PDZRN3 Antibody Blocking Peptide(bs-9191P)-500ug

PDZRN3 Antibody Blocking Pepti

de(bs-9191P)-500ug
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  • bs-9191P
  • 2025年10月16日
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      500ug

    产品编号bs-9191P
    英文名称PDZRN3 Antibody Blocking Peptide
    中文名称SEMCAP3蛋白封闭多肽
    英文别名Ligand of Numb protein X 3; likely ortholog of mouse semaF cytoplasmic domain associated protein 3; LNX3; PDZ domain containing ring finger 3; Protein SEMACAP3; SEMACAP3; Semaphorin cytoplasmic domain associated protein; PZRN3_HUMAN.
    纯化方法HPLC
    研究领域

    Cell Biology > Cell Cycle > Cell differentiation

    Developmental Biology > Organogenesis > Skeletal development > Muscle

    亚基Interacts with NLGN1 and EFNB2 (By similarity). Interacts with UBE2D2 and with MUSK via the first PDZ domain (By similarity).
    组织特异性SEMCAP3 is widely expressed at high levels, and is thought to be involved in protein/zinc ion binding.
    翻译后修饰Auto-ubiquitinated (By similarity).
    相似性Contains 2 PDZ (DHR) domains.
    Contains 1 RING-type zinc finger.
    Contains 1 TRAF-type zinc finger.
    功能E3 ubiquitin-protein ligase. Plays an important role in regulating the surface level of MUSK on myotubes. Mediates the ubiquitination of MUSK, promoting its endocytosis and lysosomal degradation. Might contribute to terminal myogenic differentiation (By similarity).
    保存条件Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    注意事项This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
    背景资料PDZRN3 contains a RING-finger motif in its N-terminal region, two PDZ domains in its central region and a consensus-binding motif for PDZ domains at its C-terminus. It was identified in silico as a homolog of the protein known as LNX1 or SEMCAP1, which possesses ubiquitin ligase activity and binds the membrane protein Semaphorin 4C. However, PDZRN3 itself has not previously been characterized. We have now evaluated the properties and functions of PDZRN3. The PDZRN3 gene was shown to be expressed in various human tissues including the heart, skeletal muscle and liver and its expression in mouse skeletal muscle was developmentally regulated. Both the differentiation of C2C12 mouse skeletal myoblasts into myotubes and injury-induced muscle regeneration in vivo were found to be accompanied by up-regulation of PDZRN3. The differentiation-associated increase in the expression of PDZRN3 in C2C12 cells follows that of myogenin and precedes that of myosin heavy chain. Depletion of PDZRN3 by RNA interference inhibited the formation of myotubes as well as the associated up-regulation of myosin heavy chain in C2C12 cells. Our data suggest that PDZRN3 plays an essential role in the differentiation of myoblasts into myotubes by acting either downstream or independently of myogenin.

     

     

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