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商品详细Cusabio/S抗体,HRP结合/100μl/CSB-PA33245YB01GMY
Cusabio/S抗体,HRP结合/100μl/CSB-PA33245YB01GMY
Cusabio/S抗体,HRP结合/100μl/CSB-PA33245YB01GMY
商品编号: CSB-PA33245YB01GMY
品牌: Cusabio
市场价: ¥5980.00
美元价: 2990.00
产地: 美国(厂家直采)
公司:
产品分类: 多肽合成
公司分类: peptide
联系Q Q: 3392242852
电话号码: 4000-520-616
电子邮箱: info@ebiomall.com
商品介绍

S Antibody, HRP conjugated

Datasheet
CodeCSB-PA33245YB01GMY
SizeUS$299
Have Questions?Leave a Message or Start an on-line Chat

Product Details

Full Product NameRabbit anti-Human Novel Coronavirus (SARS-CoV-2/ 2019-nCoV) S Polyclonal antibody
Uniprot No. P0DTC2
Target NamesS
Alternative NamesS, S1, S1-RBD, Spike glycoprotein
Raised inRabbit
Species ReactivityHuman Novel Coronavirus (SARS-CoV-2/ 2019-nCoV)
ImmunogenRecombinant Human Novel Coronavirus Spike glycoprotein (S) (319-541aa) (CSB-YP3324GMY1)
Immunogen SpeciesHuman Novel Coronavirus (SARS-CoV-2/ 2019-nCoV)
ConjugateHRP
ClonalityPolyclonal
IsotypeIgG
Purification Method>95%, Protein G purified
ConcentrationIt differs from different batches. Please contact us to confirm it.
BufferPreservative: 0.03% Proclin 300Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
FormLiquid
Tested ApplicationsELISA
Recommended Dilution
ApplicationRecommended Dilution
ELISA1:1000-1:5000
ProtocolsELISA Protocol
Troubleshooting and FAQsAntibody FAQs
StorageUpon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead TimeBasically, 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.

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Target Data

FunctionSpike glycoprotein comprises two functional subunits responsible for binding to the host cell receptor (S1 subunit) and fusion of the viral and cellular membranes (S2 subunit). For many coronavirus (CoVs), S is cleaved at the boundary between the S1 and S2 subunits, which remain non-covalently bound in the prefusion conformation. The distal S1 subunit comprises the receptor-binding domain(s) and contributes to stabilization of the prefusion state of the membrane-anchored S2 subunit that contains the fusion machinery. S is further cleaved by host proteases at the so-called S2" site located immediately upstream of the fusion peptide in all CoVs. This cleavage has been proposed to activate the protein for membrane fusion via extensive irreversible conformational changes. However, different CoVs use distinct domains within the S1 subunit to recognize a variety of attachment and entry receptors, depending on the viral species. Endemic human coronaviruses OC43 and HKU1 attach via their S domain A to 5-N-acetyl-9-O-acetyl-sialosides found on glycoproteins and glycolipids at the host cell surface to enable entry into susceptible cells. MERS-CoV S uses domain A to recognize non-acetylated sialoside attachment receptors, which likely promote subsequent binding of domain B to the entry receptor, dipeptidyl-peptidase 4. SARS-CoV and several SARS-related coronaviruses (SARSr-CoV) interact directly with angiotensin-converting enzyme 2 (ACE2) via SB to enter target cells.
Gene References into Functions
  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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Subcellular LocationVirion 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
Protein FamiliesBetacoronaviruses spike protein family
品牌介绍
CUSABIO是一家集研发,生产和销售于一体的国家高科技企业。经过12年的努力,CUSABIO已成为全球研究人员的良好合作伙伴。我们致力于为癌症,细胞生物学,免疫学,神经科学,表观遗传学等研究领域的全球客户提供60,000+种经过验证的抗体,7000 +种重组蛋白,603 +种细胞因子和数千种ELISA试剂盒。我们的所有产品都可以满足客户在各个科研领域的不同需求。