Anti-PSMA1 monoclonal antibody (DCABH-223)

Rabbit anti-Human PSMA1 monoclonal antibody for WB, IP, IHC-P, ICC


Host Species
Antibody Isotype
Species Reactivity
Mouse, Rat, Human
A synthetic peptide corresponding to residues in Human Proteasome 20S C2


Application Notes
WB: 1/1000 - 1/10000; IP: 1/10 - 1/100; IHC-P: 1/250 - 1/500; ICC: 1/100 - 1/250;
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.


Alternative Names
PSMA1; proteasome (prosome, macropain) subunit, alpha type, 1; proteasome subunit alpha type-1; HC2; MGC1667; MGC14542
Entrez Gene ID
UniProt ID

Product Background

APC/C-mediated degradation of cell cycle proteins, organism-specific biosystem; APC/C:Cdc20 mediated degradation of Securin, organism-specific biosystem; APC/C:Cdc20 mediated degradation of mitotic proteins, organism-specific biosystem; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1, organism-specific biosystem; Activation of APC/C and APC/C:Cdc20 mediated degradation of mitotic proteins, organism-specific biosystem; Activation of NF-kappaB in B Cells, organism-specific biosystem; Adaptive Immune System, organism-specific biosystem;


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Custom Antibody Labeling

We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More

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Product Name Cat. No. Applications Host Species Datasheet Price Add to Basket


Supplementation with L-carnitine downregulates genes of the ubiquitin proteasome system in the skeletal muscle and liver of piglets


Authors: Keller, J.; Ringseis, R.; Koc, A.; Lukas, I.; Kluge, H.; Eder, K.

Supplementation of carnitine has been shown to improve performance characteristics such as protein accretion in growing pigs. The molecular mechanisms underlying this phenomenon are largely unknown. Based on recent results from DNA microchip analysis, we hypothesized that carnitine supplementation leads to a downregulation of genes of the ubiquitin proteasome system (UPS). The UPS is the most important system for protein breakdown in tissues, which in turn could be an explanation for increased protein accretion. To test this hypothesis, we fed sixteen male, four-week-old piglets either a control diet or the same diet supplemented with carnitine and determined the expression of several genes involved in the UPS in the liver and skeletal muscle. To further determine whether the effects of carnitine on the expression of genes of the UPS are mediated directly or indirectly, we also investigated the effect of carnitine on the expression of genes of the UPS in cultured C2C12 myotubes and HepG2 liver cells. In the liver of piglets fed the carnitine-supplemented diet, the relative mRNA levels of atrogin-1, E(2)14k and Psma1 were lower than in those of the control piglets (P < 0.05). In skeletal muscle, the relative mRNA levels of atrogin-1, MuRF1, E(2)14k, Psma1 and ubiquitin were lower in piglets fed the carnitine-supplemented diet than that in control piglets (P < 0.05). Incubating C2C12 myotubes and HepG2 liver cells with increasing concentrations of carnitine had no effect on basal and/or hydrocortisone-stimulated mRNA levels of genes of the UPS. In conclusion, this study shows that dietary carnitine decreases the transcript levels of several genes involved in the UPS in skeletal muscle and liver of piglets, whereas carnitine has no effect on the transcript levels of these genes in cultivated HepG2 liver cells and C2C12 myotubes. These data suggest that the inhibitory effect of carnitine on the expression of genes of the UPS is mediated indirectly, probably via modulating the release of inhibitors of the UPS such as IGF-1. The inhibitory effect of carnitine on the expression of genes of the UPS might explain, at least partially, the increased protein accretion in piglets supplemented with carnitine.

26S proteasome exhibits endoribonuclease activity controlled by extra-cellular stimuli


Authors: Kulichkova, Valentina A.; Tsimokha, Anna S.; Fedorova, Olga A.; Moiseeva, Tatiana N.; Bottril, Andrew; Lezina, Larissa; Gauze, Larissa N.; Konstantinova, Irina M.; Mittenberg, Alexey G.; Barlev, Nickolai A.

26S proteasome is a large multi-subunit protein complex involved in proteolytic degradation of proteins. In addition to its canonical proteolytic activity, the proteasome is also associated with recently characterized endoribonuclease (endo-RNAse) activity. However, neither functional significance, nor the mechanisms of its regulation are currently known. In this report, we show that 26S proteasome is able to hydrolyze various cellular RNAs, including AU-rich mRNA of c-myc and c-fos. The endonucleolytic degradation of these mRNAs is exerted by one of the 26S proteasome subunits, PSMA5 (alpha 5). The RNAse activity of 26S proteasome is differentially affected by various extra-cellular signals. Moreover, this activity contributes to the process of degradation of c-myc mRNA during induced differentiation of K562 cells, and may be controlled by phosphorylation of the adjacent subunits, PSMA1 (alpha 6) and PSMA3 (alpha 7). Collectively, the data presented in this report suggest a causal link between cell signalling pathways, endo-RNAse activity of the 26S proteasome complex and metabolism of cellular RNAs.

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