Recombinant Human Proteasome Activator Complex Subunit 3 (PSME3) Protein (GST)

Name: Recombinant Human Proteasome Activator Complex Subunit 3 (PSME3) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08298P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Proteasome Activator Complex Subunit 3 (PSME3) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P61289
Target Symbol	PSME3
Synonyms	11S regulator complex gamma subunit; 11S regulator complex subunit gamma; Activator of multicatalytic protease subunit 3; Ki; Ki antigen; Ki nuclear autoantigen; Ki, PA28 gamma; PA28 gamma; PA28g; PA28gamma; Proteasome (prosome, macropain) activator subunit 3 (PA28 gamma, Ki); Proteasome (prosome, macropain) activator subunit 3; Proteasome activator 28 gamma; Proteasome activator 28 subunit gamma; Proteasome activator complex subunit 3; Proteasome activator subunit 3; PSME3; PSME3_HUMAN; REG GAMMA; REG-gamma
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	ASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAET
Expression Range	2-252aa
Protein Length	Partial
Mol. Weight	56.1kDa
Research Area	Apoptosis
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition.
Subcellular Location	Nucleus. Cytoplasm.
Protein Families	PA28 family
Database References	HGNC: 9570 OMIM: 605129 KEGG: hsa:10197 STRING: 9606.ENSP00000293362 UniGene: PMID: 29020881 data show that PIP30 deeply affects PA28gamma interactions with cellular proteins, including the 20S proteasome, demonstrating that it is an important regulator of PA28gamma in cells and thus a new player in the control of the multiple functions of the proteasome within the nucleus. PMID: 29934401 the ubiquitin-independent REGgamma proteasome regulates energy homeostasis PMID: 27511885 High expression of REGg seemed positively correlated with T-stage and lymph node metastasis in papillary thyroid carcinoma tissues. PMID: 29509725 This study demonstrates that REGgamma is a central molecule in the development of melanoma by regulating Wnt/beta-catenin pathway. PMID: 28605165 that Proteasome activator subunit 3 induces epithelial-mesenchymal transition with inducing the expression of CSC markers and influencing the tumor immune microenvironment in breast cancer PMID: 28529105 PSME3 plays an oncogenic role in pancreatic cancer by inhibiting c-Myc degradation to promote glycolysis. PMID: 27756569 Study demonstrated that the gene therapy with proteasome activator, PA28gamma can improve ubiquitin-proteasome system function as well as behavioral abnormalities in Huntington's disease model mice PMID: 26944602 Surrogate Prognostic Biomarkers in OSCC: The Paradigm of PA28gamma Overexpression. PMID: 26425675 PA28gamma in OSCC tumor tissues were significantly high expression than those in normal tissues. PMID: 26425691 REGgamma acts in skin tumorigenesis mediating MAPK/p38 activation of the Wnt/beta-catenin pathway. PMID: 25908095 Results show molecular cloning of a novel transcript variant encoding a truncated form of PA28G likely involved in cell cycle regulation and apoptosis. PMID: 25936920 In a p53-dominated cellular context, pro-apoptotic signaling might be overcome by PA28gamma-mediated caspase inhibition. PMID: 26201457 Our results suggest that the high expression of REGgamma might predict metastasis and poor prognosis in breast cancer. PMID: 25550823 Increased PA28gamma sera levels were prognostic of disease activity in rheumatoid arthritis. PMID: 25482151 Data suggest levels of gene expression of both PSME3 (proteasome activator subunit 3) and DUSP3 (dual specificity phosphatase 3) are associated with susceptibility to Staphylococcus aureus infection/sepsis in humans and in mouse disease model. PMID: 24901344 Examination of EC and normal endometrium specimens confirmed the oncogenic role of REGgamma, in that REGgamma was more highly overexpressed in p53-positive specimens than in p53-negative specimens. PMID: 25697482 PA28 gamma and p53 form a negative feedback loop that maintains the balance of p53 and PA28gamma in the cells. PMID: 24531141 Our data indicate that miR-7-5p has a critical function through blocking REGgamma in breast cancer cells. PMID: 25511742 REGgamma expression is positively correlated with ERalpha status and poor clinical prognosis in ERalpha positive breast cancer patients PMID: 25490392 The results link Chk2 and REGgamma to the mechanism underlying the DBC1-dependent SIRT1 inhibition. PMID: 25361978 PKA turnover by the REGgamma-proteasome modulates FoxO1 cellular activity and VEGF-induced angiogenesis. PMID: 24560667 Expression of PA28gamma contributes to carcinogenesis and progression of colorectal cancer. PMID: 24113729 The REGgamma-proteasome pathway is regulated differentially by p53/TGF-beta signaling and mutant p53 in cancer cells. PMID: 24157709 the regulation of REGgamma assembly and activity, suggesting a potential venue for the intervention of the ubiquitin-independent REGgamma proteasome activity. PMID: 23612972 PA28gamma acts as a co-repressor of HTLV-1 p30 to suppress virus replication and is required for the maintenance of viral latency. PMID: 23104922 statistical analysisof laryngeal carcinomas revealed that there was a positive relationship between the level of REGgamma and the expression of p53 and p2; study suggests that REgamma overexpression can facilitate the growth of laryngeal cancer cells PMID: 22938444 PA28gamma is an ATM target, being recruited to DNA damage sites where it is required for rapid accumulation of proteasomes, and the timely coordination of DNA double-strand break repair. PMID: 22134242 REG-gamma associates with and modulates the abundance of nuclear activation-induced deaminase. PMID: 22042974 A previously unrecognized mechanism regulating the activity of the proteasome activator REGgamma, is reported. PMID: 21445096 High REGgamma expression is associated with breast cancer and its metastatic lymph nodes. PMID: 20467919 HTLV-1 p30 interacts with ATM and REGgamma to increase viral spread by facilitating cell survival PMID: 21216954 REGgamma regulates cellular distribution of p53 by facilitating its multiple monoubiquitylation and nuclear export. PMID: 21084564 REGgamma-mediated p53 proteolysis contributes, as least in part, to the proviral function of REGgamma; the host REGgamma pathway is utilized and modified during CVB3 infection to promote efficient viral replication PMID: 20719955 REGgamma is present in many tissues and the highest expression is in the testis. PMID: 20494959 PA28gamma participates not only in the pathogenesis but also in the propagation of HCV by regulating the degradation of the core protein in both a ubiquitin-dependent and ubiquitin-independent manner PMID: 20683941 Overexpression of the proteasome activator subunit PA28gamma recovered proteasome function in Huntington disease cells. It improved cell viability in mutant huntingtin-expressing striatal neurons exposed to pathological stressors. PMID: 17327906 Data suggest REGgamma promoting tumor growth is a process involving multiple factor mechanisms. PMID: 19656465 PA28gamma is an endogenous substrate for caspase-3 and -7 PMID: 11859414 Ki antigen contains multiple epitopes recognized by autoimmune sera PMID: 12784391 PA28 gamma novel regulator of Cajal body integrity in response to ultraviolet radiation. PMID: 17088425 REGgamma proteasome activator is involved in the maintenance of chromosomal stability. PMID: 18235248 PA28gamma, a proteasome activator that inhibits apoptosis and promotes cell cycle progression through unknown mechanisms, exerts an effect as a cofactor in the MDM2-p53 interaction. PMID: 18309296 PA28gamma/REGgamma, which specifically binds to hepatitis c virus core protein, is required for the virulence of the core protein[review] PMID: 18321762 mammalian proteasomes cannot degrade glutamine-expanded regions within pathogenic polyQ-expanded proteins, such as Huntingtin PMID: 18343811 PA28gamma specifically binds to hepatitis C virus core protein and is involved in its degradation. PMID: 19091860 these results underline a new role for REGgamma in the control and regulation of promyelocytic leukemia subnuclear structures. PMID: 19556897

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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