Cell damage and toxicity - FABP ELISA Kits
Highly sensitive measurement of cytosolic proteins allows early and rapid detection of loss of cell membrane integrity. Highly sensitive detection of disturbed cell membrane integrity is of importance in cellular toxicology studies and in various experimental and clinical situations like myocardial infarction and liver transplantation.
Fatty acid binding proteins (FABP) with tissue specificity are especially useful for early detection of ischemically damaged organs. Interestingly, ischemically damaged organs are characterized histologically by (near) absence of FABP, facilitating recognition of such areas.
Validated ELISA kit sample types :
|CS : Cell culture supernatant||P : Plasma|
|S : Serum||U : Urine|
|Description||Species||Sample type||Product code|
|I-FABP||Human||CS P S U||HK406|
|L-FABP||Human||CS P S U||HK404|
Fatty acid-binding proteins (FABPs) are a class of cytoplasmic proteins that bind long chain fatty acids. FABPs are small intracellular proteins (~13-14 kDa) with a high degree of tissue specificity. They are abundantly present in various cell types and play an important role in the intracellular utilization of fatty acids, transport and metabolism. There are at least nine distinct types of FABP, each showing a specific pattern of tissue expression. Due to its small size, FABP leaks rapidly out of ischemically damaged necrotic cells leading to a rise in serum levels. Ischemically damaged tissues are characterized histologically by absence (or low presence) of FABP facilitating recognition of such areas.
Liver-type fatty acid binding protein (L-FABP, FABP1) is predominantly expressed in liver. The L-FABP protein is derived from the human FABP1 gene. L-FABP is a sensitive marker for cell damage of liver cells in vitro and in vivo. L-FABP is also a marker for rapid hepatocyte lysis in vitro (as for example in toxicology assays) and for detection of liver damage during and after transplantation. Serum/plasma and urine of healthy individuals contains approximately 12 ng/ml and 16 ng/ml L-FABP, respectively.
The H-FABP protein is derived from the FABP3 gene. The FABP content of heart muscle (H-FABP) is markedly high, 10-20 mol% of cytoplasmic proteins. Following acute myocardial infarction (AMI) the small protein H-FABP is rapidly released in to the circulation. Significantly elevated serum/plasma concentrations are found within 3 h after AMI which generally return to normal values within 12 to 24 h. These features make H-FABP a useful research tool for the early assessment or exclusion of AMI, and for the monitoring of a recurrent infarction. Constitutive H-FABP released from the heart after AMI is quantitatively recovered in serum/plasma. Thus assessment of H-FABP is also a very effective tool for the estimation of the infarct size. The H-FABP kit can also be used for measurement of brain-type FABP, a marker for brain injury detection.
In serum/plasma of healthy individuals approximately 1.6 ng/ml of H-FABP is present.
Intestinal FABP (I-FABP) is specifically localized in the epithelium cells of the small bowel. The I-FABP protein is derived from the human FABP2 gene. Normally, I-FABP is undetectable in serum. Many observations indicate that I-FABP is a useful biochemical marker for intestinal cell damage both in vivo and in vitro. Ischemically damaged cells are characterized histologically by absence (or low presence) of FABP facilitating recognition of areas of ischemically damaged cells.