Il existe 8+ publications pour ce produit.
L’anticorps anti-PLAU Polyclonal Lapin est utilisé pour la détection de PLAU dans des échantillons de Humain et Souris. Il a été validé pour WB, FACS et IHC (p).
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).
Antigène
PLAU
(Plasminogen Activator, Urokinase (PLAU))
Sujet
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.