SARS-CoV-2 S1 RBD ELISA Kit
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中文名稱：新型冠狀病毒S糖蛋白RBD(SARS-CoV-2 S1 RBD) 酶聯(lián)免疫試劑盒
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貨號：CSB-EL33244
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規(guī)格：96T/48T
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價格：￥3600/￥2500
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其他：
產品詳情
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產品描述：新型冠狀病毒S糖蛋白RBD(SARS-CoV-2 S1 RBD) 酶聯(lián)免疫試劑盒（CSB-EL33244）為雙抗夾心法ELISA試劑盒，定量檢測血清、血漿、樣本樣本中的SARS-CoV-2 S1 RBD含量。SARS-CoV-2 S1 RBD即新冠病毒S1蛋白受體結合域，是病毒入侵人體細胞的關鍵結構。研究機制上，它能與人體細胞表面ACE2受體結合介導病毒感染。對其研究有助于開發(fā)阻斷結合的抗體、藥物，為新冠防治提供關鍵靶點。試劑盒檢測范圍為1.25 ng/mL-80 ng/mL，靈敏度為0.31 ng/mL。適用于科研場景中病毒入侵機制研究、疫苗免疫原性評估、中和抗體效價分析等方向，支持實驗室內對病毒感染模型、藥物干預效果或免疫動物血清中S蛋白表達水平的定量分析，為病毒學基礎研究及抗病毒藥物開發(fā)提供可靠工具。本品僅用于科研，不用于臨床診斷，產品具體參數(shù)及操作步驟詳見產品說明書。
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別名：S; 2; Spike glycoprotein; S glycoprotein; E2; Peplomer protein)
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縮寫：SARS-CoV-2 S1 RBD
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Uniprot No.：
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樣本類型：serum, plasma, swabs
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檢測范圍：1.25 ng/mL-80 ng/mL
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靈敏度：0.31 ng/mL
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反應時間：1-5h
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樣本體積：50-100ul
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檢測波長：450 nm
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研究領域：Infectious Diseases
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測定原理：quantitative
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測定方法：Sandwich
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精密度：
Intra-assay Precision (Precision within an assay): CV%<8% Three samples of known concentration were tested twenty times on one plate to assess. Inter-assay Precision (Precision between assays): CV%<10% Three samples of known concentration were tested in twenty assays to assess.
Intra-Assay Precision Inter-Assay Precision Sample 1 2 3 1 2 3 n 20 20 20 20 20 20 Mean(ng/ml) 10.79 11.06 11.36 10.85 10.99 10.02 SD 0.032 0.034 0.039 0.041 0.045 0.041 CV(%) 5.53 5.74 6.43 7.05 7.64 7.55 -
標準曲線：
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
ng/ml OD1 OD2 Average Corrected 80 2.648 2.594 2.621 2.409 40 1.973 2.032 2.003 1.791 20 1.027 1.069 1.048 0.836 10 0.559 0.537 0.548 0.336 5 0.365 0.358 0.362 0.150 2.5 0.291 0.285 0.288 0.076 1.25 0.251 0.240 0.246 0.034 0 0.213 0.211 0.212
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數(shù)據(jù)處理：
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貨期：3-5 working days
產品評價
相關產品
靶點詳情
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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.
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基因功能參考文獻：
- 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
- crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2 PMID: 32365751
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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.
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蛋白家族：Betacoronaviruses spike protein family
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