PLAU/uPA Protein, Cynomolgus (HEK293, His)

PLAU, also known as uPA (urokinase plasminogen activator), exhibits defects in conserved residues critical for propagation feature annotation. This defect in the PLAU/uPA protein prevents the propagation of specific functional characteristics associated with this protein. PLAU/uPA Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived PLAU/uPA protein, expressed by HEK293 , with C-His labeled tag.

PLAU, also known as uPA (urokinase plasminogen activator), exhibits a deficiency in the conserved residue(s) crucial for propagating feature annotation. This deficiency in PLAU/uPA protein hampers the propagation of specific functional characteristics associated with this protein. PLAU/uPA is a serine protease that functions in the plasminogen activation system, playing a pivotal role in the regulation of fibrinolysis and extracellular matrix remodeling. It converts plasminogen into plasmin, a protease that degrades fibrin clots and various extracellular matrix components. PLAU/uPA is involved in processes such as tissue remodeling, cell migration, angiogenesis, and cellular invasion. The deficiency of the conserved residue(s) in PLAU/uPA protein may have significant implications for fibrinolysis regulation and extracellular matrix dynamics, warranting further investigation into the functional consequences of this deficiency on the protein's biological activities.

Cynomolgus

HEK293

C-8*His

A0A2K5WND1 (S21-L430)

102135886

Full Length of Mature Protein

SRELQVPSDCGCLNGGTCMSNKYFSSIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRSCLAWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKQLVQECMVQNCADGKKPSSPPEELQFQCGQRTLRPRFKIVGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVVSATHCFINYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHEDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSTYNDPPFGTSCEITGFGKENSTDYLYPERLKMTVVKLVSHQKCQQPHYYGSEVTTKMLCAADPQWETDSCQGDSGGPLVCSIQGHMTLTGIVSWGRGCALKDKPGVYTRVSRFLPWIHSHTREENGLAL

Approximately 23-25 kDa & 35-40 kDa & 50-60 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.