This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogène
This Urokinase (PLAU) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 60-90 amino acids from the N-terminal region of human Urokinase (PLAU).
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C,-20 °C
Date de péremption
6 months
Kim, Minai-Tehrani, Kim, Shin, Hong, Kim, Lee, Chang, Yu, Bang, Cho, Yoon, Yu, Jiang, Cho: "Suppression of tumor growth in H-ras12V liver cancer mice by delivery of programmed cell death protein 4 using galactosylated poly(ethylene glycol)-chitosan-graft-spermine." dans: Biomaterials, Vol. 33, Issue 6, pp. 1894-902, (2011) (PubMed).
Eefting, de Vries, Grimbergen, Karper, van Bockel, Quax et al.: "In vivo suppression of vein graft disease by nonviral, electroporation-mediated, gene transfer of tissue inhibitor of metalloproteinase-1 linked to the amino terminal fragment of urokinase ..." dans: Journal of vascular surgery, Vol. 51, Issue 2, pp. 429-37, (2010) (PubMed).
Bacac, Migliavacca, Stehle, McKee, Delorenzi, Coindre, Guillou, Stamenkovic: "A gene expression signature that distinguishes desmoid tumours from nodular fasciitis." dans: The Journal of pathology, Vol. 208, Issue 4, pp. 543-53, (2006) (PubMed).
Strausberg, Feingold, Grouse, Derge, Klausner, Collins, Wagner, Shenmen, Schuler, Altschul, Zeeberg, Buetow, Schaefer, Bhat, Hopkins, Jordan, Moore, Max, Wang, Hsieh, Diatchenko, Marusina, Farmer et al.: "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. ..." dans: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 26, pp. 16899-903, (2002) (PubMed).
Sperl, Jacob, Arroyo de Prada, Stürzebecher, Wilhelm, Bode, Magdolen, Huber, Moroder: "(4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase." dans: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, Issue 10, pp. 5113-8, (2000) (PubMed).
Türkmen, Schmitt, Schmalfeldt, Trommler, Hell, Creutzburg, Graeff, Magdolen: "Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer." dans: Electrophoresis, Vol. 18, Issue 5, pp. 686-9, (1997) (PubMed).
Conne, Berczy, Belin: "Detection of polymorphisms in the human urokinase-type plasminogen activator gene." dans: Thrombosis and haemostasis, Vol. 77, Issue 3, pp. 434-5, (1997) (PubMed).
Yoshimoto, Ushiyama, Sakai, Tamaki, Hara, Takahashi, Sawasaki, Hanada: "Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure." dans: Biochimica et biophysica acta, Vol. 1293, Issue 1, pp. 83-9, (1996) (PubMed).
PLAU, a member of the peptidase family S1, is a potent plasminogen activator and is clinically used for therapy of thrombolytic disorders. PLAU specifically cleaves the Arg-|-Val bond in plasminogen to form plasmin. The protein is found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A. Cleavage occurs after residue 155 in the low molecular mass form to yield a short A1 chain. The protein is used in Pulmonary Embolism (PE) to initiates fibrinolysis. Structurally, PLAU contains 1 EGF-like domain and 1 kringle domain.