Recombinant Severe acute respiratory syndrome coronavirus 2 Spike glycoprotein (S), partial (Active)

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文獻引用 (11)

貨號：

CSB-MP3324GMY
說明書：

MSDS Datasheet
規格：

￥1536
圖片：
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Activity
Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-S at 2 μg/ml can bind human ACE2 (CSB-MP866317HU), the EC₅₀ of SARS-CoV-2-S protein is 56.64 - 103.6 ng/ml.

Activity
Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-S at 2 μg/ml can bind SARS-CoV-2-S Antibody (CSB-RA33245A1GMY), the EC₅₀ of SARS-CoV-2-S protein is 36.79-48.87 ng/ml Biological Activity Assay
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靶點詳情

產品詳情

純度：

Greater than 90% as determined by SDS-PAGE.
內毒素：

Less than 1.0 EU/ug as determined by LAL method.
生物活性：

①Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-S at 2 μg/ml can bind human ACE2 (CSB-MP866317HU), the EC₅₀ of SARS-CoV-2-S protein is 56.64 - 103.6 ng/ml.②Measured by its binding ability in a functional ELISA. Immobilized SARS-CoV-2-S at 2 μg/ml can bind SARS-CoV-2-S Antibody (CSB-RA33245A1GMY), the EC₅₀ of SARS-CoV-2-S protein is 36.79-48.87 ng/ml
基因名：

S
Uniprot No.：

P0DTC2
別名：

S; 2; Spike glycoprotein; S glycoprotein; E2; Peplomer protein)
種屬：

Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
蛋白長度：

Partial
來源：

Mammalian cell
分子量：

79.6 kDa
表達區域：

16-685aa
氨基酸序列

VNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRAR
蛋白標簽：

N-terminal 10xHis-tagged and C-terminal Flag-tagged
產品提供形式：

Lyophilized powder Warning: in_array() expects parameter 2 to be array, null given in /www/web/cusabio_cn/public_html/caches/caches_template/default/content/show_product_protein.php on line 662
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
緩沖液：

Lyophilized from a 0.2 μm sterile filtered 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0
復溶：

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
儲存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質期：

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期：

3-7 business days
注意事項：

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA：

Please contact us to get it.

引用文獻

Especificidad de los anticuerpos IgG de alpacas contra antígenos de la proteína S de las variantes alfa, beta y delta de SARS-CoV-2 y coronavirus de alpaca MSR HUAMáN,Universidad Nacional Mayor de San Marcos,2024
Label-free electrochemical aptasensor for rapid detection of SARS-CoV-2 spike glycoprotein based on the composite of Cu(OH)2 nanorods arrays as a high-performance surface substrate Z Rahmati,Bioelectrochemistry,2023
Assessing antibody and nanobody nativeness for hit selection and humanization with AbNatiV S Guo,/,2024
Investigating the Interactions of Fatty Acids, Amyloid Beta & SARS-CoV-2 Spike Protein Fragment L Toma - 2023 - uwspace.uwaterloo.ca,/,2023
A magneto-optical biochip for rapid assay based on the Cotton–Mouton effect of γ-Fe2O3@ Au core/shell nanoparticles KL Chen,Journal of nanobiotechnology,2021
Ultramicronized Palmitoylethanolamide Inhibits NLRP3 Inflammasome Expression and Pro-Inflammatory Response Activated by SARS-CoV-2 Spike Protein in Cultured Murine Alveolar Macrophages Alessandro Del Re,Metabolites,2021
An electrochemical immunosensor using SARS-CoV-2 spike protein-nickel hydroxide nanoparticles bio-conjugate modified SPCE for ultrasensitive detection of SARS‐CoV‐2 antibodies Zeinab Rahmati,Microchemical Journal,2021
Screening of potent neutralizing antibodies against SARS-CoV-2 using convalescent patients-derived phage-display libraries Y Pan,Cell discovery,2021
Seropositive reaction rates of 9 B cell epitopes of the SARS-CoV-2 spike protein and the relationship between the epitopes and neutralizing antibody L Zhu,Intervirology,2021
SARS-CoV-2 uses major endothelial integrin αvβ3 to cause vascular dysregulation in-vitro during COVID-19 D Nader,PLOS ONE,2021
Electrochemical immunosensor with Cu₂O nanocube coating for detection of SARS-CoV-2 spike protein Mahmoud Roushani,Microchimica Acta,2021

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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