DNAJC5 Antibody Blocking Peptide(bs-12944P)-500ug

DNAJC5 Antibody Blocking Pepti

de(bs-12944P)-500ug
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  • bs-12944P
  • 2025年10月16日
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      500ug

    产品编号bs-12944P
    英文名称DNAJC5 Antibody Blocking Peptide
    中文名称半胱氨酸延伸蛋白α封闭多肽
    英文别名CLN 4; CLN4; CLN4B; CSP; cysteine string protein alpha; Cysteine string protein; DJC5; DnaJ (Hsp40) homolog subfamily C member 5; DnaJ homolog subfamily C member 5; DNAJC 5; Dnajc5; DNAJC5A; DNJC5_HUMAN; NCL.
    纯化方法HPLC
    研究领域

    Neuroscience > Cell Type Marker > Neuron marker > Synapse marker

    亚基Homodimer (Probable). Interacts with the chaperone complex consisting of HSC70 and SGTA (By similarity).
    亚细胞定位Membrane. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
    组织特异性Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart.
    翻译后修饰Fatty acylated. Heavily palmitoylated in the cysteine string motif.
    相似性Contains 1 J domain.
    功能May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings.
    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Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

     

     

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