|Tested species reactivity||Human|
|Host / Isotype||Goat / IgG|
|Immunogen||Purified native HMW-tcuPA and LMW-scuPA (mixture 50/50), isolated from human urine.|
|Storage buffer||PBS with mannitol|
|Storage Conditions||4° C|
|Tested Applications||Dilution *|
|Immunohistochemistry (Frozen) (IHC (F))||1:50|
|Immunohistochemistry (Paraffin) (IHC (P))||1:50|
|Western Blot (WB)||Assay dependent.|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This antibody has been pre-absorbed with immobilized total human serum proteins to remove non-specific antibodies. This antibody is known to bind human HMW-scuPA (54 kDa), HMW-tsuPA (52 kDa), and LMW-scuPA (33 kDa), completely inhibiting the ability of Urokinase to activate plasminogen.
Reconstitute with 1 ml of distilled water and add preservative if preferred.
This gene encodes a serine protease involved in degradation of the extracellular matrix and possibly tumor cell migration and proliferation. A specific polymorphism in this gene may be associated with late-onset Alzheimer's disease and also with decreased affinity for fibrin-binding. This protein converts plasminogen to plasmin by specific cleavage of an Arg-Val bond in plasminogen. Plasmin in turn cleaves this protein at a Lys-Ile bond to form a two-chain derivative in which a single disulfide bond connects the amino-terminal A-chain to the catalytically active, carboxy-terminal B-chain. This two-chain derivative is also called HMW-uPA (high molecular weight uPA). HMW-uPA can be further processed into LMW-uPA (low molecular weight uPA) by cleavage of chain A into a short chain A (A1) and an amino-terminal fragment. LMW-uPA is proteolytically active but does not bind to the uPA receptor. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
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