In addition to the monomeric mammalian progelatinase, two additional forms of progelatinase have been identified. The shorter of these additional forms is a covalently linked, disulfide-bridged protein that heterodimerizes with a short protein; an å2-Microglobulin-related protein known as neutrophil gelatinase-associated lipocalin (NGAL), which is moderately expressed in breast and lung tissues. NGAL belongs to the lipocalin family and has a high degree of similarity with rat å2-Microglobulin-related protein and mouse protein 24p3. NGAL is able to bind a derivative of the bacterial chemotactic peptide, suggesting that it has important immuno-modulatory functions. NGAL has been described as an inflammatory protein; it is released into the circulation as a result of the inflammatory activation of leukocytes initiated by the extra-corporeal circulation. In addition, NGAL synthesis is induced in epithelial cells in inflammatory and neoplastic colorectal diseases. In conclusion, NGAL may serve as a scavenger of bacterial products to function in the anti-inflammatory process.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
ELISAIFIHCIPWB
recommended for detection of NGAL of human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMonkeyMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 58-187 mapping within an internal region of NGAL of human origin
Tissue Specificity
epitope corresponding to amino acids 58-187 mapping within an internal region of NGAL of human origin