SARS-CoV-2 (2019-nCoV) Spike RBD (E484K) Mutated Peptide(bs-24790P)-500ug

SARS-CoV-2 (2019-nCoV) Spike R

BD (E484K) Mutated Peptide(bs-24790P)-500ug
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  • 2025年10月16日
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      500ug

    产品编号bs-24790P
    英文名称SARS-CoV-2 (2019-nCoV) Spike RBD (E484K) Mutated Peptide
    中文名称SARS冠状病毒2 Spike蛋白RBD(E484K)突变多肽
    英文别名SARS-CoV-2 spike protein; 2019-nCOV Spike protein; Spike glycoprotein; Spike protein S1; Spike protein RBD; Surface glycoprotein; SPIKE_SARS2; 2019-nCOV Spike protein (E484K).
    中文别名SARS冠状病毒2 Spike突变蛋白RBD(E484K)多肽
    性状Lyophilized
    纯化方法HPLC
    研究领域

    Microbiology > Organism > Virus > RNA Virus > ssRNA positive strand virus > SARS Coronavirus

    亚基Spike glycoprotein:
    Homotrimer; each monomer consists of a S1 and a S2 subunit (PubMed:32155444, PubMed:32075877). The resulting peplomers protrude from the virus surface as spikes (By similarity).
    Interacts with the accessory proteins 3a and 7a.
    Spike protein S1:
    Binds to human ACE2.
    亚细胞定位Virion membrane ; Single-pass type I membrane protein ; Host endoplasmic reticulum-Golgi intermediate compartment membrane ; Single-pass type I membrane protein ; Host cell membrane ; Single-pass type I membrane protein ;
    Note: Accumulates in the endoplasmic reticulum-Golgi intermediate compartment, where it participates in virus particle assembly. Colocalizes with S in the host endoplasmic reticulum-Golgi intermediate compartment. Some S oligomers are transported to the host plasma membrane, where they may mediate cell-cell fusion.
    组织特异性The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes.
    Specific enzymatic cleavages in vivo yield mature proteins. The precurssor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins (PubMed:32155444). Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor (By similarity). The presence of a furin polybasic cleavage site sets SARS-CoV-2 S apart from SARS-CoV S that possesses a monobasic S1/S2 cleavage site processed upon entry of target cells (PubMed:32155444).
    Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface.
    翻译后修饰The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes.
    Specific enzymatic cleavages in vivo yield mature proteins. The precurssor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins (PubMed:32155444). Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor (By similarity). The presence of a furin polybasic cleavage site sets SARS-CoV-2 S apart from SARS-CoV S that possesses a monobasic S1/S2 cleavage site processed upon entry of target cells (PubMed:32155444).
    Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface.
    功能attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.
    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The SARS-CoV-2 spike (S) protein is the target of vaccine design efforts to end the COVID-19 pandemic. Despite a low mutation rate, isolates with the D614G substitution in the S protein appeared early during the pandemic, and are now the dominant form worldwide. Here, we analyze the D614G mutation in the context of a soluble S ectodomain construct.

     

     

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