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 >  Plate>Streptavidin >SP-11

Streptavidin Coated Plates, Clear, 12×8-Well Strips, White Frame

ItemsSpecifications
MaterialPolystyrene
ColorClear
Plate Blocking2% BSA Blocking Buffer
FormulationsClear, 96-well plates, coated with 100uL of streptavidin tetramer and blocked with 200uL of 2% BSA Blocking Buffer
Detection MethodColorimetric
Capacity~5pmol biotin/well
CV% of plates/wells< 10%
TypeDetection Plate, Immunoassay, ELISA

产品展示(Product Show)

Streptavidin Plate

背景(Background)

Biotin avidin system (BAS) is a new bioreaction amplification system developed in the late 1970s. With the advent of various biotin derivatives, BAS was soon widely used in various fields of medicine. A large number of studies have confirmed in recent years that the biotin avidin system can be combined with almost kind of markers for research success. The strong binding of biotin and avidin with high affinity and multi-stage amplification effect make BAS immunolabeling and related tracer analysis more sensitive. It has become a new technique widely used in the qualitative and quantitative detection of trace antigens and antibodies, as well as in localization observation research.

应用说明(Application)

This Streptavidin Coated Plate is intended for Immunoassay and ELISA. The plate could be seperated to 12× 8-well strips and the frame is white.

存储(Storage)

The unopened plate should be stored at 2°C to 8°C,The expiry date of the plate is 24 months. Once opened, place unused plates in a resealable bag with desiccant and store at 2°C to 8°C, The shelf life is 1 month from the date of opening.

原理(Assay Principles)

Example ELISA Procedure.

Your experiment will include 5 simple steps:

a) Add your Biotinylated sample to the plate, incubation for 1 hour and wash the plate.

b) Add your sample to the plate, incubation for 1 hour and wash the plate.

c) Add a diluted Detection antibody to the plate and incubation.

d) Wash the plate and next add TMB or other colorimetric HRP substrate.

e) Stop the substrate reaction by add diluted acid, and Read OD at 450 nm, the OD Value reflects the amount of antibody bound.

Streptavidin (SA) has an extraordinarily high affinity for biotin with a dissociation constant (Kd) on the order of 10−14 mol/L, the Biotinylated molecules can bind to the SA irreversibly. Streptavidin has an isoelectric point of 5 to 6, resulting in low nonspecific interactions. The Streptavidin Coated Plates we provide are easy to use and widely available for applications.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

典型数据-Typical Data

Streptavidin TYPICAL DATA

Immobilized Biotinylated 2019-nCoV S protein RBD at 1 μg/mL (100 μL/well) on Streptavidin Coated Plates, Clear, 96-Well (Cat. No. SP-11), can bind Anti-SARS-CoV-S protein RBD with a linear range of 0.025-1.5625 ng/mL (QC tested).

Protocol

Streptavidin TYPICAL DATA

Immobilized Biotinylated Human CD19 (20-291), His,Avitag (Cat. No. CD9-H82E9) at 1 μg/mL (100 μL/well) on Streptavidin Coated Plates, Clear, 12×8-Well Strips, White Frame (Cat. No. SP-11), can bind Anti-FMC63 antibody with a linear range of 0.1-3 ng/mL (Routinely tested).

Streptavidin TYPICAL DATA

Immobilized Biotinylated Human PD-1, Fc,Avitag,His Tag (Cat. No. PD1-H82F4) at 1 μg/mL (100 μL/well) on Streptavidin Coated Plates, Clear, 12×8-Well Strips, White Frame (Cat. No. SP-11), can bind Human PD-L1, mFc Tag with a linear range of 0.4-6.25 ng/mL (Routinely tested).

Streptavidin TYPICAL DATA

Routine stability test. After placing the Streptavidin Coated Plates, Clear, 12×8-Well Strips, White Frame (Cat.No. SP-11) at 2-8°C for 24 months, binding activity between the SP-11,the Spike RBD Protein and the Anti-SARS-CoV-2 Spike RBD Antibody showed no difference from the Plate Coated Before the test.

Streptavidin TYPICAL DATA

Cat. No. SP-11, Adsorption stability test of avidin protein. After three SA plates were washed with buffer solution for three times, five times and ten times respectively, binding activity between the SA plate, the Spike RBD Protein and the Anti-SARS-CoV-2 Spike RBD Antibody showed no difference. The test shows that the SA protein has good stability on the plate.

 
评论(10)
  1. 176XXXXXXX2
  2. 1人赞
  3. 用来检测细胞中和细胞分泌的S蛋白含量,细胞培液是直接加到试剂盒提供的酶标板中,贴壁的细胞是加入细胞裂解液,4度裂解一段时间反复吹打后加入酶标板中,均可以检测出S蛋白含量
  4. 2021-10-22
  1. 135XXXXXXX7
  2. 0人赞
  3. 产品很好,冠状病毒S蛋白暴露于病毒表面并介导病毒进入宿主细胞,因此它是感染后中和抗体的主要靶标,也是药物开发和疫苗设计的重点。
  4. 2023-1-16
 
ACRO质量管理体系
 
 

前沿进展

The Novel Oncolytic Herpes Simplex Virus Type-1 (HSV-1) Vaccine Strain VC2 Constitutively Expressing GM-CSF Causes Increased Intratumoral T Cell Infiltration and Inhibition of Tumor Metastasis in the 4T1/Balb/c Mouse Model of Stage Four Breast Cancer
Nabi, Chouljenko, Musarrat et al
J Med Virol (2025) 97 (2), e70220
Abstract: Oncolytic virotherapy (OVT) aims to disrupt the tumor microenvironment and provide a unique therapeutic approach against solid tumors. Herpes simplex virus type-1 (HSV-1) has shown strong promise for treating various solid tumors and has been approved to treat melanoma and glioma in human patients. Previously, we reported the generation of an engineered HSV-1 vaccine strain VC2, which has shown exceptional promise as an oncolytic and immunotherapeutic virus. In the present work, we engineered VC2 to constitutively express the murine granulocyte-macrophage colony-stimulating factor (GM-CSF) gene inserted in place of HSV-1 Glycoprotein C (gC). We tested the efficacy of VC2-GMCSF for its ability to generate antitumor response in the 4T1 stage four metastatic breast cancer mouse model. GM-CSF expression enhanced VC2 viral replication and infectious virus production. Tumors formed after 7 days of engraftment in the mammary fat pad of Balb/CJ mice were treated by injecting ~5 × 104 plaque forming units (PFU) of VC2/VC2-GMCSF once. Intratumor treatment did not appreciably reduce average primary tumor sizes. However, metastatic foci were significantly reduced in mice lungs treated with VC2-GMCSF compared to VC2 or mock treatment. VC2-GMCSF intratumoral treatment induced a stronger intratumor T cell infiltration but not an increased cytotoxic activity. A significant T cell infiltration was observed in the metastatic areas in VC2-GMCSF treated animals, which was associated with reduced pro-tumor marker PDL1 and VEGF gene expression. These results show that constitutive expression of GM-CSF enhanced the overall efficacy of VC2 for OVT. VC2-GMCSF holds promise as oncolytic and immunotherapeutic virotherapy for breast and other cancers.© 2025 Wiley Periodicals LLC.
Enhancement of HSV-1 cell-free virion release by the envelope protein gC
Frost, Salnikov, Rice
Virology (2024) 596, 110120
Abstract: Glycoprotein C (gC), one of ∼12 HSV-1 envelope glycoproteins, carries out several important functions during infection, including the enhancement of virion attachment by binding to host cell heparan sulfate proteoglycans (HSPG). Here we report that gC can also enhance the release of cell-free progeny virions at the end of the infectious cycle. This activity was observed in multiple cellular contexts including Vero cells and immortalized human keratinocytes. In the absence of gC, progeny virions bound more tightly to infected cells, suggesting that gC promotes the detachment of virions from the infected cell surface. Given this finding, we analyzed the biochemical interactions that tether progeny virions to cells and report evidence for two distinct modes of binding. One is consistent with a direct interaction between gC and HSPG, whereas the other is gC-independent and likely does not involve HSPG. Together, our results i) identify a novel function for a long-studied HSV-1 glycoprotein, and ii) demonstrate that the extracellular release of HSV-1 virions is a dynamic process involving multiple viral and host components.Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.
Decrease in Heparan Sulphate Binding in Tropism-Retargeted Oncolytic Herpes Simplex Virus (ReHV) Delays Blood Clearance and Improves Systemic Anticancer Efficacy
Vannini, Parenti, Forghieri et al
Cancers (Basel) (2024) 16 (6)
Abstract: The role of the interaction with cell-surface glycosaminoglycans (GAGs) during in vivo HSV infection is currently unknown. The rationale of the current investigation was to improve the anticancer efficacy of systemically administered retargeted oHSVs (ReHVs) by decreasing their binding to GAGs, including those of endothelial cells, blood cells, and off-tumor tissues. As a proof-of-principle approach, we deleted seven amino acids critical for interacting with GAGs from the glycoprotein C (gC) of R-337 ReHV. The modification in the resulting R-399 recombinant prolonged the half-life in the blood of systemically administered R-399 and enhanced its biodistribution to tumor-positive lungs and to the tumor-negative liver. Ultimately, it greatly increased the R-399 efficacy against metastatic-like lung tumors upon IV administration but not against subcutaneous tumors upon IT administration. These results provide evidence that the increased efficacy seen upon R-399 systemic administration correlated with the slower clearance from the circulation. To our knowledge, this is the first in vivo evidence that the partial impairment of the gC interaction with GAGs resulted in a prolonged half-life of circulating ReHV, an increase in the amount of ReHV taken up by tissues and tumors, and, ultimately, an enhanced anticancer efficacy of systemically administered ReHV.
Glycoprotein C of Herpes Simplex Virus 1 Shields Glycoprotein B from Antibody Neutralization
Komala Sari, Gianopulos, Nicola
J Virol (2020) 94 (5)
Abstract: Viruses have evolved strategies to avoid neutralization by the host antibody response. Herpes simplex virus (HSV) glycoprotein C (gC) functions in viral entry and binds to complement component C3b, inhibiting complement-mediated immunity. We investigated whether gC protects HSV from antibody neutralization. HSV-1 that lacks gC was more sensitive to complement-independent neutralization by a panel of gB monoclonal antibodies than a wild-type gC rescuant virus. The presence of gC decreased neutralization by 2- to 16-fold. The gB in the native envelope of HSV-1 had reduced reactivity with antibodies in comparison to gB from the gC-null virus, suggesting that gC hampers the recognition of gB epitopes in the viral particle. The protein composition of the gC-null virus, including the surface glycoproteins essential for entry, was equivalent to that of the wild type, suggesting that gC is directly responsible for the reduced antibody recognition and neutralization. The neutralizing activity of antibodies to gD and gH antibodies was also increased in HSV lacking gC. Together, the data suggest that HSV-1 gC protects the viral envelope glycoproteins essential for entry, including gB, by shielding them from neutralization as a potential mechanism of immune evasion.IMPORTANCE HSV-1 causes lifelong infection in the human population and can be fatal in neonatal and immunocompromised individuals. There is no vaccine or cure, in part due to the ability of HSV to escape the host immune response by various mechanisms. The HSV particle contains at least 15 envelope proteins, four of which are required for entry and replication. This work suggests a novel role for gC in shielding the HSV entry glycoproteins. gC may function to help HSV escape neutralization by antibodies.Copyright © 2020 American Society for Microbiology.
Showing 1-4 of 143 papers.
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