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AB142123

Bortezomib, proteasome inhibitor

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(6 Publications)

MW 384.2 Da, Purity >98%. Potent, selective, reversible proteasome inhibitor (Ki = 0.6 nM). Inhibits proliferation of a number of tumor cell lines (IC50 = 7 nM). Inhibits TNF synthesis and FGF-induced angiogenesis.

View Alternative Names

26 kDa prosomal protein, 26S protease subunit S5a, 26S proteasome non-ATPase regulatory subunit 11, 26S proteasome non-ATPase regulatory subunit 12, 26S proteasome non-ATPase regulatory subunit 13, 26S proteasome non-ATPase regulatory subunit 14, 26S proteasome non-ATPase regulatory subunit 2, 26S proteasome non-ATPase regulatory subunit 4, 26S proteasome non-ATPase regulatory subunit 6, 26S proteasome non-ATPase regulatory subunit 7, 26S proteasome non-ATPase regulatory subunit 8, 26S proteasome regulatory subunit 9, 26S proteasome regulatory subunit RPN1, 26S proteasome regulatory subunit RPN12, 26S proteasome regulatory subunit RPN5, 26S proteasome regulatory subunit RPN6, 26S proteasome regulatory subunit RPN7, 26S proteasome regulatory subunit RPN8, 26S proteasome regulatory subunit RPN9, 26S proteasome regulatory subunit S10, 26S proteasome regulatory subunit S11, 26S proteasome regulatory subunit S12, 26S proteasome regulatory subunit S14, 26S proteasome regulatory subunit S2, 26S proteasome regulatory subunit S5A, 26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit p31, 26S proteasome regulatory subunit p40.5, 26S proteasome regulatory subunit p44.5, 26S proteasome regulatory subunit p55, 26S proteasome regulatory subunit rpn10, 26S proteasome regulatory subunit rpn11, 26S proteasome subunit p40.5, 26S proteasome subunit p97, 26S proteasome-associated PAD1 homolog, 26S proteasome-associated PAD1 homolog 1, 27 kDa prosomal protein, 55.11 protein, AAV38494, AF, AF-1, ASF, ATAD5_HUMAN, ATPase family AAA domain containing 5, ATPase family AAA domain-containing protein 5, Angiocidin, Antisecretory factor 1, Bone marrow serine protease, Breast cancer-associated protein SGA-113M, C10 II, C17orf41, Chromosome fragility-associated gene 1 protein, DELTA, DKFZp459C139, DS5a, EC 3.4.25.1, ELA2, ELANE, ELG1, ELNE_HUMAN, Elastase 2 neutrophil, Elastase neutrophil expressed, Elastase-2, Enhanced level of genomic instability 1 homolog, FLJ25321, FRAG1, Granulocyte derived elastase, HC 2, HC10 II, HC3, HC5, HC7 I, HC8, HC9, HIP6, HLE, HN3, HNE, HSN3, HSPC027, HYPF, HsBPROS26, HsT17706, Human leukocyte elastase, IOTA, KIAA0107, KIAA1838, LMPX, LMPY, Leukocyte elastase, MB1, MCB 1, MGC104214, MGC111191, MGC118075, MGC12306, MGC12467, MGC134464, MGC14274, MGC1660, MGC22756, MGC2333, MGC23846, MGC24813, MGC26605, MGC32631, MGC3844, MGC5169, MGC75406, MOV34, MOV34L, Macropain beta chain, Macropain chain Z, Macropain delta chain, Macropain epsilon chain, Macropain iota chain, Macropain subunit C3, Macropain subunit C5, Macropain subunit C7-I, Macropain subunit C8, Macropain subunit C9, Macropain subunit iota, Medullasin, Moloney leukemia virus 34 proviral, Moloney leukemia virus 34 proviral integration, Mov34 homolog, Mov34 protein homolog, Multicatalytic endopeptidase complex beta chain, Multicatalytic endopeptidase complex chain Z, Multicatalytic endopeptidase complex delta chain, Multicatalytic endopeptidase complex epsilon chain, Multicatalytic endopeptidase complex iota chain, Multicatalytic endopeptidase complex subunit C3, Multicatalytic endopeptidase complex subunit C5, Multicatalytic endopeptidase complex subunit C7 1, Multicatalytic endopeptidase complex subunit C7-I, Multicatalytic endopeptidase complex subunit C8, Multicatalytic endopeptidase complex subunit C9, Multiubiquitin chain-binding protein, NE, Neutrophil elastase, Nin1p, OTTHUMP00000059963, P31, P40.5, P44S10, P97, PAD1, PAD1, yeast, homolog of, PFAAP4, PMN E, PMN elastase, PMSA2, POH1, PROS-26, PROS-27, PSA2_HUMAN, PSA3_HUMAN, PSA4_HUMAN, PSA6_HUMAN, PSA7L_HUMAN, PSB1_HUMAN, PSB2_HUMAN, PSB3_HUMAN, PSB4_HUMAN, PSB5_HUMAN, PSB6_HUMAN, PSB7_HUMAN, PSC 2, PSC3, PSC5, PSC8, PSC9, PSD11_HUMAN, PSD12_HUMAN, PSD13_HUMAN, PSD7_HUMAN, PSDE_HUMAN, PSMA 2, PSMA 4, PSMA 7L, PSMA3, PSMA6, PSMA8 proteasome (prosome macropain) subunit alpha type 8, PSMA8 proteasome subunit alpha type 8, PSMB 1, PSMB2, PSMB3, PSMB5, PSMB6, PSMB7, PSMD2_HUMAN, PSMD4_HUMAN, PSMD6_HUMAN, PSMD8_HUMAN, PSX large multifunctional protease X, PSY large multifunctional protease Y, PUP1, Phosphonoformate immuno-associated protein 4, Polymorphonuclear elastase, Prosomal P27K protein, Prosome macropain, Proteasome (prosome macropain) subunit alpha type 3, Proteasome (prosome macropain) 26S subunit non ATPase 2, Proteasome (prosome macropain) 26S subunit non ATPase 4, Proteasome (prosome macropain) 26S subunit non ATPase 8, Proteasome (prosome macropain) subunit alpha type 2, Proteasome (prosome macropain) subunit alpha type 4, Proteasome (prosome macropain) subunit alpha type 6, Proteasome (prosome macropain) subunit beta type 1, Proteasome (prosome macropain) subunit beta type 4, Proteasome (prosome macropain) subunit beta type 6, Proteasome (prosome macropain) subunit beta type 7, Proteasome (prosome, macropain) 26S subunit, non ATPase 7, Proteasome (prosome, macropain) 26S subunit, non ATPase, 13, Proteasome (prosome, macropain) 26S subunit, non ATPase, 7 (Mov34 homolog), Proteasome (prosome, macropain) 26S subunit, non-ATPase, 14, Proteasome (prosome, macropain) 26S subunit, non-ATPase, 6, Proteasome (prosome, macropain) subunit beta type 2, Proteasome (prosome, macropain) subunit, beta type, 5, Proteasome 19S S5A, Proteasome 26S S12, Proteasome 26S non ATPase subunit 12 isoform 2, Proteasome 26S non ATPase subunit 4, Proteasome 26S subunit non ATPase 14, Proteasome 26S subunit non ATPase 4, Proteasome 26S subunit, no-ATPase, 7, Proteasome 26S subunit, non-ATPase 13, Proteasome 26S subunit, non-ATPase, 2, Proteasome 26S, subunit 2, Proteasome alpha 2 subunit, Proteasome alpha 3 subunit, Proteasome alpha 4 subunit, Proteasome beta 1 subunit, Proteasome beta 2 subunit, Proteasome beta 3 subunit, Proteasome beta 4 subunit, Proteasome beta 5 subunit, Proteasome beta 6 subunit, Proteasome beta 7 subunit, Proteasome beta chain, Proteasome catalytic subunit 1, Proteasome catalytic subunit 2, Proteasome catalytic subunit 3, Proteasome chain 13, Proteasome chain 3, Proteasome chain 6, Proteasome component C10-II, Proteasome component C3, Proteasome component C5, Proteasome component C7-I, Proteasome component C8, Proteasome component C9, Proteasome delta chain, Proteasome epsilon chain, Proteasome gamma chain, Proteasome iota chain, Proteasome regulatory particle subunit p44S10, Proteasome subunit C8, Proteasome subunit HC3, Proteasome subunit HC5, Proteasome subunit HC9, Proteasome subunit HsN3, Proteasome subunit L, Proteasome subunit MB1, Proteasome subunit X, Proteasome subunit Y, Proteasome subunit Z, Proteasome subunit alpha, Proteasome subunit alpha type-1, Proteasome subunit alpha type-2, Proteasome subunit alpha type-3, Proteasome subunit alpha type-4, Proteasome subunit alpha type-6, Proteasome subunit alpha type-7-like, Proteasome subunit beta 4, Proteasome subunit beta 6, Proteasome subunit beta 7, Proteasome subunit beta type-1, Proteasome subunit beta type-2, Proteasome subunit beta type-3, Proteasome subunit beta type-4, Proteasome subunit beta type-5, Proteasome subunit beta type-6, Proteasome subunit beta type-7, Proteasome subunit delta, Proteasome subunit iota, Proteasome subunit p40, Proteasome subunit, beta-5, Proteasome theta chain, Protein 55.11, RPN10 homolog, RPN11, Rpn12, Rpn6, Rpn7, Rpn8, Rpn9, S2, S5A, S5a/antisecretory factor protein, S9, SCN1, SGA-113M, TNFR associated protein 2, TRAP2, Testis tissue sperm binding protein Li 69n, Tumor necrosis factor receptor associated protein 2, Tumor necrosis factor type 1 receptor-associated protein 2, chromosome fragility associated gene 1, integration site gene, mouse, homolog of, p27K, p42A, p44.5, p55, pUB R5, protease 26S, subunit, 9, proteasome (prosome, macropain) 26S subunit, non ATPase12, proteasome (prosome, macropain) 26S subunit, non-ATPase, 11, proteasome (prosome, macropain) subunit, beta type 3, proteasome 26S subunit, non-ATPase, 11

Key facts

CAS number

179324-69-7

Purity

>98%

Form

Solid

form

Molecular weight

384.2 Da

Molecular formula

C<sub>1</sub><sub>9</sub>H<sub>2</sub><sub>5</sub>BN<sub>4</sub>O<sub>4</sub>

PubChem

387447

Nature

Synthetic

Solubility

The solubility of bortezomib, as the monomeric boronic acid, is 3.3 to 3.8 mg/mL in a pH range of 2 to 6.5.

Soluble in DMSO to 100 mM

Soluble in ethanol to 90 mM

Biochemical name

Bortezomib

Biological description

Potent, selective, reversible proteasome inhibitor (Ki = 0.6 nM). Inhibits proliferation of a number of tumor cell lines (IC50 = 7 nM). Inhibits TNF synthesis and FGF-induced angiogenesis.

Canonical smiles

B(C(CC(C)C)NC(=O)C(CC1=CC=CC=C1)NC(=O)C2=NC=CN=C2)(O)O

Isomeric smiles

B([C@H](CC(C)C)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)C2=NC=CN=C2)(O)O

InChi

InChI=1S/C19H25BN4O4/c1-13(2)10-17(20(27)28)24-18(25)15(11-14-6-4-3-5-7-14)23-19(26)16-12-21-8-9-22-16/h3-9,12-13,15,17,27-28H,10-11H2,1-2H3,(H,23,26)(H,24,25)/t15-,17-/m0/s1

InChiKey

GXJABQQUPOEUTA-RDJZCZTQSA-N

IUPAC Name

[(1R)-3-methyl-1-[[(2S)-3-phenyl-2-(pyrazine-2-carbonylamino)propanoyl]amino]butyl]boronic acid

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Store under desiccating conditions

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The proteasome is a large complex responsible for degrading ubiquitinated proteins which is essential for maintaining cellular protein homeostasis. PSMD8 also known as Proteasome 19S S5A/ASF along with other components like Neutrophil Elastase and various proteasome subunits (e.g. PSMB1 PSMA3 PSMD12) play critical roles within the 26S proteasome system. The 26S proteasome is known for its multi-subunit structure which includes a 20S core particle and 19S regulatory particles. Each subunit has a distinct mass and function contributing to the regulatory mechanisms. PSMD8 is expressed in many tissues facilitating its role in proteolytic processes.
Biological function summary

These proteasome components have key functions in the ubiquitin-proteasome pathway which is integral for degrading misfolded or damaged proteins. PSMD8 and its associated subunits are part of the 26S proteasome complex. This large complex helps regulate various cellular processes including DNA repair cell cycle progression and signal transduction. The activity of different subunits like PSMD2 and PSMB4 participates in recognizing unfolding and translocating targeted proteins into the proteolytic chamber for controlled degradation.

Pathways

The proteasome system including PSMD8 and other subunits plays a significant role in the ubiquitin-proteasome pathway and the cell cycle progression pathway. This system impacts cellular processes such as antigen processing and presentation which are important for immune responses. Moreover the 26S proteasome interacts with proteins like p53 and cyclins highlighting its involvement in regulating cell cycle checkpoints and apoptosis. These interactions demonstrate the proteasome’s central role in maintaining cellular integrity and function.

Dysregulation of proteasome activity which involves components like PSMD8 has been implicated in certain cancers and neurodegenerative diseases. For example the proteasome inhibitor bortezomib has been used successfully in treating multiple myeloma targeting proteasome activity to induce apoptosis in cancer cells. Abnormal proteasome function is also linked to Parkinson’s disease as it affects protein degradation in neurons. The relationship between proteasome dysfunction and these conditions underlines the importance of targeting subunits such as PSMB5/MB1 and PSMD14 in therapeutic strategies.

Product protocols

Publications (6)

Recent publications for all applications. Explore the full list and refine your search

Apoptosis : an international journal on programmed cell death 29:1145-1160 PubMed38684550

2024

ARTS and small-molecule ARTS mimetics upregulate p53 levels by promoting the degradation of XIAP.

Applications

Unspecified application

Species

Unspecified reactive species

Ruqaia Abbas,Oliver Hartmann,Dorin Theodora Asiss,Rabab Abbas,Julia Kagan,Hyoung-Tae Kim,Moshe Oren,Markus Diefenbacher,Amir Orian,Sarit Larisch

PLoS pathogens 20:e1011998 PubMed38530845

2024

Differential carbonic anhydrase activities control EBV-induced B-cell transformation and lytic cycle reactivation.

Applications

Unspecified application

Species

Unspecified reactive species

Samaresh Malik,Joyanta Biswas,Purandar Sarkar,Subhadeep Nag,Chandrima Gain,Shatadru Ghosh Roy,Bireswar Bhattacharya,Dipanjan Ghosh,Abhik Saha

Science advances 9:eade5224 PubMed36921039

2023

The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division.

Applications

Unspecified application

Species

Unspecified reactive species

Fredrik Hurtig,Thomas C Q Burgers,Alice Cezanne,Xiuyun Jiang,Frank N Mol,Jovan Traparić,Andre Arashiro Pulschen,Tim Nierhaus,Gabriel Tarrason-Risa,Lena Harker-Kirschneck,Jan Löwe,Anđela Šarić,Rifka Vlijm,Buzz Baum

Molecular therapy. Nucleic acids 27:335-348 PubMed35024245

2022

Mechanism of action of hepatitis B virus S antigen transport-inhibiting oligonucleotide polymer, STOPS, molecules.

Applications

Unspecified application

Species

Unspecified reactive species

C Cheng Kao,Yuchun Nie,Suping Ren,N Tilani T S De Costa,Rajendra K Pandey,Jin Hong,David B Smith,Julian A Symons,Leonid Beigelman,Lawrence M Blatt

Chemico-biological interactions 340:109450 PubMed33775688

2021

Nuclear factor-κB signaling inhibitors revert multidrug-resistance in breast cancer cells.

Applications

Unspecified application

Species

Unspecified reactive species

Shifaa M Abdin,Mai F Tolba,Dana M Zaher,Hany A Omar

PLoS pathogens 16:e1008105 PubMed32092124

2020

Proteasomal inhibition triggers viral oncoprotein degradation via autophagy-lysosomal pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Chandrima Gain,Samaresh Malik,Shaoni Bhattacharjee,Arijit Ghosh,Erle S Robertson,Benu Brata Das,Abhik Saha
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