PSMG3 Human

Proteasome Assembly Chaperone 3 Human Recombinant
Cat. No.
BT7865
Source
Escherichia Coli.
Synonyms
Proteasome assembly chaperone 3, PAC-3, hPAC3, PSMG3, PAC3, C7orf48, MGC10911.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

PSMG3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids (1-122 a.a.) and having a molecular mass of 15.2kDa. The PSMG3 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
PSMG3, a chaperone protein, plays a crucial role in the assembly of the 20S proteasome. It is believed to work in conjunction with PSMG1-PSMG2 heterodimers to ensure the accurate formation of proteasomes. PSMG3 interacts with PSMG4, as well as directly with alpha and beta subunits of the 20S proteasome. However, it dissociates before half-proteasomes are formed, likely due to the recruitment of POMP.
Description
Recombinant human PSMG3, expressed in E. coli, is a purified protein with a 20 amino acid His tag at the N-terminus. This single, non-glycosylated polypeptide chain consists of 142 amino acids (residues 1-122), resulting in a molecular weight of 15.2kDa. Purification of PSMG3 is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile filtered.
Formulation
The provided PSMG3 solution has a concentration of 0.5 mg/ml and is formulated in 20mM Tris-HCl buffer at a pH of 8.0 with 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, freezing at -20°C is recommended. Adding a carrier protein such as 0.1% HSA or BSA is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of PSMG3 is greater than 90.0% as assessed by SDS-PAGE analysis.
Synonyms
Proteasome assembly chaperone 3, PAC-3, hPAC3, PSMG3, PAC3, C7orf48, MGC10911.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MEDTPLVISK QKTEVVCGVP TQVVCTAFSS HILVVVTQFG KMGTLVSLEP SSVASDVSKP VLTTKVLLGQ DEPLIHVFAK NLVAFVSQEA GNRAVLLAVA VKDKSMEGLK ALREVIRVCQ VW.

Product Science Overview

Structure and Function

The 20S proteasome is a barrel-shaped complex composed of two outer alpha rings and two inner beta rings. The assembly of this complex is a highly ordered, multistep process that requires the assistance of specific chaperone proteins, including PSMG1, PSMG2, and PSMG3 . PSMG3 cooperates with PSMG1 and PSMG2 to assist in forming alpha rings and mediating half-proteasome formation .

PSMG3 directly binds both alpha and beta proteasome subunits in vitro and dissociates from precursor proteasomes during their maturation, suggesting distinct roles for the PSMG1-PSMG2 heterodimer and PSMG3 in 20S proteasome formation . Knockdown of PSMG3 via small interfering RNA in HEK293T cells impairs alpha-ring formation, highlighting its essential role in proteasome assembly .

Gene and Protein Information

The PSMG3 gene is located on chromosome 7p22.3 . The human PSMG3 protein consists of 122 amino acids and has an apparent molecular mass of approximately 14 kDa . Database analysis has revealed PSMG3 orthologs in various species, including mouse, chicken, Xenopus, zebrafish, rice, maize, tunicate, Cryptococcus, and Dictyostelium .

Recombinant Human PSMG3

Recombinant human PSMG3 protein, often tagged with a His-tag for purification purposes, is expressed in E. coli and purified using conventional chromatography techniques . This recombinant protein is used in research to study the assembly and function of the proteasome complex.

Research and Clinical Implications

Understanding the role of PSMG3 in proteasome assembly has significant implications for research into various diseases, including neurodegenerative disorders and cancers, where proteasome function is often dysregulated. The study of PSMG3 and its interactions with other proteasome assembly chaperones can provide insights into the mechanisms underlying proteasome-related diseases and potentially lead to the development of therapeutic interventions.

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