CaptureSelect™ Biotin Anti-Factor X Conjugate

CaptureSelect Biotin Anti-Factor X Conjugate consists of a 13-kDa recombinant single domain anti-Factor X antibody fragment chemically conjugated to biotin via an appropriate spacer that retains the binding reactivity of the antibody fragment when used in combination with streptavidin-based conjugates or streptavidin pre-coated surfaces. This conjugate allows you to detect, quantitate, and characterize the human coagulation Factor X and Factor Xa.

The antibody fragment specifically binds to human Factor X and its activated form Factor Xa from plasma and recombinant sources. It is highly selective for human Factor X and Xa with no affinity for other human plasma proteins. The ligand binds in a calcium dependent manner, so full release of the bound Factor X or Factor Xa molecule is achieved by addition of chelating agents like EDTA. Suitable binding and target-release conditions are listed below:

• Binding condition: 50 mM Tris, 150 mM NaCl, 5 mM CaCl₂ pH 7
• Release condition: 50 mM Tris, 150 mM NaCl, 5 mM EDTA pH 7

Applications for CaptureSelect Biotin Anti-Factor X Conjugate include ELISA, immunoprecipitation with streptavidin-coupled Dynabeads, Gyrolab™-based immunoassays, and label-free detection platforms such as those based on surface plasmon resonance (Biacore™ and IBIS-MX96 systems) and bio-layer interferometry (ForteBio™ Octet™ systems).

Coagulation Factor X is a vitamin K-dependent, liver-produced serine protease that serves as the first enzyme in the coagulation cascade to form fibrin. It is a two-chain glycoprotein with a molecular weight of approximately 59 kDa. While Factor X normally circulates in the plasma as an inactive molecule, the activation of Factor X is involved in both the intrinsic and extrinsic coagulation pathways.

Animal origin statement

CaptureSelect products contain affinity ligands based on recombinant single-domain antibody fragments (V_HH) created by a proprietary technology. The V_HH affinity ligand is a 12–15 kDa fragment comprising the three complementarity-determining regions (CDRs) that form the antigen-binding domain, efficiently produced in the yeast Saccharomyces cerevisiae by a production process free of any animal components (Animal Origin-Free).