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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.

 
 
ACRO质量管理体系
 
 

前沿进展

ACE2 Deficiency Protects Against Heme Protein-Induced Acute Kidney Injury
Croatt, Singh, Grande et al
Am J Physiol Renal Physiol (2025)
Abstract: Angiotensin-converting enzyme 2 (ACE2) exerts countervailing effects on the renin-angiotensin aldosterone system. ACE2 also engages the spike protein of SARS-CoV-2. ACE2 protein has been shown recently to avidly bind heme. We examined the pathobiologic relevance of this heme-binding property of ACE2 by employing the glycerol-induced model of heme protein mediated AKI (HP-AKI) which is characterized by increased kidney heme content. We studied the response of ACE2-wildtype (ACE2+/y) and ACE2-deficient (ACE2-/y) mice to HP-AKI and quantitated kidney and cellular content of heme under relevant conditions. ACE2-deficient mice, compared with ACE2-wildtype mice, were significantly protected against HP-AKI as reflected by filtration markers, less histologic injury, and less expression of apoptosis and ferroptosis markers. ACE2-deficient mice also evinced lesser kidney heme content and a blunted induction of HO-1. HEK293 ACE2-overexpressing cells, compared with HEK293-native, when exposed to heme, retained higher amounts of heme. In HP-AKI, ACE2 expression and activity were reduced, and myoglobin and heme, administered independently, reduced ACE2 expression in the otherwise intact mouse kidney. Finally, with more severe HP-AKI, the protective effect of ACE2 deficiency was attenuated. We conclude that ACE2 deficiency confers protection against HP-AKI. We suggest that this reflects the recently recognized binding of heme to ACE2, such binding serving to facilitate renal entry of heme, a known nephrotoxin. These findings uncover a novel pathway of heme-dependent acute kidney injury. This is the first demonstration of the biologic relevance of chemical binding of heme by ACE2. Finally, we identify heme proteins and heme as novel determinants of ACE2 expression.
Modulation of RAAS receptors and miRNAs in COVID-19: implications for disease severity, immune response, and potential therapeutic targets
Barreto Fernandes, Pilotto, Cezar et al
BMC Infect Dis (2025) 25 (1), 399
Abstract: The SARS-CoV-2 spike protein interacts with ACE2, a key receptor within the renin-angiotensin-aldosterone system (RAAS), which plays a critical role in maintaining vascular homeostasis, regulating blood pressure, and modulating inflammation. An observational study analyzed the gene expression profiles of RAAS receptors and associated miRNAs in 88 hospitalized COVID-19 patients and 20 healthy controls, comparing the acute and post-acute phases to assess their impact on disease severity and recovery. Our findings revealed an association between reduced MAS1 expression in both advanced age (P = 0.03) and the need for oxygen supplementation (P = 0.04). Additionally, reduced ACE expression was associated with worse mortality outcomes (P = 0.01). Notably, ACE2 and TMPRSS2 expression was significantly decreased (P < 0.0001) in individuals requiring oxygen supplementation and in those with diabetes mellitus during both the acute and post-COVID-19 phases, further highlighting the impact of these conditions on RAAS. The miRNA analysis revealed significant downregulation of miR-200c (P = 0.005), miR-let-7 (P = 0.01), and miR-122 (P = 0.03) in acute-phase COVID-19 patients. This dysregulation contributes to the inflammatory response and highlights the interaction between viral entry and immune regulation. These results underscore the significance of the ACE2/Ang-(1-7)/MAS1 axis in inflammation regulation and suggest that targeting this pathway may have therapeutic potential. Our study provides valuable insights into the molecular mechanisms of COVID-19 pathogenesis and identifies the modulation of RAAS receptors and miRNAs as promising biomarkers for disease severity and potential therapeutic interventions. CLINICAL TRIAL: Not applicable.© 2025. The Author(s).
Diagnostic Value of Let-7a-5p in Essential Hypertension
Wang, Zhu, Cheng et al
J Clin Hypertens (Greenwich) (2025) 27 (3), e70033
Abstract: This study aimed to investigate the role of let-7a-5p in the pathogenesis of essential hypertension (EH) and its correlation with the renin-angiotensin-aldosterone system (RAAS) biomarkers. Ninety-eight EH patients and 24 healthy controls (HC) enrolled in the study were assayed for the relative expression of let-7a-5p in plasma by quantitative real-time polymerase chain reaction (Q-PCR), and biomarkers of the RAAS system, including angiotensin-converting enzyme 2 (ACE2), Ang (1-7), MAS1, angiotensin-converting enzyme (ACE), angiotensin II (Ang II), and angiotensin II type 1 receptor (AT1R), were determined by enzyme-linked immunosorbent assay (ELISA) The expression levels of the biomarkers of RAAS system were determined. The results showed that the expression levels of let-7a-5p in the plasma of EH patients were remarkably higher than those of HC. The prediction model of combined let-7a-5p showed high accuracy by constructing a subject operating characteristic (ROC) curve with an area under the curve (AUC) of 0.885, and the reliability of the model was further verified by the Hosmer-Lemeshow (H-L) goodness-of-fit test, the Model Calibration Curve, and the Decision Curve Analysis. Spearman correlation analysis revealed that the expression of let-7a-5p was positively correlated with ACE (r = 0.352, p < 0.001), and mediation analysis indicated that ACE partially mediated between let-7a-5p and the development of hypertension. The present study concludes with the potential of let-7a-5p as a companion diagnostic biomarker for EH. It suggests that there may be a complex regulatory mechanism between it and specific RAAS biomarkers, which provides a new perspective on the pathogenesis and diagnosis of EH.© 2025 The Author(s). The Journal of Clinical Hypertension published by Wiley Periodicals LLC.
Interaction of Asparagusic Acid, Asparaptines and Related Dithiolane Derivatives With Angiotensin-Converting Enzyme-2 (ACE-2): A Molecular Docking Study
Vergoten, Bailly
J Biochem Mol Toxicol (2025) 39 (4), e70236
Abstract: A variety of sulfur-containing small molecules can be found in the spears of asparagus (Asparagus Officinalis L.) including compounds derived from asparagusic acid such as the amino acid derivatives asparaptines A, B, and C. The previous characterization of asparaptine A as an inhibitor of angiotensin-converting enzyme (ACE) prompted us to compare the binding of the three asparaptines to ACE2 using molecular modeling. The lysine conjugate asparaptine B was found to bind better to the enzyme than the arginine (asparaptine A) and histidine (asparaptine C) conjugates. The stability of ACE2-asparaptine B complexes was only a little inferior to that observed with the reference ACE2 inhibitor MLN-4760. On this basis, 20 additional compounds bearing a thiol group or a dithiolane motif were evaluated as potential binders to ACE2 using the same docking methodology. Three compounds emerged as robust ACE2 binders: the natural products isovalthine and N-acetyl-felinine, and the drug candidate CMX-2043. The empirical energy of interaction (ΔE) of N-acetyl-felinine with ACE2 was comparable to that measured with asparaptine B, and a little higher with the thiol metabolite isovalthine. Remarkably, CMX-2043 revealed a high capacity to form stable complexes with ACE2, superior to that of the reference MLN-4760. Both the l-Glu-l-Ala dipeptide motif and the α-lipoic acid moiety of CMX-2043 are implicated in the protein interaction. Our observations pave the way to the design of novel ligands of ACE2 equipped with a dithiolane motif.© 2025 The Author(s). Journal of Biochemical and Molecular Toxicology published by Wiley Periodicals LLC.
Showing 1-4 of 14417 papers.
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