Recombinant Human Proteasome subunit beta type-8 (PSMB8)

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Code CSB-EP018886HU
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity
Greater than 85% as determined by SDS-PAGE.
Target Names
PSMB8
Uniprot No.
Research Area
Cell Biology
Alternative Names
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)
Source
E.coli
Expression Region
73-276aa
Target Protein Sequence
TTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
42.7 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The expression region of this recombinant Human PSMB8 covers amino acids 73-276. The expected molecular weight for the PSMB8 protein is calculated to be 42.7 kDa. This protein is generated in a e.coli-based system. The PSMB8 coding gene included the N-terminal 10xHis-SUMO tag and C-terminal Myc tag, which simplifies the detection and purification processes of the recombinant PSMB8 protein in following stages of expression and purification.

The proteasome subunit beta type-8 (PSMB8) is a subunit of the immunoproteasome, a specialized form of the proteasome involved in antigen presentation. The immunoproteasome plays a crucial role in the major histocompatibility complex (MHC) class I antigen processing pathway, generating peptides for presentation on the cell surface to cytotoxic T lymphocytes. PSMB8 is specifically incorporated into the immunoproteasome, influencing its catalytic properties and enhancing the production of peptides for MHC class I molecules. Research on PSMB8 is significant in understanding immune responses, inflammatory processes, and autoimmune diseases. Dysregulation of PSMB8 has been implicated in various autoimmune conditions, highlighting its potential as a target for therapeutic interventions aimed at modulating immune responses.

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Target Background

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.
Gene References into Functions
  1. PSMB8 is closely associated with migration, proliferation, and apoptosis of glioma cells. PMID: 29428669
  2. 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
  3. 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
  4. Upregulation of proteasome subunit beta type 8 PSMB8 and PDZ binding kinase PBK was confirmed by real-time reverse transcription-PCR analysis. PMID: 26894977
  5. 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
  6. 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
  7. results suggest that PSMB8 is a predictive marker of preoperative radiosensitivity in locally advanced rectal cancer patients. PMID: 28721901
  8. 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
  9. 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
  10. We described a Brazilian patient with CANDLE syndrome possessing a novel mutation in the PSMB8 gene. PMID: 26567544
  11. designed siRNAs that efficiently silence LMP2, LMP7 and MECL-1 gene expression. PMID: 26944796
  12. Proteasome beta5i Subunit Deficiency Affects Opsonin Synthesis and Aggravates Pneumococcal Pneumonia. PMID: 27100179
  13. 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
  14. lupus nephritis showed up-regulation of the immunoproteasome subunit LMP7 in tubular epithelial cells associated with type I interferon signature. PMID: 25889472
  15. 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
  16. 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
  17. In patients with primary Sjogren's syndrome, the expression of LMP7 (but not LMP2) is up-regulated in the labial gland. PMID: 21529441
  18. 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
  19. 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
  20. CANDLE syndrome is caused by mutations in PSMB8, a gene recently reported to cause "JMP" syndrome in adults. PMID: 21953331
  21. the genetic variant within the LMP2/LMP7 gene would increase the risk of intestinal M. tuberculosis infection. PMID: 21303409
  22. 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
  23. Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome PMID: 21852578
  24. 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
  25. 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
  26. 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
  27. 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
  28. The frequencies of LMP7 genotypes and alleles showed no significant differences among different ages of diabetic onset. PMID: 11793848
  29. Impaired expression of proteasome subunits is involved in the loss of HLA class I expression in human colon cancer cells. PMID: 12519221
  30. LMP7 is associated with vitiligo. PMID: 14551602
  31. upregulation by IRF-1 and interferon gamma PMID: 15907481
  32. Expression of LMP7E1 is cancer cells is an additional strategy of oncogenesis PMID: 16423992
  33. 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
  34. LMP7-145 site is associated with the risk of HBV infection. PMID: 17525827
  35. study found strong associations of psoriasis with variant alleles of LMP and TAP PMID: 17581627
  36. 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
  37. 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
  38. Downregulation of LMP7 is associated with acute myeloid leukaemic blasts. PMID: 19148137
  39. 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
  40. 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
  41. 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
  42. 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

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Involvement in disease
Nakajo syndrome (NKJO)
Subcellular Location
Cytoplasm. Nucleus.
Protein Families
Peptidase T1B family
Database Links

HGNC: 9545

OMIM: 177046

KEGG: hsa:5696

STRING: 9606.ENSP00000364016

UniGene: Hs.180062

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