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  4. Recombinant Mouse Dysferlin (Dysf), partial

Recombinant Mouse Dysferlin (Dysf), partial

  • 中文名称：
    小鼠Dysf重组蛋白
  • 货号：
    CSB-YP884154MO
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 中文名称：
    小鼠Dysf重组蛋白
  • 货号：
    CSB-EP884154MO
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 中文名称：
    小鼠Dysf重组蛋白
  • 货号：
    CSB-EP884154MO-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    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.

  • 其他：
  • 中文名称：
    小鼠Dysf重组蛋白
  • 货号：
    CSB-BP884154MO
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 中文名称：
    小鼠Dysf重组蛋白
  • 货号：
    CSB-MP884154MO
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
  • Uniprot No.：
  • 别名：
    Dysf; Fer1l1Dysferlin; Dystrophy-associated fer-1-like protein; Fer-1-like protein 1
  • 种属：
    Mus musculus (Mouse)
  • 蛋白长度：
    Partial
  • 蛋白标签：
    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.
  • 产品提供形式：
    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.
  • 复溶：
    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.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    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.
  • 货期：
    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.
  • 注意事项：
    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.

产品评价

靶点详情

  • 功能：
    Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress.
  • 基因功能参考文献：
    1. Our data suggest that dysferlin modulates SR Ca(2+) release in skeletal muscle, and that in its absence osmotic shock injury causes increased RyR1-mediated Ca(2+) leak from the SR into the cytoplasm. PMID: 28568606
    2. dysferlin has membrane tubulating capacity and that it shapes the T-tubule system. PMID: 28104817
    3. These results provide one mechanism by which the C57BL/6J background intensifies dysferlinopathy, giving rise to a more severe form of muscular dystrophy in the Dysf(B6) mouse model through increased membrane leak and inflammation. PMID: 27070822
    4. dysferlin-deficient cardiomyocytes showed slower Ca2+ re-sequestration. Dysferlin deficiency blunted the beta-adrenergic effect on relaxation and pumping function of ex vivo working hearts. PMID: 26415898
    5. Using both naturally occurring and genetically engineered dysferlin-deficient mice, the s demonstrated that loss of dysferlin confers increased susceptibility to coxsackievirus infection and myocardial damage. PMID: 26073173
    6. By targeting DYSF premRNA introns harbouring differentially defined 3' splice sites (3' SS), we found that target introns encoding weakly defined 3' SSs were trans-spliced successfully in vitro in human myoblasts also in vivo in skeletal muscle of mice. PMID: 25904108
    7. Dysferlin does not regulate cardiac voltage-dependent ion channels in cardiomyocytes. PMID: 26112643
    8. results show that dysferlin exerts protective effects on the fukutin(Hp/-) FCMD mouse model, and the (dysferlin(sjl/sjl): fukutin(Hp/-)) mice will be useful as a novel model for a recently proposed antisense oligonucleotide therapy for FCMD PMID: 25198651
    9. These novel observations of conspicuous intermyofibrillar lipid and progressive adipocyte replacement in dysferlin-deficient muscles. PMID: 24685690
    10. Laser-wounding induced rapid recruitment of local dysferlin-containing sarcolemma, formation of stable dysferlin accumulations surrounding lesions, endocytosis of dysferlin, and formation of large cytoplasmic vesicles from distal regions of the fiber. PMID: 24784578
    11. Dysferlin, a calcium-triggered exocytotic membrane repair protein, is required for the cytoprotective effects of TRAF2-mediated signaling after myocardial ischemia reperfusion injury. PMID: 24572254
    12. Alternate splicing of the dysferlin C2A domain confers Ca(2+)-dependent and Ca(2+)-independent binding for membrane repair. PMID: 24239457
    13. these findings demonstrate the importance of dysferlin and myoferlin for transverse tubule function and in the genesis of muscular dystrophy. PMID: 24177035
    14. Data indicate that bone marrow transplantation (BMT) improved functional and histological outcome in the A/J Dysfprmd mouse model. PMID: 23777246
    15. discovery of dysferlin as a t-tubule protein that stabilizes stress-induced Ca(2+) signaling offers a therapeutic avenue for limb girdle muscular dystrophy 2B and Miyoshi myopathy patients. PMID: 24302765
    16. Dysferlin-peptides reallocate mutated dysferlin thereby restoring function PMID: 23185377
    17. The results suggest that decreased myotube fusion in dysferlin deficiency is attributable to intrinsic inflammatory activation and can be improved using anti-inflammatory mediators. PMID: 22560623
    18. Mice with dystrophin and dysferlin double mutations develop mixed sarcomas with variable penetrance and latency. PMID: 22682622
    19. C2 domains mediate high affinity self-association of dysferlin in a parallel homodimer PMID: 22110769
    20. We observed that dysferlin-deficient muscles recovered the tetanic force production to the same extent as their WT counterparts following a saponin exposure. Data suggest that dysferlin is unlikely involved in repairing saponin-induced membrane damage. PMID: 21941430
    21. Data suggest dysferlin has an important function in the internal membrane systems of skeletal muscle, involved in calcium homeostasis and excitation-contraction coupling. PMID: 22043020
    22. Data show that dysferlin is not only a membrane repair protein but also important for muscle membrane maintenance and integrity. PMID: 21079765
    23. Dysferlin function in intracellular vesicles and its implication in muscle membrane resealing. PMID: 21119217
    24. Using dysferlin-deficient mouse myocytes, demonstrate that membrane blebbing in skeletal muscle myotubes in response to hypotonic shock requires dysferlin. PMID: 20558759
    25. Dysf deficiency led to increased expression of complement factors in muscle, while muscle-specific transgenic expression of dysf normalized the expression of complement factors and eliminated the dystrophic phenotype present in dysf-null mice. PMID: 21060153
    26. loss of dysferlin in endothelial cells resulted in deficient adhesion followed by growth arrest and impaired angiogenic response PMID: 20724702
    27. Data show that components of the inflammasome pathway are specifically up-regulated and activated in dysferlin-deficient but not in dystrophin-deficient and normal muscle, and suggest that muscle cells can actively participate in inflammasome formation. PMID: 20413686
    28. Our goal was to define a functional signature for skeletal muscles that lack dysferlin PMID: 20544921
    29. In the absence of dysferlin, cardiomyocyte membrane damage occurs and is localized to the intercalated disk and sarcoplasm PMID: 19875504
    30. Dysferlin-null myofibers can survive contraction-induced injury for at least 3 days but are subsequently eliminated by necrosis and inflammation. Myogenesis to replace lost fibers does not appear to be significantly compromised in dysferlin-null mice. PMID: 19923419
    31. Data show that restoration of dysferlin in skeletal muscle fibers is sufficient to rescue Dysf-deficient mice, although its mild overexpression does not appear to functionally enhance membrane repair in other models of muscular dystrophy. PMID: 19834057
    32. SJL/J mice show spontaneous myopathy and have a mutation in the dysferlin gene, a gene which is also mutated in human limb-girdle muscular dystrophy type 2B (LGMD2B) PMID: 11891182
    33. Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains. PMID: 11959863
    34. Dysferlin-null mice maintain a functional dystrophin-glycoprotein complex but nevertheless develop a progressive muscular dystrophy PMID: 12736685
    35. dysferlin binds to annexins A1 and A2 and has a role in Ca2+-dependent repair of sarcolemmal injury through a process of vesicle fusion PMID: 14506282
    36. Data show that affixin is a dysferlin binding protein that colocalizes with dysferlin at the sarcolemma of normal skeletal muscle. PMID: 15835269
    37. Overexpression of CAR may lead to physiological dysfunction by impairing sarcolemmal repair (through dysferlin deficiency). PMID: 17148677
    38. Study examined the degradation of normal and mutant (L1341P) dysferlin; mutant dysferlin aggregates in the ER-stimulated autophagosome formation to engulf them via activation of ER stress-eIF2alpha phosphorylation pathway. PMID: 17331981
    39. dysferlin-mediated membrane repair is important for maintaining membrane integrity of cardiomyocytes, particularly under conditions of mechanical stress PMID: 17607357
    40. Dysf was detected immunohistochemically in wild type mice, but not knockout mice. PMID: 17612291
    41. These data suggest that disturbances in dysferlin as well as Z-line proteins and transcription factors particularly under mechanical stress cause cardiomyopathy. PMID: 17828519
    42. Caveolin-1 or Caveolin-3, but not specific caveolin mutants, inhibit endocytosis of dysferlin through a clathrin-independent pathway colocalizing with internalized glycosylphosphatidylinositol-anchored proteins. PMID: 18096699
    43. Data show that dysferlin-null muscles produce higher contractile torque, and are equally susceptible to initial injury but recover from injury more slowly. PMID: 18815587
    44. Gadofluorine M-enhanced MR imaging may be of value in monitoring dysferlin-deficient muscular dystrophy disease progression in this animal model and could prove to be a useful tool in following the course of chronic muscle diseases in humans. PMID: 19001151
    45. Results suggest that dysferlin functions as a membrane fusion protein in the wound healing system of plasma membrane, and that the defect in dysferlin causes insufficient membrane fusion resulting in accumulation of vesicles. PMID: 19218742
    46. Muscle regeneration is attenuated in a mouse model of dysferlinopathy. PMID: 19286669
    47. The presence or absence of dysferlin does not have any consequences for the triggering or effector phase of experimental autoimmune encephalomyelitis. PMID: 19301206

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  • 相关疾病：
    Defects in Dysf are the cause of a slowly progressive muscular dystrophy observed in SJL mice. It affects primarily the proximal muscles and it is inherited as autosomal recessive trait.
  • 亚细胞定位：
    Cell membrane, sarcolemma; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Cell membrane.
  • 蛋白家族：
    Ferlin family
  • 组织特异性：
    Expressed in skeletal and cardiac muscles (at protein level). Expressed in skeletal muscle and heart. Also found in brain, liver and kidney.
  • 数据库链接：

    KEGG: mmu:26903

    STRING: 10090.ENSMUSP00000080579

    UniGene: Mm.220982