商品详细Cusabio/SARS-CoV-2 S1 RBD ELISA试剂盒/96T、5×96T、10×96T/CSB-EL33244

Cusabio/SARS-CoV-2 S1 RBD ELISA试剂盒/96T、5×96T、10×96T/CSB-EL33244

商品编号： CSB-EL33244

品牌： Cusabio

市场价： ¥0.00

美元价： 0.00

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

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商品介绍

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ELISA Kit
SARS-CoV-2 S1 RBD ELISA Kit

SARS-CoV-2 S1 RBD ELISA Kit

^Instructions

Code	CSB-EL33244
Size	96T,5×96T,10×96T
Trial Size
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Target Data

Product Details

Target Name

Novel Coronavirus Spike Glycoprotein RBD (SARS-CoV-2 S1 RBD)

Alternative Names

2019 Novel Coronavirus; Coronavirus; CoV; COVID-19 virus; HCoV-2; Human Coronavirus 2019; SARS2; SARS-CoV-2; Severe acute respiratory syndrome coronavirus 2; Spike glycoprotein RBD; Spike Protein RBD

Abbreviation

SARS-CoV-2 S1 RBD

Uniprot No.

P0DTC2

Sample Types

serum, plasma, swabs

Detection Range

1.25 ng/mL-80 ng/mL

Sensitivity

0.31 ng/mL

Assay Time

1-5h

Sample Volume

50-100ul

Detection Wavelength

450 nm

Research Area

Infectious Diseases

Assay Principle

quantitative

Measurement

Sandwich

Precision

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

Typical Data

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

Troubleshooting and FAQs

ELISA kit FAQs

Storage

Store at 2-8°C. Please refer to protocol.

Lead Time

3-5 working days

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Target Data

Function	Spike 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	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 Show More Hide All
Subcellular Location	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
Protein Families	Betacoronaviruses spike protein family

品牌介绍

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