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Merck
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Fontos dokumentumok

SRP6273

Sigma-Aldrich

UPA human

recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

Szinonimák:

ATF, BDPLT5, PLAU, QPD, UPA, URK, Urokinase, u-PA

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352202
NACRES:
NA.32

biológiai forrás

human

rekombináns

expressed in HEK 293 cells

tag

6-His tagged (C-terminus)

Teszt

≥95% (SDS-PAGE)

Forma

lyophilized powder

molekulatömeg

calculated mol wt 45 kDa
observed mol wt 18 kDa
observed mol wt 32 kDa
observed mol wt 50 kDa

kiszerelés

pkg of 10 μg
pkg of 50 μg

szennyeződések

<1 EU/μg endotoxin (LAL test)

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

−20°C

Géninformáció

human ... uPA(5328)

Általános leírás

DTT-reduced. Protein migrates as three bands corresponding to the long α chain, β chain and unprocessed full-length chain due to glycosylation and cleavage. Ser21, Ile179 & Lys156 is the predicted N-terminus.
The PLAU (plasminogen activator, urokinase) gene is mapped to human chromosome 10q22.2.
Urokinase-type plasminogen activator is also known as PLAU and uPA. The human uPA is initially synthesized as 431 amino acid precursor with an N-terminal signal peptide (20 residues). The single chain molecule is processed into a disulfide-linked two-chain molecule of different molecular weights. Two forms of the A chain exist, starting at Ser21 (the long form) and Lys156 (the short form). The long and short A chains are unique to the high and low molecular weight forms, respectively. The long A chain contains an EGF (epidermal growth factor)-like domain, responsible for binding of the PLAU receptor. The B chain corresponds to the catalytic domain. The gene encoding it is localized on human chromosome 10.

Biokémiai/fiziológiai hatások

Urokinase-type plasminogen activator is a serine protease with extremely limited substrate specificity, cleaving the sequence Cys-Pro-Gly-Arg560-Val561-Val-Gly-Gly-Cys in plasminogen to form plasmin. It is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium. uPA (plasminogen activator, urokinase) - mediated degradation of extracellular matrix of migrating cells is essential for tissue remodeling, invasiveness and angiogenesis. uPA promotes pathogenesis of Psoriasis and basal cell carcinoma. uPA activates growth factors and metalloproteinases.

Fizikai forma

Lyophilized from 0.22 μm filtered solution in HEPES, NaCl and CaCl2. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.

Feloldás

Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Increased expression of uPA, uPAR, and PAI-1 in psoriatic skin and in basal cell carcinomas.
Rubina K A, et al.
Archives of Dermatological Research, 309(6), 433-442 (2017)
Enhanced meta-analysis and replication studies identify five new psoriasis susceptibility loci.
Tsoi L C, et al.
Nature Communications, 6, 7001-7001 (2015)
Up-Regulation of PAI-1 and Down-Regulation of uPA Are Involved in Suppression of Invasiveness and Motility of Hepatocellular Carcinoma Cells by a Natural Compound Berberine.
Wang X
International Journal of Molecular Sciences, 17(4), 577-577 (2016)
Ajay Kumar et al.
Frontiers in immunology, 12, 807775-807775 (2022-01-04)
Leptospira, a zoonotic pathogen, is known to infect various hosts and can establish persistent infection. This remarkable ability of bacteria is attributed to its potential to modulate (activate or evade) the host immune response by exploiting its surface proteins. We
Jason J Paxman et al.
Nature communications, 10(1), 1967-1967 (2019-05-01)
Autotransporters are the largest family of outer membrane and secreted proteins in Gram-negative bacteria. Most autotransporters are localised to the bacterial surface where they promote colonisation of host epithelial surfaces. Here we present the crystal structure of UpaB, an autotransporter

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