Olink Target 96 Cardiovascular III Panel

The Olink Target 96 Cardiovascular III Panel enables the simultaneous analysis of 92 protein biomarkers with only 1 μL of biological sample. These protein biomarkers were selected to take into account both the dynamic range in the sample and the degree of closeness to cardiovascular disease. The Cardiovascular Disease-III panel contains known human cardiovascular and inflammatory markers, as well as candidate proteins with the same potential as cardiovascular disease markers. Each protein is carefully selected by experts in the field. Each low-abundance protein analyte of interest has been evaluated based on sample material, specificity, precision, sensitivity, dynamic range, matrix effects, and interferences.

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human Olink Proteomics Panel
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What is the Olink Target 96 Cardiovascular III Panel

Customized panel for human

The Olink Target 96 Cardiovascular III Panel is designed to accurately quantify proteins, with comprehensive biomarker details accessible on our company website. Employing advanced Biomarker technology, the panel analyzes 92 proteins through a three-step process: incubation, extension/amplification, and detection. During the incubation phase, DNA-labeled antibody pairs are added to the sample and incubated overnight to bind specific target proteins. The next day, extension and amplification steps produce unique DNA reporter sequences for each protein, followed by preamplification using standard PCR. Detection is performed using high-throughput real-time qPCR on the Olink Signature Q100 System to measure the DNA reporter sequences. To ensure unbiased analysis, samples were randomly allocated across plates. Data quality control and normalization were conducted using internal extension and interplate controls, addressing both intra- and inter-batch variability. Protein levels are expressed as normalized protein expression (NPX) values, calculated on a log2 scale for accurate and reliable interpretation.

 Features of the pane

  • Species: Primarily tested for human proteins; cross-reactivity with other species is not confirmed.  
  • Proteins: Measures 92 protein biomarkers simultaneously in a single run.
  • Sample: Just 1µL of plasma, serum, or comparable biofluids is required.
  • Readout: Delivers data in normalized protein expression (NPX) units, ensuring reliable quantification of protein abundance.
  • Platform: Optimized for use with the Olink Signature Q100 platform for streamlined performance.

List of 92 human derived biomarkers

Protein category

The Olink Target 96 Oncology III Panel includes 92 proteins categorized into nine main groups:

the Cytokines & Growth Factors (7), Receptors (18), the enzymes (17), Extracellular Matrix Proteins (6), Immune-related Proteins (10), Transport & Binding Proteins (6), Enzyme Inhibitors (5), Signaling Molecules (9), and other functional proteins (14). These protein biomarkers were selected by taking into account both their dynamic range in the sample and their closeness to cardiovascular disease. The Cardiovascular Disease-III panel contains known human cardiovascular and inflammatory markers as well as candidate proteins with great potential as cardiovascular disease markers. Each protein was carefully selected by experts in the field. Each of the low-abundance protein analytes of interest has been evaluated in terms of sample material, specificity, precision, sensitivity, dynamic range, matrix effects, and interference.

Table. List of Olink Target 96 Cardiovascular III Panel.

Protein Category UniProt ID Gene Protein Name
Cytokines & Growth Factors Q99988 GDF15 Growth/differentiation factor 15
P13500 CCL2 C-C motif chemokine 2
Q9H2A7 CXCL16 C-X-C motif chemokine 16
O15467 CCL16 C-C motif chemokine 16
Q16663 CCL15 C-C motif chemokine 15
Q9Y275 TNFSF13B Tumor necrosis factor ligand superfamily member 13B
P04085 PDGFA Platelet-derived growth factor subunit A
Receptors P01130 LDLR Low-density lipoprotein receptor
Q96F46 IL17RA Interleukin-17 receptor A
P20333 TNFRSF1B Tumor necrosis factor receptor superfamily member 1B
P54760 EPHB4 Ephrin type-B receptor 4
P01589 IL2RA Interleukin-2 receptor subunit alpha
O14798 TNFRSF10C Tumor necrosis factor receptor superfamily member 10C
P08887 IL6R Interleukin-6 receptor subunit alpha
P30530 AXL Tyrosine-protein kinase receptor UFO
P14778 IL1R1 Interleukin-1 receptor type 1
O00300 TNFRSF11B Tumor necrosis factor receptor superfamily member 11B
P36941 LTBR Tumor necrosis factor receptor superfamily member 3
Q92956 TNFRSF14 Tumor necrosis factor receptor superfamily member 14
P25445 FAS Tumor necrosis factor receptor superfamily member 6
P19438 TNFRSF1A Tumor necrosis factor receptor superfamily member 1A
Q01638 IL1RL1 Interleukin-1 receptor-like 1
P00533 EGFR Epidermal growth factor receptor
Q03405 PLAUR Urokinase plasminogen activator surface receptor
P78324 SIRPA Tyrosine-protein phosphatase non-receptor type substrate 1
Enzymes P14780 MMP9 Matrix metalloproteinase-9
P24158 PRTN3 Myeloblastin
P10646 TFPI Tissue factor pathway inhibitor
P05164 MPO Myeloperoxidase
P13686 ACP5 Tartrate-resistant acid phosphatase type 5
P15144 ANPEP Aminopeptidase N
P15085 CPA1 Carboxypeptidase A1
P15086 CPB1 Carboxypeptidase B
P07339 CTSD Cathepsin D
Q92876 KLK6 Kallikrein-6
P08254 MMP3 Stromelysin-1
Q9UBR2 CTSZ Cathepsin Z
P15166 PON3 Serum paraoxonase/lactonase 3
P00750 PLAT Tissue-type plasminogen activator
P08253 MMP2 72 kDa type IV collagenase
P00749 PLAU Urokinase-type plasminogen activator
P42574 CASP3 Caspase-3
Extracellular Matrix Proteins Q9HCB6 SPON1 Spondin-1
P98160 HSPG2 Basement membrane-specific heparan sulfate proteoglycan core protein
Q9NQ76 MEPE Matrix extracellular phosphoglycoprotein
P02452 COL1A1 Collagen alpha-1(I) chain
P10451 SPP1 Osteopontin
P35247 SFTPD Pulmonary surfactant-associated protein D
Immune-related Proteins P05107 ITGB2 Integrin beta-2
P20160 AZU1 Azurocidin
P16109 SELP P-selectin
Q86VB7 CD163 Scavenger receptor cysteine-rich type 1 protein M130
P17931 LGALS3 Galectin-3
Q9UM47 NOTCH3 Neurogenic locus notch homolog protein 3
Q9NPY3 CD93 Complement component C1q receptor
Q9HCN6 GP6 Platelet glycoprotein VI
Q9Y624 F11R Junctional adhesion molecule A
Q5T2D2 TREML2 Trem-like transcript 2 protein
Transport & Binding Proteins P02786 TFRC Transferrin receptor protein 1
P15090 FABP4 Fatty acid-binding protein
P08833 IGFBP1 Insulin-like growth factor-binding protein 1
P18065 IGFBP2 Insulin-like growth factor-binding protein 2
Q16270 IGFBP7 Insulin-like growth factor-binding protein 7
Q96PL1 SCGB3A2 Secretoglobin family 3A member 2
Enzyme Inhibitors P05121 SERPINE1 Plasminogen activator inhibitor 1
Q99727 TIMP4 Metalloproteinase inhibitor 4
P04080 CSTB Cystatin-B
O95998 IL18BP Interleukin-18-binding protein
P19957 PI3 Elafin
Signaling Molecules Q12860 CNTN1 Contactin-1
P80370 DLK1 Protein delta homolog 1
Q13740 ALCAM CD166 antigen
P33151 CDH5 Cadherin-5
P28799 GRN Progranulin
Q13867 BLMH Bleomycin hydrolase
Q99969 RARRES2 Retinoic acid receptor responder protein 2
P16284 PECAM1 Platelet endothelial cell adhesion molecule
P04275 VWF von Willebrand factor
Others P16581 SELE E-selectin
Q9HD89 RETN Resistin
Q13231 CHIT1 Chitotriosidase-1
P16422 EPCAM Epithelial cell adhesion molecule
Q07654 TFF3 Trefoil factor 3
P56470 LGALS4 Galectin-4
O75594 PGLYRP1 Peptidoglycan recognition protein 1
Q8NBP7 PCSK9 Proprotein convertase subtilisin/kexin type 9
P02144 MB Myoglobin
NT-proBNP NT-proBNP N-terminal prohormone of brain natriuretic peptide
P27930 IL1R2 Interleukin-1 receptor type 2
P36222 CHI3L1 Chitinase-3-like protein 1
Q9UBR2 CTSZ Cathepsin Z
P15086 CPB1 Carboxypeptidase B

Protein Functions

Biological process

Primarily associated with immune systerm diseases, signal transduction, innate immune system, and cytokine signaling in immune systerm.

Disease area

Primarily associated with carsiovascule, metsbolic, cancer, imuune, and rheumatoid arthritis.

Workflow of Olink Proteomics

Demo Results of Olink Data

Heatmap of differentially expressed targets in diabetic AVs, highlighting sex-specific molecular pathway variations.

Diabetic AVs show sex-specific molecular pathway differences. (Miriam Goñi-Olóriz, et al. 2025)

Case Study

Cardiomyocyte and stromal cell cross-talk influences the pathogenesis of arrhythmogenic cardiomyopathy: a multi-level analysis uncovers DLK1-NOTCH pathway role in fibro-adipose remodelling

Journal: Cell death discovery
Year: 2024

  • Background
  • Results

ACM is a life-threatening, genetically determined disease primarily caused by gene mutations in desmosomal genes such as PKP2. Due to the complex etiology of ACM, the pathogenesis has not been fully elucidated, and there are currently no treatment methods targeting its causes. Various types of cardiomyocytes affected by gene mutations, such as cardiomyocytes (CM) and cardiac mesenchymal stem cells (cMSC), each contribute to the ACM phenotype, driving functional abnormalities and fibrofatty replacement, respectively. However, the relative importance of changes in CM and cMSC, as well as their interactions in disease progression, remain poorly understood.

Cell-to-cell communication occurs through paracrine signaling, involving soluble mediators. To investigate the efficient release of these mediators, we conducted a secretome analysis of co-cultures using Olink technology. Conditioned media were collected, and 92 cardiovascular-related factors were screened, with 36 showing differential secretion across four co-culture groups. Figure 5A illustrates the secretion diversity, while levels of the 36 factors are detailed. We focused on factors linked to ACM-dependent phenotypic changes. Col1a1, MMP9, and TIMP4 secretion increased in ACM-containing cMSC co-cultures (Figures 5B-D). Fibrosis- and mechanosensory-related factors, such as uPAR and PECAM-1, were elevated in ACM cMSCs and HC cMSCs, respectively (Figures 5E-F). GDF-15 and LDL receptors were upregulated in ACM cMSC co-cultures, while MBs were more abundant in ACM CM co-cultures (Figures 5G-I). Notably, DLK1 was uniquely secreted by HC CM co-cultures (Figure 5L).

Heatmap of paracrine signaling proteins mediating cell-cell communication in co-culture systems.Figure 1. Proteins involved in co-culturing paracrine interactions. (Angela Serena Maione, et al. 2024)

FAQs

How are the biomarkers in the Olink panel selected?

When building the new panel, we gathered information from widely used public bioinformatics databases such as Uniprot, Human Protein Atlas, Gene Ontology, and DisGeNET. We select and evaluate a combination of known and exploratory biomarkers to obtain suitable antibodies, which are then required to pass our rigorous validation tests and requirements. The selection process and panel composition are developed based on the input of experts in the respective fields.

What instruments do I need to run the Olink Target 96?

If you are running our panels in your lab, the Olink Signature Q100 needs to be used for detection and quantification. A validated PCR instrument with a reaction volume of 100 μL with a heated lid is also required during the extension step of the protocol. Standard BioTool's BioMark HD Reader and IFC Controller HX/MX/AX/Juno can be used in place of the Olink Signature Q100.

Should I dilute my samples before shipping them to Olink?

Generally not. For our dilution panels, we dilute your sample as part of the analysis. However, if you are running a matrix sample other than serum or plasma, we recommend that you discuss the dilution with your sales representative or our Olink support team, as well as protein concentration or cell density in some cases.

Why Creative Proteomics

Cutting-Edge Data Integration

Combining Olink proteomics with multi-omics data enables holistic disease insights and accelerates therapeutic target discovery.

Customized Analytical Pipelines

Custom bioinformatics pipelines are created to enable precise data processing and generate actionable insights in complex research projects.

Collaborative Research Partnerships

collaborates with academia and industry, offering co-development and innovative solutions to achieve impactful research outcomes.

Sample Requirements

Sample Type Recommended Sample Size Sample Quality Pre-treatment and Storage Sample Transport
Plasma/Serum/Body Fluid 40µL/sample Protein concentration: 0.5mg/ml ~ 1mg/ml Transfer to a clean tube, aliquot into EP tubes or 96-well plates, store at -80℃ Seal with foil, ship with dry ice
Tissue
Cells
Exosomes
Other

References

  1. Maione, A. S., Iengo, L., Sala, L., et al. (2024). Cardiomyocyte and stromal cell cross-talk influences the pathogenesis of arrhythmogenic cardiomyopathy: a multi-level analysis uncovers DLK1-NOTCH pathway role in fibro-adipose remodelling. Cell death discovery, 10(1), 484. https://doi.org/10.1038/s41420-024-02232-8 
  2. Goñi-Olóriz, M., Garaikoetxea Zubillaga, M., San Ildefonso-García, S., et al. (2025). Chemerin is a new sex-specific target in aortic stenosis concomitant with diabetes regulated by the aldosterone/mineralocorticoid receptor axis. American journal of physiology. Heart and circulatory physiology, 328(3), H639–H647. https://doi.org/10.1152/ajpheart.00763.2024 

* For research purposes only, not intended for clinical diagnosis, treatment, or individual health assessments.

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