Recombinant Human Proteasome Subunit Beta Type-8 (PSMB8) Protein (His-SUMO&Myc)

Name: Recombinant Human Proteasome Subunit Beta Type-8 (PSMB8) Protein (His-SUMO&Myc)
Brand: Beta LifeScience
SKU: BLC-02850P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Proteasome Subunit Beta Type-8 (PSMB8) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P28062
Target Symbol	PSMB8
Synonyms	ALDD; D6S216; D6S216E; Large multifunctional peptidase 7; Large multifunctional protease 7; LMP 7; LMP7; Low molecular mass protein 7; Low molecular weight protein 7; Macropain subunit C13; MGC1491; Multicatalytic endopeptidase complex subunit C13; NKJO; OTTHUMP00000062981; Protease component C13; Proteasome (prosome macropain) subunit beta type 8; Proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7); Proteasome beta 8 subunit; Proteasome catalytic subunit 3i; Proteasome component C13; Proteasome related gene 7; Proteasome subunit beta 5i; Proteasome subunit beta 8; Proteasome subunit beta type 8; Proteasome subunit beta type; Proteasome subunit beta type-8; Proteasome subunit beta-5i; Proteasome subunit Y2; PSB8_HUMAN; PSMB 8; PSMB5i; PSMB8; Really interesting new gene 10 protein; RING 10; RING10; Y2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-SUMO&C-Myc
Target Protein Sequence	TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ
Expression Range	73-276aa
Protein Length	Full Length of Mature Protein
Mol. Weight	42.7 kDa
Research Area	Cell Biology
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	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein. Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	Peptidase T1B family
Database References	HGNC: 9545 OMIM: 177046 KEGG: hsa:5696 STRING: 9606.ENSP00000364016 UniGene: PMID: 29428669 The present study illustrated that the carriage of LMP7 rs2071543-AA and TAP2 rs1800454-AA had a negative effect on treatment response to pegIFN-alpha/RBV among genotype 1 patient with chronic hepatitis C (CHC) in a Chinese Han population PMID: 29039469 JAK1 mutations are highly frequent in microsatellite unstable endometrial cancer, not associated with survival, but are associated with impaired upregulation of LMP7 and HLA class I and may therefore facilitate immune escape PMID: 27213585 Upregulation of proteasome subunit beta type 8 PSMB8 and PDZ binding kinase PBK was confirmed by real-time reverse transcription-PCR analysis. PMID: 26894977 This is the first study to report that the heterozygous LMP2 R/C and homozygous C/C genotypes increase susceptibility to ESCC in the Kazakh population and that the heterozygous LMP7 Q/K genotype decreases susceptibility to ESCC in this population PMID: 29073155 PSMB8 rs2071464 was associated with generalized and active vitiligo from Gujarat whereas TAP1 rs1135216 showed no association. The down-regulation of PSMB8 in patients with risk genotype 'CC' advocates the vital role of PSMB8 in the autoimmune basis of vitiligo. PMID: 28700671 results suggest that PSMB8 is a predictive marker of preoperative radiosensitivity in locally advanced rectal cancer patients. PMID: 28721901 Data show that tight junction protein 1 (TJP1) suppressed expression of the catalytically proteasome subunits LMP7 and LMP2, decreased proteasome activity, and enhanced proteasome inhibitor sensitivity in vitro and in vivo through suppression of EGFR/JAK1/STAT3 signaling. PMID: 27132469 there was no significant difference with respect to the genotypic frequencies of the SNPs in PSMB8, TAP1, and TAP2 loci in Parkinson's disease patients PMID: 27098790 We described a Brazilian patient with CANDLE syndrome possessing a novel mutation in the PSMB8 gene. PMID: 26567544 designed siRNAs that efficiently silence LMP2, LMP7 and MECL-1 gene expression. PMID: 26944796 Proteasome beta5i Subunit Deficiency Affects Opsonin Synthesis and Aggravates Pneumococcal Pneumonia. PMID: 27100179 demonstrated that patients with the LMP-7 CA/AA genotypes were more likely to have advanced fibrosis scores than those bearing the CC genotype PMID: 27156327 lupus nephritis showed up-regulation of the immunoproteasome subunit LMP7 in tubular epithelial cells associated with type I interferon signature. PMID: 25889472 Comparison with reference profiles of sorted immune cells and healthy muscle confirmed upregulation of PSMB8 and -9 in myositis biopsies beyond infiltration related changes. PMID: 25098831 The LMP7 gene promoter methylation and protein downregulation were correlated at high extent in Kazakh's ESCC patients, and may explain the epigenetic regulation on gene expression. PMID: 23283737 In patients with primary Sjogren's syndrome, the expression of LMP7 (but not LMP2) is up-regulated in the labial gland. PMID: 21529441 The MAGE-C(2336-344) antigenic peptide is produced by the immunoproteasome and intermediate proteasome beta1i-beta5i, but not by the standard proteasome nor intermediate proteasome beta5i. PMID: 22925930 high risk of colon cancer was associated with LMP7-K/Q genotype and low risk with LMP7-Q/Q genotype; results suggest the presence of LMP7-K can reduce formation of immunoproteasomes and thus peptide processing, followed by reduced peptide-HLA presentation, a crucial factor in the immune response against cancer PMID: 22037870 CANDLE syndrome is caused by mutations in PSMB8, a gene recently reported to cause "JMP" syndrome in adults. PMID: 21953331 the genetic variant within the LMP2/LMP7 gene would increase the risk of intestinal M. tuberculosis infection. PMID: 21303409 found a homozygous missense mutation (G197V) in immunoproteasome subunit, beta type 8 (PSMB8), which encodes one of the beta subunits induced by IFN-gamma in patients from 2 consanguineous families with lipodystrophy PMID: 21881205 Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome PMID: 21852578 we identified two single nucleotide polymorphisms within the beta5i/LMP7-encoding gene sequences, which were in strong linkage disequilibrium, as independent genetic risk factors for type 1 diabetes development in humans PMID: 21804012 HLA-I, TAP1, CNX, LMP7, Erp57, Tapasin and ERAP1 were down-regulated in 68%, 44%, 48%, 40%, 52%, 32% and 20% of esophageal squamous cell carcinoma lesions then, respectively. PMID: 21362330 PSMB8 encodes a catalytic subunit of the 20S immunoproteasomes called beta5i. Immunoproteasome-mediated proteolysis generates immunogenic epitopes presented by major histocompatibility complex (MHC) class I molecules PMID: 21129723 In a southern Spanish population, no differences were observed in the frequencies of the LMP and TAP genotypes between brucellosis patients and controls. PMID: 20470844 The frequencies of LMP7 genotypes and alleles showed no significant differences among different ages of diabetic onset. PMID: 11793848 Impaired expression of proteasome subunits is involved in the loss of HLA class I expression in human colon cancer cells. PMID: 12519221 LMP7 is associated with vitiligo. PMID: 14551602 upregulation by IRF-1 and interferon gamma PMID: 15907481 Expression of LMP7E1 is cancer cells is an additional strategy of oncogenesis PMID: 16423992 two inducible subunits of the proteasome, lmp2 and lmp7, are transcriptionally up-regulated by heat shock; heat-shocked cells show enhanced presentation of immunoproteasome-dependent MHC I antigenic epitopes, but not immunoproteasome-independent epitopes PMID: 17142736 LMP7-145 site is associated with the risk of HBV infection. PMID: 17525827 study found strong associations of psoriasis with variant alleles of LMP and TAP PMID: 17581627 Patients with proteinuria greater than 0.5 g/1.73 m(2)/day had a significant switch of the chymotryptic-like beta5 protease to the LMP7 subunit, but this did not occur in patients with idiopathic nephrotic syndrome PMID: 19037255 The different proteasome profiles of (IFN)DC and (IL-4)DC were associated with a greater ability of (IFN)DC to present an immunodominant epitope that requires LMP7 expression for its processing. PMID: 19065646 Downregulation of LMP7 is associated with acute myeloid leukaemic blasts. PMID: 19148137 the immunoproteasome appears to be a key link between inflammatory factors and the control of vascular cell apoptosis and may thus be an important factor in plaque rupture and myocardial infarction. PMID: 19443843 LMP7 gene polymorphism showed identical frequency of different genotypes in hypertensive patients (Lys/Lys--92.4%, Lys/Gln--7.6%, Gln/Gln--0%) and healthy people (97.3%, 2.7%, 0% correspondingly; P = 0.16). PMID: 19526842 the reduced LMP7-mRNA level by HSV-1 could be of biological importance, since the virus could escape/hide from immune system of the host and establish latency processes. PMID: 19619915 Interferon-induced PSMB8/LMP7 accelerates the degradation of Mcl-1 and increases the sensitivity of vascular lesion cells to apoptosis induced by fas ligation. PMID: 19443843

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.