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HABP2 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q14520 |
|---|---|
| Other Accession | NP_004123 |
| Clone Names | 80513188 |
| Gene ID | 3026 |
|---|---|
| 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 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | HABP2 |
|---|---|
| Synonyms | HGFAL, PHBP |
| 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 (PubMed:8827452, PubMed:10754382, PubMed:11217080). May function as a tumor suppressor negatively regulating cell proliferation and cell migration (PubMed:26222560). |
| 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.
Background
HABP2 is an extracellularserine protease that binds hyaluronic acid and is involved in celladhesion. The encoded protein is synthesized as a single chain, butthen undergoes an autoproteolytic event to form the functionalheterodimer. Further autoproteolysis leads to smaller, inactivepeptides. This protease is known to cleave urinary plasminogenactivator, coagulation factor VII, and the alpha and beta chains offibrinogen, but not prothrombin, plasminogen, or the gamma chain offibrinogen. Two transcript variants encoding different isoformshave been found for this gene.
References
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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