|Application ||WB, IHC-P, E|
|Calculated MW||62672 Da|
|Antigen Region||378-408 aa|
|Other Names||Hyaluronan-binding protein 2, 3421-, Factor VII-activating protease, Factor seven-activating protease, FSAP, Hepatocyte growth factor activator-like protein, Plasma hyaluronan-binding protein, Hyaluronan-binding protein 2 50 kDa heavy chain, Hyaluronan-binding protein 2 50 kDa heavy chain alternate form, Hyaluronan-binding protein 2 27 kDa light chain, Hyaluronan-binding protein 2 27 kDa light chain alternate form, HABP2, HGFAL, PHBP|
|Target/Specificity||This HABP2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 378-408 amino acids from the C-terminal region of human HABP2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HABP2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.|
|Cellular Location||Secreted. Note=Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form|
|Tissue Location||Ubiquitously expressed.|
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Provided below are standard protocols that you may find useful for product applications.
HABP2 is an extracellular serine protease that binds hyaluronic acid and is involved in cell adhesion. The encoded protein is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. This protease is known to cleave urinary plasminogen activator, coagulation factor VII, and the alpha and beta chains of fibrinogen, but not prothrombin, plasminogen, or the gamma chain of fibrinogen. Two transcript variants encoding different isoforms have been found for this gene.
Choi-Miura, N.H., et al. Biol. Pharm. Bull. 24(2):140-143(2001)
Sumiya, J., et al. J. Biochem. 122(5):983-990(1997)
Choi-Miura, N.H., et al. J. Biochem. 119(6):1157-1165(1996)
Gupta, S., et al. Eur. J. Cell Biol. 56(1):58-67(1991)
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