Log In Sign up
The largest database of trusted experimental protocols

8k instrument

Manufactured by Cytiva
Visit Supplier

The 8K instrument is a laboratory equipment designed for high-performance analytical applications. It features advanced technological capabilities to assist researchers and scientists in their work.

Automatically generated - may contain errors

Lab products found in correlation

Insight evaluation software, by Cytiva (3 mentions) Nta chip, by Cytiva (2 mentions) Hace2, by Sino Biological (2 mentions) Cm5 chip, by Cytiva (2 mentions) 8k software, by Cytiva (1 mentions) αiibβ3, by R&D Systems (1 mentions) Cm5 chip, by GE Healthcare (1 mentions) Human fab capture kit, by GE Healthcare (1 mentions)

10 protocols using 8k instrument

1

Neutralization Mechanism of SARS-CoV-2 Monoclonal Antibody

Check if the same lab product or an alternative is used in the 5 most similar protocols
To determine the neutralization mechanism of MAb 22.9-1, binding competition experiments were conducted by SPR assay with the Biacore 8K instrument and NTA chip (Cytiva). Purified hACE2 (Sino Biological) was immobilized at a concentration of 10 μg/mL. The following samples were injected: (i) 40 μg/mL O-RBD, (ii) complex of 40 μg/mL O-RBD and 0.15 mg/mL MAb 22.9-1, (iii) complex of 40 μg/mL O-RBD and 0.15 mg/mL MAb 20.8-8. The data were analyzed with the Biacore Insight Evaluation software. The curves were plotted using GraphPad Prism software.
Hua R.H., Zhang S.J., Niu B., Ge J.Y., Lan T, & Bu Z.G. (2023). A Novel Conserved Linear Neutralizing Epitope on the Receptor-Binding Domain of the SARS-CoV-2 Spike Protein. Microbiology Spectrum, 11(4), e01190-23.
+ Open protocol
+ Expand
2

Neutralization Mechanism of SARS-CoV-2 Monoclonal Antibody

Check if the same lab product or an alternative is used in the 5 most similar protocols
To determine the neutralization mechanism of MAb 22.9-1, binding competition experiments were conducted by SPR assay with the Biacore 8K instrument and NTA chip (Cytiva). Purified hACE2 (Sino Biological) was immobilized at a concentration of 10 μg/mL. The following samples were injected: (i) 40 μg/mL O-RBD, (ii) complex of 40 μg/mL O-RBD and 0.15 mg/mL MAb 22.9-1, (iii) complex of 40 μg/mL O-RBD and 0.15 mg/mL MAb 20.8-8. The data were analyzed with the Biacore Insight Evaluation software. The curves were plotted using GraphPad Prism software.
Hua R.H., Zhang S.J., Niu B., Ge J.Y., Lan T, & Bu Z.G. (2023). A Novel Conserved Linear Neutralizing Epitope on the Receptor-Binding Domain of the SARS-CoV-2 Spike Protein. Microbiology Spectrum, 11(4), e01190-23.
+ Open protocol
+ Expand
3

SARS-CoV-2 RBD Binding Kinetics

Check if the same lab product or an alternative is used in the 5 most similar protocols
SPR experiments were performed using a protein A capture chip on a Biacore 8k instrument. The running buffer was HBS-EP (3 M sodium chloride, 200 mM HEPES, 60 mM EDTA, 1.0% Tween 20) with 1 mg/ml bovine serum albumin (BSA). The SARS-CoV-2 RBD was used as an analyte at concentrations of 100 nM, 10 nM, and 1 nM. The experiment had an association phase for 120 sec and the dissociation phase for 600 sec. The data were fit by a 1:1 Langmuir model.
Walker S.N., Chokkalingam N., Reuschel E.L., Purwar M., Xu Z., Gary E.N., Kim K.Y., Helble M., Schultheis K., Walters J., Ramos S., Muthumani K., Smith T.R., Broderick K.E., Tebas P., Patel A., Weiner D.B, & Kulp D.W. (2020). SARS-CoV-2 Assays To Detect Functional Antibody Responses That Block ACE2 Recognition in Vaccinated Animals and Infected Patients. Journal of Clinical Microbiology, 58(11), e01533-20.
+ Open protocol
+ Expand
4

Biacore Analysis of CD98hc Binding Affinities

Check if the same lab product or an alternative is used in the 5 most similar protocols
Affinities of ATVs for CD98hc were determined by surface plasmon resonance using a Biacore™ 8 K instrument. ATVs were immobilized on a Cytiva Series S CM5 sensor chip (Cytiva, 29149603) using a Cytiva Human Fab capture kit (Cytiva, 28958325) at 10 µg/mL using a flow rate of 10 µL/min for 60 s. 3-fold serial dilutions of recombinant CD98hc at concentrations of 24.5, 74.0, 222, 667, 2000, and 6000 nM were injected at a flow rate of 30 μL/min for 300 s followed by a 600-s dissociation in a 1X HBS-EP+ running buffer (Cytiva, BR100826). Data analysis was conducted using Biacore Insight Evaluation software (version 2.0.15.12933). For affinities tighter than 600 nM a kinetic analysis was performed with a 1:1 Langmuir kinetic binding model for evaluation of kon, koff and KD. Affinities weaker than 600 nM were measured 3 independent times and averaged using a steady state model analysis to determine KD values.
Chew K.S., Wells R.C., Moshkforoush A., Chan D., Lechtenberg K.J., Tran H.L., Chow J., Kim D.J., Robles-Colmenares Y., Srivastava D.B., Tong R.K., Tong M., Xa K., Yang A., Zhou Y., Akkapeddi P., Annamalai L., Bajc K., Blanchette M., Cherf G.M., Earr T.K., Gill A., Huynh D., Joy D., Knight K.N., Lac D., Leung A.W., Lexa K.W., Liau N.P., Becerra I., Malfavon M., McInnes J., Nguyen H.N., Lozano E.I., Pizzo M.E., Roche E., Sacayon P., Calvert M.E., Daneman R., Dennis M.S., Duque J., Gadkar K., Lewcock J.W., Mahon C.S., Meisner R., Solanoy H., Thorne R.G., Watts R.J., Zuchero Y.J, & Kariolis M.S. (2023). CD98hc is a target for brain delivery of biotherapeutics. Nature Communications, 14, 5053.
+ Open protocol
+ Expand
5

Measuring SARS-CoV-2 RBD-ACE2 Interaction

Check if the same lab product or an alternative is used in the 5 most similar protocols
Surface plasmon resonance experiments were conducted on a Biacore 8K instrument. The running and dilution buffers were HBS-EP, 1 mg/ml BSA, and 0.05% Tween. The biotin CAPture reagent was injected over the Series S CAP Sensor chip (28920234; Cytiva Life Sciences) at 2 μl/min for 300 s. SARS-CoV-2 receptor binding domain was biotinylated using the Lightning-Link type-A biotinylation kit (370-0005; Expedeon/Abcam) and injected over the chip for 180 s at 10 μl/min, followed by injection of the sample (ACE2-IgHu) at 8 concentrations of 1,500 nM to 0.7 nM. The association was for 120 s at a flow rate of 30 μl/min, followed by a short dissociation time of 15 s. ACE2-IgHu was injected at a constant 100-nM concentration in each flow cell for 120 s, followed by a 60-s dissociation at a flow rate of 30 μl/min. The difference in response units before injection and after dissociation of the sample application and the constant receptor was calculated for each curve. The regeneration solution was made using 3-parts 8 M guanidine hydrochloride and 1-part 1 M sodium hydroxide.
Walker S.N., Chokkalingam N., Reuschel E.L., Purwar M., Xu Z., Gary E.N., Kim K.Y., Helble M., Schultheis K., Walters J., Ramos S., Muthumani K., Smith T.R., Broderick K.E., Tebas P., Patel A., Weiner D.B, & Kulp D.W. (2020). SARS-CoV-2 Assays To Detect Functional Antibody Responses That Block ACE2 Recognition in Vaccinated Animals and Infected Patients. Journal of Clinical Microbiology, 58(11), e01533-20.
+ Open protocol
+ Expand
6

Quantifying PDI Binding to αIIbβ3 via SPR

Check if the same lab product or an alternative is used in the 5 most similar protocols
Direct binding of PDI, or the fragments or mutants of PDI, to αIIbβ3 was measured by surface plasmon resonance (SPR) with a Biacore 8K instrument. 8 μg/ml of αIIbβ3 (R and D Systems) in 10 mM sodium acetate buffer, pH 4.5 was immobilized on the surface of a Biacore CM5 chip. Purified recombinant PDI, fragments or mutants of PDI at different concentrations were infused over the chip at a flow rate of 10 μl/min for 2min with a running buffer of 10 mM HEPES, 150 mM NaCl, 1 mM MnCl2, 0.05% Tween 20. The dissociation constant was analyzed with Biacore 8K software.
Methods for the aggregation and secretion studies of human and mouse platelets, labeling of αIIbβ3 on platelets with 3-(N-Maleimidylpropionyl)biocytin (MPB), intravital microscopy of laser-induced thrombosis of the cremaster muscle arterioles, and the statistics are in the supplemental methods.
Wang L., Zhou J., Wang L., Wang C.C, & Essex D.W. (2019). The b′ domain of protein disulfide isomerase cooperates with the a and a′ domains to functionally interact with platelets. Journal of thrombosis and haemostasis : JTH, 17(2), 371-382.
+ Open protocol
+ Expand
7

Kinetic Analysis of D-2-HGDH Binding

Check if the same lab product or an alternative is used in the 5 most similar protocols
The SPR analysis was performed using a Biacore 8 K instrument at 25 °C. Prior to analysis, the D-2-HGDH protein was exchanged to the running buffer containing 25 mM HEPES (pH 7.5) and 200 mM NaCl via gel filtration. The protein was covalently immobilized onto the sensor CM5 chip (GE Healthcare) in 10 mM sodium acetate (pH 5.5) following standard amine-coupling procedure. The analytes were used to flow over the chip surface with the response units measured. The binding kinetics was analyzed with the Biacore Insight Evaluation Software using the 1:1 binding model. The binding of D-2-HG, D-MAL, or D-LAC with D-2-HGDH could be measured reliably, but that of L-2-HG and 2-OG could not.
Yang J., Zhu H., Zhang T, & Ding J. (2021). Structure, substrate specificity, and catalytic mechanism of human D-2-HGDH and insights into pathogenicity of disease-associated mutations. Cell Discovery, 7, 3.
+ Open protocol
+ Expand
8

Quantifying TREM2 Binding Affinities

Check if the same lab product or an alternative is used in the 5 most similar protocols
Human TREM2, mouse TREM2, and mouse TREM1 ECD binding affinities to 4D9 were determined by SPR using a Biacore 8K instrument. Biacore Series S CM5 sensor chip was immobilized with a mixture of two monoclonal mouse anti‐Fab antibodies (Human Fab Capture Kit from GE Healthcare). Serial twofold dilutions of recombinant mouse Trem2 were injected at a flow rate of 30 μl/min for 300 s followed by 1,200‐s dissociation in HBS‐EP+ running buffer (GE, #BR100669). Binding response was corrected by subtracting the RU from a blank flow cell. A 1:1 Langmuir model of simultaneous fitting of kon and koff was used for kinetics analysis.
Schlepckow K., Monroe K.M., Kleinberger G., Cantuti‐Castelvetri L., Parhizkar S., Xia D., Willem M., Werner G., Pettkus N., Brunner B., Sülzen A., Nuscher B., Hampel H., Xiang X., Feederle R., Tahirovic S., Park J.I., Prorok R., Mahon C., Liang C., Shi J., Kim D.J., Sabelström H., Huang F., Di Paolo G., Simons M., Lewcock J.W, & Haass C. (2020). Enhancing protective microglial activities with a dual function TREM2 antibody to the stalk region. EMBO Molecular Medicine, 12(4), e11227.
+ Open protocol
+ Expand
9

Affinity Kinetics of HER2 Interactions

Check if the same lab product or an alternative is used in the 5 most similar protocols
The affinity of the interactions between ZHER2:342-Cys or Z-M ADCN and extracellular domain (ECD) of HER2 were analyzed by a Biacore 8 K instrument. HER2ECD was immobilized on a CM5 chip by amine coupling firstly and the immobilization level was about 1000 RU for experiments. Then the affinity constants were detected by injecting a series dilution concentration as required.
Xia X., Yang X., Huang W., Xia X, & Yan D. (2021). Self-Assembled Nanomicelles of Affibody-Drug Conjugate with Excellent Therapeutic Property to Cure Ovary and Breast Cancers. Nano-Micro Letters, 14, 33.
+ Open protocol
+ Expand
10

Measuring Binding Kinetics via Biacore 8K+

Check if the same lab product or an alternative is used in the 5 most similar protocols
The binding kinetics were measured using a Biacore 8K+ instrument. The antigens and knob domain constructs were immobilised on a Biacore CM5 chip via amine coupling; serial dilutions of their respective binding partners were prepared in HBS-EP+ buffer (10 mM HEPES pH 7.4, 150 mM NaCl, 3 mM EDTA, 0.005% v/v Surfactant P20). For each injection, a flow rate of 40 µL/min was used. Association was recorded for 300 s (K8 and K57) or 100 s (aIL2_1); dissociation was recorded for 6000 s (K8 and K57) or 1000 s (aIL2_1). The surface was regenerated by two sequential 30 s pulses of 2 M MgCl2. To determine the binding kinetics, the data obtained after subtraction of reference measurements were fitted to 1:1 (K8 and K57) or a two-state (aIL2_1) binding model using Biacore evaluation software. In the latter case, we report the fastest association rate and the slowest dissociation rate constants only.
Kuravsky M., Gibbons G.F., Joyce C., Scott-Tucker A., Macpherson A, & Lawson A.D. (2024). Modular design of bi- and multi-specific knob domain fusions. Frontiers in Immunology, 15, 1384467.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!