Sciences (1 mentions) Spautin 1, by Merck Group (1 mentions) Mg132, by Enzo Life Sciences (1 mentions) Penicillin streptomycin, by Thermo Fisher Scientific (1 mentions) Rpmi 1640, by Thermo Fisher Scientific (1 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (1 mentions) Non essential amino acids (neaa), by Thermo Fisher Scientific (1 mentions) Doxorubicin, by Merck Group (1 mentions) Vincristine, by Merck Group (1 mentions) Honokiol, by Enzo Life Sciences (1 mentions) Stemspan sfem 2, by STEMCELL (1 mentions) Necrostatin 1, by Enzo Life Sciences (1 mentions) Z vad fmk, by Merck Group (1 mentions) Etoposide, by Teva Pharmaceuticals (1 mentions) Protein a g plus agarose bead, by Santa Cruz Biotechnology (1 mentions) Rabbit anti psma6, by Fortis Life Sciences (1 mentions) Isotype control antibody, by Merck Group (1 mentions) Anti p53 antibody fl393, by Santa Cruz Biotechnology (1 mentions) 35s methionine labeling mix, by PerkinElmer (1 mentions)

5 protocols using bortezomib

Dendritic Cell Infection Dynamics

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DCs (2 × 10⁶) were infected in a total volume of 300 µl RPMI 1640 medium supplemented with 20 mM Hepes at an MOI of 2. Infection was performed for 1 h at 37°C at 300 rpm in a shaking heating block (Eppendorf). Subsequently, cells were transferred to RPMI 1640 medium containing 1% autologous serum, 10 mM Hepes, 2 mM L-glutamine, 100 U/ml penicillin, 100 µg/ml streptomycin, 40 U/ml GM-CSF, and 250 U/ml IL-4, adjusted to a final concentration of 10⁶ cells/ml.
Where indicated, cells were treated with 10 µM MG-132, 2 µM bortezomib, or 10 nM rapamycin (all from Enzo Life Sciences) at 1 hpi. To inhibit autophagy and lysosomal degradation, cells were incubated with 10 µM spautin-1 or 1 µM BA-1 (all from Sigma-Aldrich) 1 h before infection.

Turan A., Grosche L., Krawczyk A., Mühl-Zürbes P., Drassner C., Düthorn A., Kummer M., Hasenberg M., Voortmann S., Jastrow H., Dörrie J., Schaft N., Kraner M., Döhner K., Sodeik B., Steinkasserer A, & Heilingloh C.S. (2019). Autophagic degradation of lamins facilitates the nuclear egress of herpes simplex virus type 1. The Journal of Cell Biology, 218(2), 508-523.

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Culturing T-ALL Cell Lines

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Jurkat T-lymphoblasts (clone E6-1) were purchased form the American Type Culture Collection. Dr. Weng provided the T-ALL cell lines THP-6, SUP-T1, DND-41, Peer, BE-13 and Karpas. Dr. Roberts provided the CD47-decifient Jurkat cell line, JinB8^{24 (link)}. All cells were maintained at 37 °C, 5% CO₂, in cRPMI (cRPMI is RPMI 1640 supplemented with 10% fetal bovine serum (Invitrogen), non-essential amino acids (Invitrogen), and penicillin-streptomycin (Gibco)). Where indicated, serum-free RPMI contains 1% bovine serum albumin (BSA). The primary T-ALL, BD-67, was as described previously^{25 (link)}. Cells harvested from spleens of xenografted mice were maintained in vitro up to 7 days in StemSpan SFEMII (StemCell Technologies). Chemotherapeutics used were doxorubicin and vincristine (Sigma-Aldrich), bortezomib (cell signaling) and honokiol (Enzo). All other reagents were from Sigma unless otherwise stated.

Leclair P., Liu C.C., Monajemi M., Reid G.S., Sly L.M, & Lim C.J. (2018). CD47-ligation induced cell death in T-acute lymphoblastic leukemia. Cell Death & Disease, 9(5), 544.

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Evaluating Compound-Induced Cell Death

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The following reagents were purchased from Sigma-Aldrich: Necrostatin-1, Bortezomib; Enzo: z-VAD.fmk; Millipore: Necrosulfonamide; LC Labs: 17-DMAG; StressMarq: VER-155008; and Teva Pharmaceuticals: Etoposide. JG-98 was synthesized and characterized as previously described^{14 (link)}. All compounds were suspended in DMSO and the final solvent concentration in the assays was held to 1%.

Srinivasan S.R., Cesa L.C., Li X., Julien O., Zhuang M., Shao H., Chung J., Maillard I., Wells J.A., Duckett C, & Gestwicki J.E. (2017). Heat Shock Protein 70 (Hsp70) Suppresses RIP1-Dependent Apoptotic and Necroptotic Cascades. Molecular cancer research : MCR, 16(1), 58-68.

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Proteasome Immunoprecipitation from Sciatic Nerve

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Sciatic nerves were flash frozen, pulverized in liquid nitrogen, suspended in APB buffer (25 mM HEPES-KOH pH 7.5, 150 mM NaCl, 5 mM MgCl₂, 1 mM ATP, 1 mM DTT, and 10% glycerol) plus 1 μM Bortezomib (Enzo), sonicated (three times, 10 s on–30 s off, 25% power, Bandelin HD 2200), and centrifuged at 14,000g for 10 min at 4°C. Protein concentration of the clarified lysates was determined by Bradford assay and equal amounts of total protein per genotype were pre-cleared with Protein A/G Plus agarose beads (Santa Cruz Biotechnology) for 30 min at 4°C. Rabbit anti PSMA6 (Bethyl Laboratories) was added to the supernatant at a final concentration of 2 μg/ml and the samples rotated end over end for 2 h at 4°C. Protein A/G Plus agarose beads, washed 3x in APB buffer, were added and the mixture was rotated end over end for 1 h at 4°C. The beads were then collected by centrifugation and washed 3X in APB buffer for 5 min each time. The immunoprecipitates were eluted by boiling for 5 min in 2X Laemmli sample buffer (120 mM Tris–HCl pH 6.8, 4% SDS, 200 mM DTT, 0.002% xylene cyanol).

VerPlank J.J., Gawron J.M., Silvestri N.J., Wrabetz L, & Feltri M.L. (2024). Knockout of PA200 improves proteasomal degradation and myelination in a proteotoxic neuropathy. Life Science Alliance, 7(4), e202302349.

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Immunoprecipitation of p53 Protein

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For immunoprecipitation, cells were treated for 4 h with Etoposide and/or Roc-A in the absence or presence of 100 nM Bortezomib (Enzo Life Sciences). In the case of metabolic pulse-labeling experiments, treatment was followed by adding 100 μCi/ml of [³⁵S]-methionine-labeling mix (PerkinElmer, Waltham, MA, USA) to the medium for 0–15 min. Subsequently, cells were washed in ice-cold PBS, lysed in IP buffer (20 mM Tris-HCl, 5 M NaCl, 2 mM EDTA, 1% Triton X-100, protease inhibitors) and centrifuged (10 000 × g, 20 min) to clear lysates. Aliquots were taken for input control and lysates were incubated overnight with sepharose-coupled protein A beads, anti-p53 antibody (FL-393; Santa Cruz) or isotype control antibody (Sigma-Aldrich). Two wash steps with IP buffer preceded boiling of beads in denaturing sample buffer at 95°C for 5 min. Incorporation of [³⁵S]-methionine into p53 protein was detected by the phosphoimaging system FLA-7000 IR (Fujifilm Europe GmbH, Düsseldorf, Germany).

Becker M.S., Schmezer P., Breuer R., Haas S.F., Essers M.A., Krammer P.H, & Li-Weber M. (2014). The traditional Chinese medical compound Rocaglamide protects nonmalignant primary cells from DNA damage-induced toxicity by inhibition of p53 expression. Cell Death & Disease, 5(1), e1000-.

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