Mouse myeloma cell line NS0-derived recombinant human u-Plasminogen Activator (uPA)/Urokinase Catalytic Domain Ser21-Leu431 Accession # P00749
Specificity
Detects human u-Plasminogen Activator (uPA)/Urokinase Catalytic Domain in direct ELISAs and Western blots. In Western blots under reducing conditions, it reacts with the catalytic domain (B chain) only. In Western blots under non-reducing conditions, it reacts with the B chain and disulfide bond-linked B and A chains. In direct ELISAs, no cross-reactivity with recombinant human (rh) Factor X, rhHGFA, rhKLK‑3, -4, -5, -6, -8, -10, -11, rhThrombin, or recombinant mouse WIF-1 is observed.
Source
N/A
Isotype
IgG2a
Clonality
Monoclonal
Host
Mouse
Gene
PLAU
Purity Statement
Protein A or G purified from hybridoma culture supernatant
Innovator's Reward
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Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.5 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for u-Plasminogen Activator/Urokinase Antibody (204212) [Unconjugated]
ATF
EC 3.4.21
EC 3.4.21.73
plasminogen activator, urokinase
PLAU
uPA
u-PA
uPlasminogen Activator
u-Plasminogen Activator
urinary
Urokinase
urokinase-type plasminogen activator
Background
uPA is a serine protease with an extremely limited substrate specificity, cleaving the sequence Cys-Pro-Gly-Arg560-Val561-Val-Gly-Gly-Cys in plasminogen to form plasmin (1). uPA is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium (2). For example, the combination (both low vs. either or both high) of uPA and its inhibitor, plasminogen activator inhibitor-1 (PAI-1), outperforms the single factors as well as other traditional prognostic factors with regard to risk group assessment for breast cancer, particularly in node-negative breast cancer (3). The human uPA is initially synthesized as 431 amino acid precursor with a N-terminal signal peptide (20 residues) (4‑6). The single chain molecule is processed into a disulfide-linked two-chain molecule. The B chain starting at Ile179 corresponds to the catalytic domain. Two forms of the A chain exist, one starting at Ser21 (the long form) and the other at Lys156 (the short form). The resulting two-chain forms have different molecular weights (MW). The B chain is common for both forms whereas the long and short A chains are unique to the high and low MW forms, respectively. The long A chain contains an EGF-like domain, which is responsible for binding of the uPA receptor (uPAR).
Ellis, V. (2004) in Handbook of Proteolytic Enzymes. Barrett, A.J. et al. eds., Academic Press, San Diego, pp.1677.
Duffy, M.J. (2002) Biochem. Soc. Trans. 30:207.
Harbeck, N. et al. (2002) Clin. Breast Cancer 3:196.
Riccio, A. et al. (1985) Nucleic Acids Res. 13:2785.
Nagai, M. et al. (1985) Gene 36:183.
Jacobs, P. et al. (1985) DNA 4:139.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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