Pegylated Interferon α-2a
IFNa-2a consists of a 165 amino acid chain. The amino acids Cys1 and Cys98 and Cys29 and Cys138 are connected by disulphide bonds
As a modification of the free IFN-α2a – a 19 kDa protein - the yeast-derived PEGylated IFN protein is chemically linked to a linear PEG reagent of a molecular weight of 20,000 Da (±5000 Da).
Renal Cell Carcinoma: Alone or in combination with Vinblastine or Sorafenib.
Hirudin has an unusual asymmetry of structural elements. A compact, hydrophobic core region in the amino-terminal half of the molecule contains alternating polar and nonpolar segments and all three disulfide bonds. The carboxy-terminal region is more extended and extremely hydrophilic. The tight and essentially irreversible binding of hirudin to thrombin depends on both ionic and hydrophobic interactions.
In thrombotic disorders Hirudin inactivates thrombin by forming a 1:1 stoichiometric complex that is stable throughout the physiological pH range. Hirudin directly inhibits the active site pocket and the fibrinogen binding site of free and clot-bound thrombin.
Thrombexx® ampoule /
Thrombexx® cream /
Extrauma® cream /
Extrauma® Forte Gel /
Extrauma ® HAEMO rrhoids
Follicle stimulating hormone
Human FSH (hFSH) is a dimeric glycoprotein (i.e. composed of two protein subunits) to which there are attached four complex carbohydrate structures. The FSH molecule exists in many different (iso)-forms.
The micro heterogeneity is due to differences in carbohydrate moieties. The carbohydrate moieties are important in determining the half-life of FSH and therefore modulate in-vivo biological action.
In female infertility:
In male infertility caused by hypogonadotrophic hypogonadism: