| Product | Product Code | Pack Size | Concentration | RT Storage | 2-8°C Storage | Shelf Life |
|---|---|---|---|---|---|---|
| Collagen | HB-5504-FG | 2 x 1.0 ml | 100µg/ml 95% type-I fibrils from equine tendon |
8 hours | 14 days | 3 years |
Hart Biologicals Collagen Reagent is used to diagnose platelet dysfunction, or normal platelet activity in human platelet rich plasma or whole blood. The reagent contains a lyophilised preparation of approximately 100µg/ml of Type I (>95%) collagen fibrils from equine tendon with added stabilisers.
Collagen is a structural protein which is virtually ubiquitous throughout the human body. During primary haemostasis following blood vessel injury, the adhesion of platelets to exposed collagen at the site of injury plays a key role in the arrest of bleeding from this site. Any interference with the ability of platelets to interact with exposed collagen is therefore a possible cause of an unexplained bleeding tendency. Some congenital defects of platelet function, as well as some acquired and drug-induced effects can affect the aggregation of platelets stimulated by collagen.
Investigation of the ability of patient platelets to aggregate to a controlled preparation of collagen fibrils is an important part of the investigation of suspected disorder of platelet function.
| Product | Product Code | Pack Size | Concentration | RT Storage | 2-8°C Storage | Shelf Life |
|---|---|---|---|---|---|---|
| Collagen | HB-5504-FG | 2 x 1.0 ml | 100µg/ml 95% type-I fibrils from equine tendon |
8 hours | 14 days | 3 years |
Hart Biologicals Collagen Reagent is used to diagnose platelet dysfunction, or normal platelet activity in human platelet rich plasma or whole blood. The reagent contains a lyophilised preparation of approximately 100µg/ml of Type I (>95%) collagen fibrils from equine tendon with added stabilisers.
Collagen is a structural protein which is virtually ubiquitous throughout the human body. During primary haemostasis following blood vessel injury, the adhesion of platelets to exposed collagen at the site of injury plays a key role in the arrest of bleeding from this site. Any interference with the ability of platelets to interact with exposed collagen is therefore a possible cause of an unexplained bleeding tendency. Some congenital defects of platelet function, as well as some acquired and drug-induced effects can affect the aggregation of platelets stimulated by collagen.
Investigation of the ability of patient platelets to aggregate to a controlled preparation of collagen fibrils is an important part of the investigation of suspected disorder of platelet function.
