Anti-PSMD1 antibody
5
(1 Review)
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(10 Publications)
Rabbit Polyclonal PSMD1 antibody. Suitable for IP, WB, IHC-Fr and reacts with Human, Mouse samples. Cited in 10 publications. Immunogen corresponding to Synthetic Peptide within Human PSMD1 aa 900 to C-terminus.
View Alternative Names
26S proteasome non-ATPase regulatory subunit 1, 26S proteasome regulatory subunit RPN2, 26S proteasome regulatory subunit S1, 26S proteasome subunit p112, PSMD1
- IHC-Fr
Supplier Data
Immunohistochemistry (Frozen sections) - Anti-PSMD1 antibody (AB140682)
Immunohistochemical analysis of frozen section of Human breast carcinoma tissue with ab140682 at 1 : 5,000 (0.2μg/ml) dilution.
Detection : DAB
- IP
Unknown
Immunoprecipitation - Anti-PSMD1 antibody (AB140682)
ab140682 at 1 µg/ml detecting PSMD1 in 293T whole cell lysate by WB following IP.
Lane 1 : IP with an antibody which recognizes a different epitope of PSMD1.
Lane 2 : ab140682 at 6 µg/mg of lysate.
Lane 3 : Control IgG.
In each case, 1 mg of lysate was used for IP and 20% of the IP was loaded.
Detection : Chemiluminescence with an exposure time of 3 seconds
All lanes:
Immunoprecipitation - Anti-PSMD1 antibody (ab140682)
Predicted band size: 105 kDa
false
- IHC-Fr
Supplier Data
Immunohistochemistry (Frozen sections) - Anti-PSMD1 antibody (AB140682)
Immunohistochemical analysis of frozen section of Mouse renal cell carcinoma tissue with ab140682 at 1 : 5,000 (0.2μg/ml) dilution.
Detection : DAB
- WB
Unknown
Western blot - Anti-PSMD1 antibody (AB140682)
All lanes:
Western blot - Anti-PSMD1 antibody (ab140682) at 0.1 µg/mL
Lane 1:
Whole cell lysate prepared from 293T cells at 50 µg
Lane 2:
Whole cell lysate prepared from 293T cells at 15 µg
Lane 3:
Whole cell lysate prepared from HeLa cells at 50 µg
Lane 4:
Whole cell lysate prepared from Jurkat cells at 50 µg
Predicted band size: 105 kDa
true
Exposure time: 10s
- WB
Unknown
Western blot - Anti-PSMD1 antibody (AB140682)
All lanes:
Western blot - Anti-PSMD1 antibody (ab140682) at 0.1 µg/mL
All lanes:
whole cell lysate prepared from NIH3T3 cells at 50 µg
Predicted band size: 105 kDa
true
Exposure time: 30s
- WB
CiteAb
Western blot - Anti-PSMD1 antibody (AB140682)
Western Blotting using Anti-PSMD1 antibody, ab140682. Publication image from Lobanova, E. S. et al., 2018, Nat Commun, 29712894. Legend direct from paper.
Proteasome composition of the mouse retina. a The molar ratio among 20S, 19S, and 11S proteasomal components determined by quantitative mass spectrometry. Data are shown as mean ± SEM; n = 3. b Fractionation of proteasome components in retinal extracts from 1-month-old mice (200 µg total protein) by size-exclusion chromatography on a Superose-6 column. Proteins in 0.5 ml fractions were probed by western blotting using antibodies against β1 subunit of the 20S proteasome core, PSMD11 subunit of the 19S proteasome cap, and PA28α subunit of the 11S cap. Data are taken from one of the four similar experiments. c The distribution of β1, PSMD11, and PA28α in 20 µm serial tangential sections throughout the entire WT mouse retina. Each section was solubilized in 30 µl SDS-PAGE sample buffer for analysis. Proteins were visualized by western blotting using the ECL technique. Rhodopsin was used as a photoreceptor outer segment marker; phosducin was used as a marker of the entire photoreceptor layer. Data are taken from one of two similar experiments. A representative retinal cross-section is shown below western blot panes; the corresponding position of the photoreceptor cells is illustrated by a cartoon
false
- WB
CiteAb
Western blot - Anti-PSMD1 antibody (AB140682)
Western Blotting using Anti-PSMD1 antibody, ab140682. Publication image from Lobanova, E. S. et al., 2018, Nat Commun, 29712894. Legend direct from paper.
Characterization of PA28α and PSMD11 overexpressing (OE) mice. a Western blots of proteasomal subunits in retinal lysates containing 30 µg total protein. Bands were visualized using the LiCor Odyssey imaging system. Each protein was analyzed in at least 3 pairs of 1-month-old WT and overexpressing animals. b Retinal morphology of 3-month-old overexpressing and WT mice. Retinas were embedded in plastic, 1 µm cross-sections were stained by toluidine blue and analyzed by light microscopy. Data are taken from one of the five similar experiments; scale bar : 20 µm. c Chymotrypsin-like proteasomal activity in retinal extracts from 1-month-old overexpressing and WT mice; measurements were performed in the presence or absence of ATP, as indicated. The number of measurements was 10, 7, and 5 for WT, PA28α overexpressing, and PSMD11 overexpressing mice, respectively. The data are shown as mean ± SEM; p values determined across individual preparations are indicated in the text. d Fractionation of proteasomal components in retinal extracts from 2-month-old overexpressing and WT mice by size-exclusion chromatography on a Superose-6 Increase column. Proteins in 0.5 ml fractions were probed by western blotting using antibodies against the β1 subunit of the 20S proteasome core, PSMD11 subunit of the 19S proteasome cap, and PA28α subunit of the11S cap. Data are taken from one of the three similar experiments
false
- WB
CiteAb
Western blot - Anti-PSMD1 antibody (AB140682)
Western Blotting using Anti-PSMD1 antibody, ab140682. Publication image from Lobanova, E. S. et al., 2018, Nat Commun, 29712894. Legend direct from paper.
Overexpression of PA28α or PSMD11 does not affect accumulation of the UbG76V-GFP reporter. The UbG76V-GFP reporter was detected in retinal lysates from 1-month-old mice of indicated genotypes (30 µg total protein/lane) using an anti-GFP antibody; Hsc-70 was used as a loading control. The band representing the non-proteolyzed non-fluorescent GFP product co-accumulating with this reporter in cells suffering from proteasomal insufficiency10,58 is labeled as xGFP. Data are taken from one of the four similar experiments
false
- WB
CiteAb
Western blot - Anti-PSMD1 antibody (AB140682)
Western Blotting using Anti-PSMD1 antibody, ab140682. Publication image from Lobanova, E. S. et al., 2018, Nat Commun, 29712894. Legend direct from paper.
Proteasome composition of the mouse retina. a The molar ratio among 20S, 19S, and 11S proteasomal components determined by quantitative mass spectrometry. Data are shown as mean ± SEM; n = 3. b Fractionation of proteasome components in retinal extracts from 1-month-old mice (200 µg total protein) by size-exclusion chromatography on a Superose-6 column. Proteins in 0.5 ml fractions were probed by western blotting using antibodies against β1 subunit of the 20S proteasome core, PSMD11 subunit of the 19S proteasome cap, and PA28α subunit of the 11S cap. Data are taken from one of the four similar experiments. c The distribution of β1, PSMD11, and PA28α in 20 µm serial tangential sections throughout the entire WT mouse retina. Each section was solubilized in 30 µl SDS-PAGE sample buffer for analysis. Proteins were visualized by western blotting using the ECL technique. Rhodopsin was used as a photoreceptor outer segment marker; phosducin was used as a marker of the entire photoreceptor layer. Data are taken from one of two similar experiments. A representative retinal cross-section is shown below western blot panes; the corresponding position of the photoreceptor cells is illustrated by a cartoon
false
- WB
CiteAb
Western blot - Anti-PSMD1 antibody (AB140682)
Western Blotting using Anti-PSMD1 antibody, ab140682. Publication image from Lobanova, E. S. et al., 2018, Nat Commun, 29712894. Legend direct from paper.
Characterization of PA28α and PSMD11 overexpressing (OE) mice. a Western blots of proteasomal subunits in retinal lysates containing 30 µg total protein. Bands were visualized using the LiCor Odyssey imaging system. Each protein was analyzed in at least 3 pairs of 1-month-old WT and overexpressing animals. b Retinal morphology of 3-month-old overexpressing and WT mice. Retinas were embedded in plastic, 1 µm cross-sections were stained by toluidine blue and analyzed by light microscopy. Data are taken from one of the five similar experiments; scale bar : 20 µm. c Chymotrypsin-like proteasomal activity in retinal extracts from 1-month-old overexpressing and WT mice; measurements were performed in the presence or absence of ATP, as indicated. The number of measurements was 10, 7, and 5 for WT, PA28α overexpressing, and PSMD11 overexpressing mice, respectively. The data are shown as mean ± SEM; p values determined across individual preparations are indicated in the text. d Fractionation of proteasomal components in retinal extracts from 2-month-old overexpressing and WT mice by size-exclusion chromatography on a Superose-6 Increase column. Proteins in 0.5 ml fractions were probed by western blotting using antibodies against the β1 subunit of the 20S proteasome core, PSMD11 subunit of the 19S proteasome cap, and PA28α subunit of the11S cap. Data are taken from one of the three similar experiments
false
Reactivity data
Properties and storage information
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Purification technique
Purification notes
Storage buffer
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PSMD1 contributes to the regulation of protein homeostasis through its function in the 26S proteasome complex. This multi-protein complex enables the ATP-dependent degradation of ubiquitinated proteins a critical process for maintaining cellular function. The proteasome's activity ensures the removal of damaged or misfolded proteins and regulates concentrations of specific proteins to maintain cellular processes. Its interaction with other proteasome subunits indicates a strong functional integration within this complex.
Pathways
PSMD1 plays a role in the ubiquitin-proteasome pathway a major pathway for protein catabolism. This pathway is critical for various cellular processes including cell cycle regulation and apoptosis. PSMD1 interacts with other subunits in the proteasome such as PSMA1 and PSMB5 to execute its function. Its connection to these pathways highlights its importance in regulating protein turnover and quality control in cells.
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Target data
Publications (10)
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Nature communications 14:3126 PubMed37253751
2023
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Nature chemical biology 19:55-63 PubMed36577875
2022
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Cell death and differentiation 30:125-136 PubMed35974250
2022
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Cells 11: PubMed35805088
2022
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Proceedings of the National Academy of Sciences of the United States of America 119:e2118479119 PubMed35275792
2022
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Antioxidants & redox signaling 32:636-655 PubMed31903784
2020
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eNeuro 5: PubMed29911170
2018
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Molecular cell 70:906-919.e7 PubMed29804830
2018
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Nature communications 9:1738 PubMed29712894
2018
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Molecular cell 68:1054-1066.e6 PubMed29225035
2017
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Product promise
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