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S Monoclonal Antibody

Rare Species
  • 中文名稱：
    S鼠單克隆抗體
  • 貨號：
    CSB-MA33245A0m
  • 規格：
    ￥1320
  • 圖片：
    •   The Binding Activity of SARS-CoV-2-S Antibody with SARS-CoV-2-S1-RBD
      Activity: Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-S1-RBD (CSB-YP3324GMY1) at 2 μg/ml can bind SARS-CoV-2-S Antibody, the EC50 is 32.59 to 39.33 ng/ml.
  • 其他：

產品詳情

  • 產品描述：
    本產品是針對新型冠狀病毒（SARS-CoV-2/2019-nCoV）刺突蛋白（S蛋白）研發的小鼠源單克隆抗體（CUSABIO貨號：CSB-MA33245A0m），該抗體特異性識別病毒表面關鍵S蛋白抗原表位，該靶點作為介導病毒入侵宿主細胞的核心功能蛋白，是疫苗開發及抗病毒藥物研究的重要靶標。經嚴格驗證可兼容ELISA、Western Blot及免疫組化（IHC）三大實驗平臺，具備出色的抗原結合能力和批次穩定性，適用于病毒入侵機制研究、中和抗體篩選、疫苗效力評估等基礎科研領域。該S蛋白單克隆抗體采用雜交瘤技術制備，通過免疫印跡和免疫組化雙重驗證，可精準檢測重組表達或天然構象的S蛋白，為新冠病毒相關科研工作提供可靠工具。在病毒蛋白互作分析、感染模型建立及抗病毒化合物篩選等場景中展現優異性能，是冠狀病毒基礎研究與生物醫藥開發的重要試劑。該產品聚焦于SARS-CoV-2研究、刺突蛋白檢測、新冠病毒抗體開發等科研需求，為病毒學、免疫學及分子生物學領域研究者提供高質量解決方案。
  • Uniprot No.：
  • 別名：
    S; 2; Spike glycoprotein; S glycoprotein; E2; Peplomer protein)
  • 宿主：
    Mouse
  • 反應種屬：
    Human Novel Coronavirus (SARS-CoV-2/ 2019-nCoV)
  • 免疫原：
    Recombinant Human Novel Coronavirus Spike glycoprotein (S) (319-541aa)
  • 免疫原種屬：
    Human Novel Coronavirus (SARS-CoV-2/ 2019-nCoV)
  • 標記方式：
    Non-conjugated
  • 克隆類型：
    Monoclonal
  • 純化方式：
    >95%, Protein G purified
  • 克隆號：
    8A1G8
  • 濃度：
    It differs from different batches. Please contact us to confirm it.
  • 保存緩沖液：
    Preservative: 0.03% Proclin 300
    Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
  • 產品提供形式：
    Liquid
  • 應用范圍：
    ELISA
  • 推薦稀釋比：
    Application Recommended Dilution
    ELISA 1:1000-1:5000
  • Protocols：
  • 儲存條件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 貨期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
  • 用途：
    For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產品評價

靶點詳情

  • 功能：
    attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein. Binding to host NRP1 and NRP2 via C-terminal polybasic sequence enhances virion entry into host cell. This interaction may explain virus tropism of human olfactory epithelium cells, which express high level of NRP1 and NRP2 but low level of ACE2. The stalk domain of S contains three hinges, giving the head unexpected orientational freedom. Uses human TMPRSS2 for priming in human lung cells which is an essential step for viral entry. Can be alternatively processed by host furin. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.; mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.; Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.; May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity.
  • 基因功能參考文獻：
    1. Study presents crystal structure of C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike S protein in complex with human ACE2 (hACE2); hACE2-binding mode similar overall to that observed for SARS-CoV. However, details at the binding interface show that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-CoV receptor-binding domain. PMID: 32378705
    2. crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2 PMID: 32365751
    3. crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2 PMID: 32320687
    4. Out of the two isolates from India compared to the isolates from Wuhan, China, one was found to harbor a mutation in its receptor-binding domain (RBD) at position 407 where, arginine was replaced by isoleucine. This mutation has been seen to change the secondary structure of the protein at that region and this can potentially alter receptor binding of the virus. PMID: 32275855
    5. Structural modeling of the SARS-CoV-2 spike glycoprotein show similar receptor utilization between SARS-CoV-2 and SARS-CoV, despite a relatively low amino acid similarity in the receptor binding module. Compared to SARS-CoV and all other coronaviruses in Betacoronavirus lineage B, an extended structural loop containing basic amino acids were identified at the interface of the receptor binding (S1) and fusion (S2) domains. PMID: 32245784
    6. crystal structure of CR3022, a neutralizing antibody from a SARS patient, in complex with the receptor-binding domain of the SARS-CoV-2 spike (S) protein to 3.1 A; study provides insight into how SARS-CoV-2 can be targeted by the humoral immune response and revealed a conserved, but cryptic epitope shared between SARS-CoV-2 and SARS-CoV PMID: 32225176
    7. SARS-CoV and SARS-CoV-2 spike proteins have comparable binding affinities achieved by balancing energetics and dynamics. The SARS-CoV-2-ACE2 complex contains a higher number of contacts, a larger interface area, and decreased interface residue fluctuations relative to the SARS-CoV-ACE2 complex. PMID: 32225175
    8. Interaction interface between cat/dog/pangolin/Chinese hamster ACE2 and SARS-CoV/SARS-CoV-2 S protein was simulated through homology modeling. Authors identified that N82 of ACE2 showed closer contact with receptor-binding domain of S protein than human ACE2. PMID: 32221306
    9. SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs; determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer. PMID: 32201080
    10. Study demonstrates that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. PMID: 32155444
    11. The ACE2-B0AT1 complex exists as a dimer of heterodimers. Structural alignment of the RBD-ACE2-B0AT1 ternary complex with the S protein of SARS-CoV-2 suggests that two S protein trimers can simultaneously bind to an ACE2 homodimer. PMID: 32142651
    12. study demonstrated SARS-CoV-2 S protein entry on 293/hACE2 cells is mainly mediated through endocytosis, and PIKfyve, TPC2 and cathepsin L are critical for virus entry; found that SARS-CoV-2 S protein could trigger syncytia in 293/hACE2 cells independent of exogenous protease; there was limited cross-neutralization activity between convalescent sera from SARS and COVID-19 patients PMID: 32132184
    13. study determined a 3.5-angstrom-resolution cryo-electron microscopy structure of the 2019-nCoV S trimer in the prefusion conformation; provided biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S PMID: 32075877

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  • 亞細胞定位：
    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.
  • 蛋白家族：
    Betacoronaviruses spike protein family


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