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AB90928

Native human Plasmin protein (Active)

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(3 Publications)

Native human Plasmin protein (Active) is a Human Full Length protein with >=95% purity and suitable for Functional studies and SDS-PAGE.The predicted molecular weight of ab90928 native protein is 81 kDa.

- Save time and ensure accurate results- use our Plasmin protein as a control
- Optimal protein bioactivity and stability

View Alternative Names

Plasminogen, PLG

1 Images
SDS-PAGE - Native human Plasmin protein (Active) (AB90928)
  • SDS-PAGE

Unknown

SDS-PAGE - Native human Plasmin protein (Active) (AB90928)

4-12% Bis-Tris NuPAGE gel.

Lane 1 : Plasmin - 5 μg (reduced/ heated)

Lane 2 : Plasmin - 10 μg (reduced/ heated)

Lane 3 : Plasmin - 20 μg (reduced/ heated)

Lane 4 : LMW Standard

Lane 5 : Plasmin - 5 μg (non-reduced/ no heat)

Lane 6 : Plasmin - 10 μg (non-reduced/ no heat)

Lane 7 : Plasmin - 20 μg (non-reduced/ no heat)

Key facts

Purity

>95% SDS-PAGE

Expression system

Native

Tags

Tag free

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

15 units/mg protein

One unit is defined as the amount of enzyme that hydrolyzes one μmole of tosyl-Gly-Pro-Lys-pNA per minute at 25°C, pH 7.8. Note: One unit = 1.25 CU.

Accession

P00747

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

pH: 7.4 Constituents: 0.946% D-(+)-Trehalose dihydrate, 0.24% Sodium dihydrogen phosphate

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

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We recommend this product because it’s often used in the same experiment or related research.

We advise that you always check the datasheet to ensure it fits your experiments, or contact ourtechnical teamfor help.

Product details

The Native human Plasmin protein (Active) ab90928 is prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.

Ensure the validity of your result using our native human Plasmin protein as a positive control in SDS-PAGE. The bioactive native human Plasmin ab90928 has been prepared by using streptokinase to activate human plasma plasminogen.

Check out our protein gel staining guide for SDS-PAGE here

Protein Determination: Extinction Coefficient (ε) 0.1% at 280 nm 1cm pathway = 1.71

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"81 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Native","expressionSystem":null,"accessionNumber":"P00747","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Plasmin a serine protease enzyme with a mass of approximately 79 kDa is an important player in the fibrinolytic system. Commonly referred to by alternate names like profibrinolysin or fibrinolysin it is mainly expressed in the liver and circulates in the blood as an inactive zymogen called plasminogen. Plasminogen is activated to plasmin through the action of activators such as tissue plasminogen activator (tPA) and urokinase (uPA). The activation to plasmin involves a cleavage at specific peptide bonds which exposes the active site that allows it to function as a protease.
Biological function summary

The enzyme plasmin degrades fibrin in blood clots a critical function in the process of clot resolution. It belongs to the family of serine proteases and does not form part of a larger protein complex. The activity of plasmin is modulated by inhibitors like alpha-2-antiplasmin which bind to plasmin and prevent excessive degradation of fibrin. Bovine plasmin shares similar functions and serves as a model for studying human plasmin activity. Researchers often measure plasmin activity through specific assays to understand changes in fibrinolytic activity within the body.

Pathways

Plasmin plays an integral role in the fibrinolytic pathway and is also involved in tissue remodeling and wound healing. The fibrinolytic pathway centers on the balance of plasminogen activation and inhibition which directly influences thrombolysis. Proteins such as tPA and uPA facilitate the conversion of plasminogen to plasmin and are tightly regulated to ensure proper physiological function. In the context of wound healing plasmin helps activate matrix metalloproteases leading to extracellular matrix breakdown and cell migration.

The regulation of plasmin is closely associated with pathological conditions such as thrombosis and liver disease. An overactive plasmin system can result in conditions like excessive bleeding or hemorrhage while inadequate plasmin activity may lead to thrombosis due to impaired clot breakdown. The interaction between plasmin and plasmin inhibitors like alpha-2-antiplasmin is critical in diseases such as liver cirrhosis where imbalances in fibrinolysis can have significant clinical outcomes. Understanding these interactions helps in developing therapeutic strategies to modulate plasmin activity in various disorders.

Specifications

Form

Lyophilized

General info

Function

Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.. Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.. (Microbial infection) ENO/enoloase from parasite P.falciparum (strain NF54) interacts with PLG present in the mosquito blood meal to promote the invasion of the mosquito midgut by the parasite ookinete (PubMed : 21949403). The catalytic active form, plasmin, is essential for the invasion of the mosquito midgut (PubMed : 21949403).. (Microbial infection) Binds to OspC on the surface of B.burgdorferi cells, possibly conferring an extracellular protease activity on the bacteria that allows it to traverse host tissue.

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Post-translational modifications

N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 sialic acid residues (microheterogeneity).. In the presence of the inhibitor, the activation involves only cleavage after Arg-580, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide.. (Microbial infection) The Y.pestis Pla protein cleaves between Arg-580 and Val-581, generating plasmin which facilitates bacterial migration and infection (PubMed:22645135).

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.. Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.. (Microbial infection) ENO/enoloase from parasite P.falciparum (strain NF54) interacts with PLG present in the mosquito blood meal to promote the invasion of the mosquito midgut by the parasite ookinete (PubMed : 21949403). The catalytic active form, plasmin, is essential for the invasion of the mosquito midgut (PubMed : 21949403).. (Microbial infection) Binds to OspC on the surface of B.burgdorferi cells, possibly conferring an extracellular protease activity on the bacteria that allows it to traverse host tissue.
See full target information PLG

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Translational vision science & technology 12:23 PubMed37074731

2023

Plasmin-Induced Lens Epithelial Cells Detachment for the Reduction of Posterior Capsular Opacification.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaomei Bai,Jingli Liang,Yufan Yin,Yuanfeng Jiang,Fangyu Zhao,Fang Tian,Xiteng Chen,Lijie Dong,Shaochong Bu

Nature chemical biology 18:1125-1134 PubMed35941237

2022

Programmable DARPin-based receptors for the detection of thrombotic markers.

Applications

Unspecified application

Species

Unspecified reactive species

Tobias Strittmatter,Yidan Wang,Adrian Bertschi,Leo Scheller,Patrick C Freitag,Preetam Guha Ray,Pascal Stuecheli,Jonas V Schaefer,Thomas Reinberg,Dimitrios Tsakiris,Andreas Plückthun,Haifeng Ye,Martin Fussenegger

Human molecular genetics 25:328-39 PubMed26604146

2015

Extracellular cleavage of collagen XVII is essential for correct cutaneous basement membrane formation.

Applications

Unspecified application

Species

Unspecified reactive species

Machiko Nishimura,Wataru Nishie,Yoshinori Shirafuji,Satoru Shinkuma,Ken Natsuga,Hideki Nakamura,Daisuke Sawamura,Keiji Iwatsuki,Hiroshi Shimizu
View all publications

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