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AB3329

Anti-Proteasome 20S LMP7 抗体

Anti-Proteasome 20S LMP7 antibody

4

(12 Reviews)

|

(65 Publications)

Rabbit Polyclonal Proteasome 20S LMP7 antibody. Suitable for ICC, WB and reacts with Human samples. Cited in 65 publications. Immunogen corresponding to Synthetic Peptide within Human PSMB8 aa 250 to C-terminus.

別名を表示する

LMP7, PSMB5i, RING10, Y2, PSMB8, Proteasome subunit beta type-8, Low molecular mass protein 7, Macropain subunit C13, Multicatalytic endopeptidase complex subunit C13, Proteasome component C13, Proteasome subunit beta-5i, Really interesting new gene 10 protein

4 Images
Immunocytochemistry - Anti-Proteasome 20S LMP7 antibody (AB3329)
  • ICC

Supplier Data

Immunocytochemistry - Anti-Proteasome 20S LMP7 antibody (AB3329)

Immunocytochemistry/ Immunofluorescence analysis of HeLa cells labeling Proteasome 20S LMP7 with ab3329 at 5μg/ml. The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.1% Triton X-100 in TBS for 10 minutes, and blocked with 3% Blocker BSA in PBS for 15 minutes at room temperature. Cells were stained with or without Anti-Proteasome 20S LMP7 antibody (ab3329), at a concentration of 5μg/ml for 1 hour at room temperature, and then incubated with a Alexa Fluor® 488 goat anti-rabbit IgG secondary antibody at a dilution of 1/1000 for 1 hour s at room temperature (both panels, green). Nuclei (both panels, blue) were stained with Hoechst 33342 dye.

Immunocytochemistry - Anti-Proteasome 20S LMP7 antibody (AB3329)
  • ICC

Unknown

Immunocytochemistry - Anti-Proteasome 20S LMP7 antibody (AB3329)

ICC/IF image of ab3329 stained MCF7 cells. The cells were 4% formaldehyde fixed (10 min) and then incubated in 1%BSA / 10% normal goat serum / 0.3M glycine in 0.1% PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated with the antibody (ab3329, 5µg/ml) overnight at +4°C. The secondary antibody (green) was Alexa Fluor® 488 goat anti-rabbit IgG (H+L) used at a 1/1000 dilution for 1h. Alexa Fluor® 594 WGA was used to label plasma membranes (red) at a 1/200 dilution for 1h. DAPI was used to stain the cell nuclei (blue) at a concentration of 1.43µM.

Western blot - Anti-Proteasome 20S LMP7 antibody (AB3329)
  • WB

Supplier Data

Western blot - Anti-Proteasome 20S LMP7 antibody (AB3329)

Detected by chemiluminescence.

All lanes:

Western blot - Anti-Proteasome 20S LMP7 antibody (ab3329) at 2 µg/mL

Lane 1:

HeLa whole cell extracts at 30 µg

Lane 2:

HeLa treated with IFN gamma (100ng/ml IFN gamma for 72h) whole cell extracts at 30 µg

Lane 3:

U-937 whole cell extracts at 30 µg

Lane 4:

Raji whole cell extracts at 30 µg

Lane 5:

Ramos whole cell extracts at 30 µg

Secondary

All lanes:

Goat anti-Rabbit IgG (H+L) HRP conjugate at 1/2500 dilution

Predicted band size: 30 kDa

Observed band size: 20 kDa

false

Western blot - Anti-Proteasome 20S LMP7 antibody (AB3329)
  • WB

Unknown

Western blot - Anti-Proteasome 20S LMP7 antibody (AB3329)

Western blot of proteasome 20S LMP7 from HeLa cell extract using ab3329.

All lanes:

Western blot - Anti-Proteasome 20S LMP7 antibody (ab3329)

Predicted band size: 30 kDa

false

Key facts

宿主種

Rabbit

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

交差種

Human

アプリケーション

ICC, WB

applications

免疫原

Synthetic Peptide within Human PSMB8 aa 250 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

P28062

Reactivity data

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出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification Immunogen
バッファー組成
Constituents: 99% PBS, 0.1% BSA
出荷温度
Blue Ice
短期保存期間
1-2 weeks
短期保存温度
+4°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle

補足情報

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

Proteasome 20S LMP7 also known as β5i or PSMB8 is a subunit of the immunoproteasome. It weighs about 23 kDa and it is expressed predominantly in immune cells such as lymphocytes and macrophages. LMP7 is part of the proteasome 20S a cylindrical core particle involved in the degradation of ubiquitinated proteins. This process helps maintain protein homeostasis by breaking down misfolded and damaged proteins.
Biological function summary

The immunoproteasome in which LMP7 is an essential component plays an important role in the adaptive immune system. It influences the generation of antigenic peptides that are presented on MHC class I molecules. LMP7's expression is increased during immune responses particularly following gamma interferon (IFN-γ) stimulation contributing to the immune-mediated proteasome conformation. The immunoproteasome enables more efficient peptide processing enhancing antigen presentation to cytotoxic T lymphocytes.

Pathways

LMP7 is involved in the MHC class I antigen presentation pathway. This pathway allows the immune system to detect and respond to intracellular pathogens such as viruses. Additionally LMP7 interacts with TAP (Transporter associated with Antigen Processing) and other proteasome subunits to ensure effective peptide processing for loading onto MHC class I molecules. Through this involvement it closely links to immune signaling and cellular stress responses.

Research shows that LMP7 connects to autoimmune diseases and inflammatory disorders such as lupus and rheumatoid arthritis. Dysregulation of LMP7 expression or activity can lead to improper immune responses contributing to disease pathogenesis. Furthermore LMP7 impacts the degradation of specific proteins relevant to these conditions. For example it works alongside other proteasome subunits like LMP2 and MECL-1 in modulating the inflammatory response which can exacerbate autoimmune disease symptoms.

製品プロトコール

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ターゲットの情報

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (PubMed : 27049119). Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes.
See full target information PSMB8

文献 (65)

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

Nature 644:516-526 PubMed40681898

2025

Pathology-oriented multiplexing enables integrative disease mapping.

Applications

Unspecified application

Species

Unspecified reactive species

Malte Kuehl,Yusuke Okabayashi,Milagros N Wong,Lukas Gernhold,Gabriele Gut,Nico Kaiser,Maria Schwerk,Stefanie K Gräfe,Frank Y Ma,Jovan Tanevski,Philipp S L Schäfer,Sam Mezher,Jacobo Sarabia Del Castillo,Thiago Goldbeck-Strieder,Olga Zolotareva,Michael Hartung,Fernando M Delgado Chaves,Lukas Klinkert,Ann-Christin Gnirck,Marc Spehr,David Fleck,Mehdi Joodaki,Victor Parra,Mina Shaigan,Martin Diebold,Marco Prinz,Jennifer Kranz,Johan M Kux,Fabian Braun,Oliver Kretz,Hui Wu,Florian Grahammer,Sven Heins,Marina Zimmermann,Fabian Haas,Dominik Kylies,Nicola Wanner,Jan Czogalla,Bernhard Dumoulin,Nikolay Zolotarev,Maja Lindenmeyer,Pall Karlson,Jens R Nyengaard,Marcial Sebode,Sören Weidemann,Thorsten Wiech,Hermann-Josef Groene,Nicola M Tomas,Catherine Meyer-Schwesinger,Christoph Kuppe,Rafael Kramann,Alexandre Karras,Patrick Bruneval,Pierre-Louis Tharaux,Diego Pastene,Benito Yard,Jennifer A Schaub,Phillip J McCown,Laura Pyle,Ye Ji Choi,Takashi Yokoo,Jan Baumbach,Pablo J Sáez,Ivan Costa,Jan-Eric Turner,Jeffrey B Hodgin,Julio Saez-Rodriguez,Tobias B Huber,Petter Bjornstad,Matthias Kretzler,Olivia Lenoir,David J Nikolic-Paterson,Lucas Pelkmans,Stefan Bonn,Victor G Puelles

Cancers 17: PubMed40507366

2025

LMP7-Specific Inhibitor M3258 Modulates the Tumor Microenvironment of Triple-Negative Breast Cancer and Inflammatory Breast Cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Xuemei Xie,Jangsoon Lee,Ganiraju C Manyam,Troy Pearson,Gina Walter-Bausch,Manja Friese-Hamim,Sheng Zhao,Julia Jabs,Angela A Manginelli,Nadine Piske,Thomas Mrowiec,Corinna M Wolf,Bharat S Kuntal,Debu Tripathy,Jing Wang,Michael P Sanderson,Naoto T Ueno

iScience 28:111873 PubMed40060909

2025

Mutational pressure promotes release of public CD8 T cell epitopes by proteasome from SARS-CoV-2 RBD of Omicron and its current lineages.

Applications

Unspecified application

Species

Unspecified reactive species

Anna A Kudriaeva,Ivan O Butenko,George A Saratov,Maxim Т Ri,Yuliana A Mokrushina,Alexey A Bondarev,Alena S Evpak,Ivan V Smirnov,Daria S Matyushkina,Alexander G Gabibov,Vadim M Govorun,Alexey A Belogurov

Proceedings of the National Academy of Sciences of the United States of America 122:e2419607122 PubMed39964708

2025

Tracking proteasome degradation: A cross-organ analysis via intact degradomics mass spectrometry.

Applications

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Species

Unspecified reactive species

Katharina I Zittlau,Daniel Zachor-Movshovitz,Yegor Leushkin,Roy Schimmel Brener,David Morgenstern,Gili Ben-Nissan,Michal Sharon

Autophagy 21:1212-1227 PubMed39878121

2025

Limiting cap-dependent translation increases 20S proteasomal degradation and protects the proteomic integrity in autophagy-deficient skeletal muscle.

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Unspecified reactive species

Han Dong,Yifan Lyu,Chien-Yung Huang,Shih-Yin Tsai

Journal of neuroinflammation 21:191 PubMed39095788

2024

Targeting the immunoproteasome in hypothalamic neurons as a novel therapeutic strategy for high-fat diet-induced obesity and metabolic dysregulation.

Applications

Unspecified application

Species

Unspecified reactive species

Nicolás Albornoz,Javiera Álvarez-Indo,Adely de la Peña,Eloisa Arias-Muñoz,Alanis Coca,Fabián Segovia-Miranda,Bredford Kerr,Mauricio Budini,Alfredo Criollo,María A García-Robles,Eugenia Morselli,Andrea Soza,Patricia V Burgos

Arteriosclerosis, thrombosis, and vascular biology 44:1346-1364 PubMed38660806

2024

Immunoproteasomal Inhibition With ONX-0914 Attenuates Atherosclerosis and Reduces White Adipose Tissue Mass and Metabolic Syndrome in Mice.

Applications

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Species

Unspecified reactive species

Frank H Schaftenaar,Andrea D van Dam,Gerjan de Bruin,Marie A C Depuydt,Jill de Mol,Jacob Amersfoort,Hidde Douna,Menno Meijer,Mara J Kröner,Peter J van Santbrink,Mireia N A Bernabé Kleijn,Gijs H M van Puijvelde,Bogdan I Florea,Bram Slütter,Amanda C Foks,Ilze Bot,Patrick C N Rensen,Johan Kuiper

Molecular cancer 22:196 PubMed38049829

2023

Immunoproteasome function maintains oncogenic gene expression in KMT2A-complex driven leukemia.

Applications

Unspecified application

Species

Unspecified reactive species

Nuria Tubío-Santamaría,Ashok Kumar Jayavelu,Tina M Schnoeder,Theresa Eifert,Chen-Jen Hsu,Florian Perner,Qirui Zhang,Daniela V Wenge,Fynn M Hansen,Joanna M Kirkpatrick,Nidhi Jyotsana,Steven W Lane,Björn von Eyss,Aniruddha J Deshpande,Michael W M Kühn,Juerg Schwaller,Clemens Cammann,Ulrike Seifert,Frédéric Ebstein,Elke Krüger,Andreas Hochhaus,Michael Heuser,Alessandro Ori,Matthias Mann,Scott A Armstrong,Florian H Heidel

International journal of molecular sciences 24: PubMed37895057

2023

Ubiquitin Proteasome System Role in Diabetes-Induced Cardiomyopathy.

Applications

Unspecified application

Species

Unspecified reactive species

Ortal Nahum-Ankonina,Efrat Kurtzwald-Josefson,Aaron Ciechanover,Maayan Waldman,Orna Shwartz-Rohaker,Edith Hochhauser,Sam J Meyer,Dan Aravot,Moshe Phillip,Yaron D Barac

Nature communications 14:4092 PubMed37433777

2023

Immunoproteasome-specific subunit PSMB9 induction is required to regulate cellular proteostasis upon mitochondrial dysfunction.

Applications

Unspecified application

Species

Unspecified reactive species

Minji Kim,Remigiusz A Serwa,Lukasz Samluk,Ida Suppanz,Agata Kodroń,Tomasz M Stępkowski,Praveenraj Elancheliyan,Biniyam Tsegaye,Silke Oeljeklaus,Michal Wasilewski,Bettina Warscheid,Agnieszka Chacinska
View all publications

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