HABP2
HABP2 (hyaluronan binding protein 2) is a secreted serine protease of the peptidase S1 family, also known as Factor VII-activating protease, HABP, PHBP, HGFAL and FSAP. It activates coagulation factor VII and converts pro-urokinase to its active two-chain form. Browse Assay Genie's current range of HABP2 research reagents below, or read on for the biology behind the target.
HABP2 is an extracellular serine protease that acts on several components of the coagulation and fibrinolysis systems. It activates coagulation factor VII and converts the inactive single-chain urinary plasminogen activator (pro-urokinase) to the active two-chain form. It does not cleave prothrombin or plasminogen. On fibrinogen, it cleaves the alpha-chain at multiple sites and the beta-chain between Lys-53 and Lys-54, but it does not cleave the gamma-chain. It therefore does not initiate fibrin clot formation and does not cause fibrinolysis directly. UniProt also notes that HABP2 may act as a tumour suppressor, negatively regulating cell proliferation and cell migration.
The HABP2 gene encodes a member of the peptidase S1 family, classed by HGNC among the serine proteases and the kringle domain-containing genes. The preproprotein is secreted by hepatocytes and processed into heavy and light chains, which form the mature heterodimer. Further autoproteolysis produces smaller, inactive peptides. The protein binds hyaluronic acid, which gives the gene its name, and may contribute to coagulation and fibrinolysis. Alternative splicing gives multiple transcript variants, and at least one of them encodes a preproprotein that is proteolytically processed. Orthologues are annotated in mouse and rat (Habp2).
The gene has been known under several names, including hyaluronan-binding protein 2 as a previous name, and the symbols HABP, PHBP, HGFAL and FSAP. Mutations in HABP2 are associated with nonmedullary thyroid cancer and with susceptibility to venous thromboembolism. Researchers studying this protein often use an HABP2 antibody or HABP2 ELISA kit to follow its expression and processing.
HABP2 activates coagulation factor VII, so it is studied as a protease that contributes to the coagulation system.
By converting pro-urokinase to its active two-chain form, HABP2 links to fibrinolytic pathways without cleaving plasminogen directly.
Mutations in HABP2 are associated with susceptibility to venous thromboembolism, which makes it a candidate in thrombosis genetics.
HABP2 mutations are associated with nonmedullary thyroid cancer, and the protein may suppress cell proliferation and migration.
HABP2 is a secreted serine protease that activates coagulation factor VII and converts pro-urokinase to active two-chain urokinase. It cleaves fibrinogen alpha- and beta-chains but not the gamma-chain, so it does not form fibrin clots or cause fibrinolysis directly. It also binds hyaluronic acid.
HABP2 is also called Factor VII-activating protease, with the aliases HABP, PHBP, HGFAL and FSAP. The earlier name was hyaluronan-binding protein 2. Alternative splicing produces several transcript variants, and the secreted preproprotein is processed into heavy and light chains that form a heterodimer.
Mutations in HABP2 are associated with nonmedullary thyroid cancer and susceptibility to venous thromboembolism. Orthologues named Habp2 are annotated in mouse and rat. Check the datasheet of any product for its validated reactivity.
Coagulation factors, fibrinolysis components and other serine proteases that connect to HABP2 biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q14520; product specifications from Assay Genie datasheets.