Recombinant Mouse Proteasome subunit beta type-8 (Psmb8)

Code CSB-YP018886MO
MSDS
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Source Yeast
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Code CSB-EP018886MO
MSDS
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Source E.coli
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Code CSB-EP018886MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP018886MO
MSDS
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Source Baculovirus
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Code CSB-MP018886MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Psmb8
Uniprot No.
Alternative Names
Psmb8; Lmp7; Mc13; Proteasome subunit beta type-8; EC 3.4.25.1; Low molecular mass protein 7; Macropain subunit C13; Multicatalytic endopeptidase complex subunit C13; Proteasome component C13; Proteasome subunit beta-5i
Species
Mus musculus (Mouse)
Expression Region
73-276
Target Protein Sequence
TTTLAFKF QHGVIVAVDS RATAGSYISS LRMNKVIEIN PYLLGTMSGC AADCQYWERL LAKECRLYYL RNGERISVSA ASKLLSNMML QYRGMGLSMG SMICGWDKKG PGLYYVDDNG TRLSGQMFST GSGNTYAYGV MDSGYRQDLS PEEAYDLGRR AIAYATHRDN YSGGVVNMYH MKEDGWVKVE SSDVSDLLYK YGEAAL
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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℃/-80℃. 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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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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. May participate in the inflammatory response pathway. Required for adipocyte differentiation. May be 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.
Gene References into Functions
  1. Employing the lymphocytic choriomeningitis virus (LCMV) infection model, we showed that the immunoproteasome subunit LMP7 was absolutely required for the generation of LCMV GP118-125 -specific T cells although the class I mediated presentation of GP118-125 was not dependent on LMP7. PMID: 29067678
  2. Proteostatic responses included a significant increase in the levels of Lmp7, a component of the immunoproteasome. Increased Lmp7 levels and activity were also quantified in postmortem human brains with PD and dementia with Lewy bodies. PMID: 29759483
  3. Psmb8 directly regulates the differentiation of preadipocytes and additionally the differentiation of preadipocytes to mature adipocytes. Psmb8(-/-) mice had slower weight gain, reduced adipose tissue volume, less preadipocyte precursors and preadipocytes, and smaller size of mature adipocytes compared with controls. Loss of Psmb8 activity in 3T3-L1 cells disturbed the differentiation to mature adipocytes. PMID: 27225296
  4. The regulation of miR-451 via the LMP7/NF-kappaB central inflammatory pathway during progression of DN. PMID: 27264074
  5. The authors found that selective inhibition of LMP7 had neither an influence on allograft survival in an major histocompatibility complex-mismatch model nor in a multiple minor mismatch skin transplantation model. PMID: 28582644
  6. LMP7 deficiency decreased inflammatory responses such as macrophage infiltration and chemokine expression while it increased serum adiponection levels. PMID: 26515636
  7. these data support that LMP7 inhibition in the context of BMT modulates allogeneic responses by decreasing endogenous miHA presentation and that the consequential reduction in allogeneic stimulation and cytokine production reduces GVHD development. PMID: 26093043
  8. genetic polymorphism is associated with ovarian cancer and metastasis PMID: 24374040
  9. PSMB8, ALDH1A1, and HSPA4 were identified to be located in ovarian tissues, to regulate 12 cellular pathways, and demonstrate age-dependent dynamic changes in expression profiling. PMID: 24156634
  10. Overexpression of the immunoproteasome LMP7 subunit in antigen-presenting cells due to lipopolysaccharide exposure as well as LMP7 expression in peripheral cells, are required for CD8+ T-cell auto-reactivity. PMID: 23763593
  11. we present novel evidence for the requirement of the beta5i immunosubunit to generate a strong Th2 response during OVA- but not HDM-induced acute asthma. PMID: 23593249
  12. Red blood cells of LMP7-deficient mice were more likely to deform in response to infection with malaria parasites, presumably resulting in higher susceptibility to phagocytosis and in the partial resistance to malaria. PMID: 23527234
  13. Deletion or inhibition of LMP7 suppresses generation of T helper (Th)17 cells but promotes regulatory T cell (Treg) development. PMID: 22984077
  14. Probeta5 predominantly promotes integration into LMP2/MECL-1-containing precursors in IFNgamma-stimulated, LMP7-deficient cells and infected LMP7-deficient mice. PMID: 22768135
  15. LMP7 and MECL1 regulate cytokine expression, suggesting this system represents a novel mechanism for the regulation of cytokines and cytokine signaling PMID: 22398747
  16. We show that mice deficient for the immunosubunits beta5i/low molecular mass polypeptide (LMP7) and beta2i/multicatalytic endopeptidase complex-like-1 develop early-stage multiorgan autoimmunity following irradiation and bone marrow transplantation PMID: 21804012
  17. Findings strongly support the concept that LMP7/MECL-1 proteasomes subunits actively function to regulate LPS-induced NO production by affecting the TRIF/TRAM pathway. PMID: 21455681
  18. A dominant role for the immunoproteasome in CD8+ T cell responses to murine cytomegalovirus. PMID: 21304910
  19. Immunoproteasome LMP7 can at least in part determine subdominance and shape the epitope hierarchy of cytotoxic T cell responses in vivo. PMID: 15356141
  20. Immunoproteasome LMP7 may affect CD8+ T cell responses to only a limited number of viral epitopes; its main biological function may lie elsewhere. PMID: 16002717
  21. phenotype of hyperproliferation of T cells lacking both Mecl1 and LMP7 implicates a specific role for immunoproteasomes in T cell proliferation that is not obviously connected to MHC class I Ag processing PMID: 16547243
  22. Results show that mice lacking LMP7 were highly susceptible to infection with T. gondii and showed a reduced number of functional CD8+ T cells. PMID: 19830724

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Subcellular Location
Cytoplasm. Nucleus.
Protein Families
Peptidase T1B family
Tissue Specificity
Detected in liver (at protein level). Expressed in spleen, thymus, lung, liver, heart and, at a very low level, in kidney. Not expressed in brain nor testis.
Database Links
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