Rabbit anti-Human HABP2 Polyclonal Antibody, HRP conjugated

Uniprot Id

Q14520

Target Species

Human

Target Name

HABP2

Target Full Name

Hyaluronan-binding protein 2

Target Function

Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII. May function as a tumor suppressor negatively regulating cell proliferation and cell migration.

Target Involvement

Thyroid cancer, non-medullary, 5 (NMTC5)

Target Subcellular Location

Secreted. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form.

Target Protein Families

Peptidase S1 family

Target Tissue Specificity

Ubiquitously expressed.

Target Research Area

Cardiovascular

Target Synonyms

Factor seven activating protease; Factor seven-activating protease; Factor VII activating protein; Factor VII-activating protease; FSAP; HABP 2; HABP; Habp2; HABP2_HUMAN; Hepatocyte growth factor activator like protein; Hepatocyte growth factor activator-like protein; HGFAL; Hyaluronan binding protein 2; Hyaluronan-binding protein 2 27 kDa light chain alternate form; Hyaluronic acid binding protein 2; PHBP; Plasma hyaluronan binding protein; Plasma hyaluronan-binding protein

Target Background

This gene encodes a member of the peptidase S1 family of serine proteases. The encoded preproprotein is secreted by hepatocytes and proteolytically processed to generate heavy and light chains that form the mature heterodimer. Further autoproteolysis leads to smaller, inactive peptides. This extracellular protease binds hyaluronic acid and may play a role in the coagulation and fibrinolysis systems. Mutations in this gene are associated with nonmedullary thyroid cancer and susceptibility to venous thromboembolism. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed.