Anti-PSMA1 monoclonal antibody (DCABH-230)

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


Host Species
Antibody Isotype
Species Reactivity
Mouse, Rat, Human
Synthetic peptide corresponding to a region within the C-terminal end of Human Proteasome 20S C2.


Application Notes
WB: 1/1000 - 1/10000; IP: 1/10 - 1/100; IHC-P: 1/100 - 1/250; ICC: 1/250 - 1/500; Flow Cyt: 1/10 - 1/100;
*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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Rabbit IgG Isotype Control CABT-B8382 IA Rabbit PDF Inquiry


Regulation of Endoribonuclease Activity of Alpha-Type Proteasome Subunits in Proerythroleukemia K562 Upon Hemin-Induced Differentiation


Authors: Mittenberg, Alexey G.; Moiseeva, Tatyana N.; Kuzyk, Valeria O.; Barlev, Nickolai A.

The proteasome is the main intracellular proteolytic machine involved in the regulation of numerous cellular processes, including gene expression. In addition to their proteolytic activity, proteasomes also exhibit ATPase/helicase (the 19S particle) and RNAse (the 20S particle) activities, which are regulated by post-translational modifications. In this report we uncovered that several 20S particle subunits: alpha 1 (PSMA6), alpha 2 (PSMA2), alpha 4 (PSMA7), alpha 5 (PSMA5), alpha 6 (PSMA1) and alpha 7 (PSMA3) possess RNAse activity against the p53 mRNA in vitro. Furthermore, we found that the RNAse activity of PSMA1 and PSMA3 was regulated upon hemin-induced differentiation of K562 proerythroleukemia cells. The decrease in RNAse activity of PSMA1 and PSMA3 was paralleled by changes in their status of phosphorylation and ubiquitylation. Collectively, our data support the notion that proteasomal RNAse activity may be functionally important and provide insights into the potential mechanism of p53 repression in erythroleukemia cells by RNAse activity of the 20S alpha-type subunits.

Mechanisms of propofol attenuation of ketamine-induced neonatal brain injury


Authors: Zhao, C. -H.; Li, G-H.; Wang, Q.; Zhao, B.; Wang, Z-B.

OBJECTIVE: We studied the mechanisms of protective effects of propofol on ketamine-induced damage to neonatal cognitive function. MATERIALS AND METHODS: We utilized a rat model of ketamine anaesthesia. Eighty neonatal rats (7 days after birth) were divided into four groups: normal saline group, ketamine group, and low-and high-dose propofol combined with ketamine groups. Six hours after anaesthesia, we obtained hippocampal tissue, and quantified apoptotic index and total protein concentration, and assessed global proteomics changes induced by two tested drugs. The latter changes were documented by two-dimensional electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry. To evaluate cognitive functions, water maze test was applied after animals grew for 21 days. We further repeated proteomics studies at 21 days post-anaesthesia. RESULTS: Ketamine markedly up-regulated apoptotic index and decreased total protein concentration. Propofol dose-dependently reverted these adverse changes. Six hours post-anaesthesia, combined propofol and ketamine administration up-regulated the following proteins in the hippocampus: PD1A3, NDUFB10, HSPA8, ATP5JD, and PSMA1. Furthermore, the following proteins were down-regulated: PPIA, PKM2, GFAP, NSE, PPIA, PKM2, and GFAP. After 21 days, animals treated with ketamine showed marked disturbances in cognitive function as demonstrated by increased time of the water maze test, whereas propofol diminished these changes. In addition, expression of proteins largely normalized in propofol-treated animals, with only two up-regulated proteins (FUBP3 and PRDX5) and three down-regulated proteins (GAPDH, AKR1A1, and VCP). CONCLUSIONS: Adverse effects of ketamine on cognitive function are reverted by propofol, also through beneficial effects on protein expression in the hippocampus.

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