Recombinant Mouse Sharpin (Sharpin)

Code CSB-YP845983MO
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Source Yeast
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Code CSB-EP845983MO
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Source E.coli
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Code CSB-EP845983MO-B
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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-BP845983MO
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Source Baculovirus
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Code CSB-MP845983MO
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Sharpin
Uniprot No.
Alternative Names
Sharpin; Cpdm; Sipl1; Sharpin; Shank-associated RH domain-interacting protein; Shank-interacting protein-like 1; mSIPL1
Species
Mus musculus (Mouse)
Expression Region
1-380
Target Protein Sequence
MSPPAGGAAV AADPASPVVL LAVHAAVRPL GAGQDAEAQP RKLQLIADPE RPGRFRLGLL GTEPGAVSLE WPLEAICYTV RGPNQHELQP PPGGPGTFSV HFLDPEEAQQ WAALVRDATA EGQNGSGSPA PAPAPAMCPI SPPCSSMAQI PKATQPEVDL PQSSGNFKKE ELATRLSQAI AGGDEKAAAQ VAAVLAQHHV ALNVQLMEAW FPPGPIRLQV TVEDATSVLS SSSSAHVSLK IHPHCSIAAL QDQVFSEFGF PPAVQRWVIG RCLCMPERSL ASYGVSQDGD PAFLYLLSAP REVSGQSLQN SKMDRKLGLF PQSLGLPHDL QPSSSSLPSP SQPGWSCPSC TFINASNRPG CEMCSTQRPC AWDPLAAAST
Protein Length
full length 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.

Customer Reviews and Q&A

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Target Background

Function
Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis.
Gene References into Functions
  1. Both Sharpin/Fas and Sharpin/Fasl compound mutant mice developed an auto-inflammatory phenotype similar to that seen in Sharpin null mice, indicating that initiation of apoptosis by FAS signalling is likely not involved in the pathogenesis of this disease. PMID: 28094869
  2. results altogether demonstrate distinct roles of SHARPIN in initiating systemic inflammation and dermatitis. Furthermore, skin inflammation in Sharpin(cpdm) mice is specifically modulated by IL-1beta, highlighting the importance of specific targeted therapies in the IL-1 signaling blockade. PMID: 27892465
  3. Itgb1 inhibition alleviates the chronic hyperproliferative dermatitis phenotype of Sharpin-deficient mice. PMID: 29040328
  4. LUBAC components control TLR3-mediated innate immunity, thereby preventing development of immunodeficiency and autoinflammation. PMID: 27810922
  5. Suppression of SHARPIN impaired cell proliferation, angiogenesis, and invasion and reduced levels of MMP-9 in Prostate cancer cells and reduced the size of Metastatic Lung tumors induced by these cells in mice. PMID: 28230260
  6. Together, these data imply that SHARPIN regulates the normal invasive mammary gland branching morphogenesis in an epithelial cell extrinsic manner by controlling the organisation of the stromal extracellular matrix. PMID: 27974362
  7. Study found that the NZF domain of SHARPIN, but not that of HOIL-1L, is critical for effective protection from programmed cell death by enhancing the recruitment of the linear ubiquitin chain assembly complex to the activated TNFR complex. The binding activity to K63-linked ubiquitin chains that the NZF domain of SHARPIN, but not that of HOIL-1L, possesses appears to be involved in the recruitment. PMID: 26976635
  8. this study reveals a critical function of SHARPIN in TCR-induced NF-kappaB and JNK signalling and thymic Treg cell generation PMID: 26931177
  9. SHARPIN-deficient mice develop a chronic proliferative dermatitis presenting angiogenesis and lymphatic dilatation. PMID: 27794420
  10. Study identifies a role for SHARPIN in TCR signaling whereby it maintains immunological homeostasis and tolerance by regulating Treg cells. PMID: 26829767
  11. severity of the esophagitis was not affected by crossing SHARPIN-deficient mice with lymphocyte-deficient Rag1 null mice PMID: 26321245
  12. Sharpin Controls Osteogenic Differentiation of Mesenchymal Bone Marrow Cells. PMID: 26363054
  13. Data indicate that genetic ablation of caspase-1 and -11 from cpdm mice significantly reduced skin inflammation in sharpin-deficient mice. PMID: 26216893
  14. Our results suggest that SHARPIN plays a significant role in skeletal homeostasis and that this role is strongly regulated through TNF pathways. PMID: 25524971
  15. Sharpin deficiency sensitized primary murine keratinocytes, human keratinocytes, and mouse embryonic fibroblasts to TNF-induced apoptosis. PMID: 25443631
  16. Tnfr1, but not Tnfr2, deficiency suppresses inflammation in sharpin deficient mice. PMID: 25443632
  17. SHARPIN is required for optimal NLRP3 inflammasome activation. PMID: 25637014
  18. Sharpin deficiency results in chronic proliferative dermatitis/ autoinflammatory disease in the absence of B and T lymphocytes and IL4/IL13 signaling. PMID: 24465642
  19. SHARPIN controls lymphocyte migration by endogenously maintaining LFA-1 inactive to allow adjustable detachment of the uropods in polarized cells. PMID: 24210817
  20. RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice. PMID: 24821972
  21. SHARPIN expression is required for the normal development and maintenance, but not initiation, of Peyer's patch PMID: 23424624
  22. loss of Sharpin in mice significantly affects the immune function of dendritic cells and this may partially account for the systemic inflammation and Th2-biased immune response. PMID: 22348129
  23. TNFalpha induced activation of NFkappaB was strongly reduced in hepatocytes from Sharpin-deficient mice. PMID: 22253853
  24. molecular pathways involved in the keratinocyte apoptosis caused by loss of function of SHARPIN PMID: 21620685
  25. SHARPIN inhibits the critical switching of beta1-integrins from inactive to active conformations. PMID: 21947080
  26. the effects of SHARPIN deficiency on the TLR2-induced transcriptome were strikingly correlated with the effects of the recently described hypomorphic L153P/panr2 point mutation in Ikbkg (NEMO), suggesting that SHARPIN and NEMO interact PMID: 21709223
  27. Sharpin appears to regulate bone metabolism in a mouse model (a loss-of-function mutation in Sharpin which results in an osteopenic phenotype). PMID: 21069580
  28. Deletion of SHARPIN drastically reduced the amount of LUBAC, which resulted in attenuated TNF-alpha- and CD40-mediated activation of NF-kappaB in mouse embryonic fibroblasts (MEFs) or B cells from cpdm mice PMID: 21455180
  29. SHARPIN activates NF-kappaB and inhibits apoptosis via distinct pathways in vivo PMID: 21455181
  30. absence of SHARPIN causes hypereosinophilic syndrome with eosinophilic dermatitis by NF-kappaB activation PMID: 20811394
  31. study shows 2 spontaneous mutations in the Sharpin gene, cpdm & cpdm(Dem), cause a chronic proliferative dermatitis phenotype, characterized histologically by severe inflammation, eosinophilic dermatitis & defects in secondary lymphoid organ development PMID: 17538631

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Involvement in disease
Defects in Sharpin are the cause of chronic proliferative dermatitis (cpdm). Cpdm is a spontaneous mutation causing a chronic proliferative dermatitis phenotype, which is characterized histologically by severe inflammation, eosinophilic dermatitis and defects in secondary lymphoid organ development. Mice also display lower total and cortical bone mineral content and bone mineral density, trabecular and cortical bone volume, and trabecular number. TNF-alpha-induced NF-kappa-B activation is attenuated due to inability of the LUBAC complex to mediate linear ubiquitination.
Subcellular Location
Cytoplasm, cytosol. Cell junction, synapse.
Tissue Specificity
Highly expressed in thymus and spleen. Present at high level in splenic B- and T-cells (at protein level).
Database Links
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