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PLG protein :: Plasminogen, Glu Protein

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Catalog # MBS635131
Unit / Price
  1 mg  /  $410 +1 FREE 8GB USB
PLG protein
Product Name

Plasminogen, Glu (PLG), Protein

Also Known As

Plasminogen, Glu, Human

Product Gene Name
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Chromosome Location
Chromosome: 6; NC_000006.11 (161123225..161175086). Location: 6q26
OMIM
173350
3D Structure
ModBase 3D Structure for P00747
Host
Human plasma
Purity/Purification
Affinity Purified
Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino (3), utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and C
Form/Format
Supplied as a liquid in 50% glycerol/H2O.
Extinction Coefficient
E1%1cm, 280nm=17.0 (5)
Isoelectric Point
6.2 (1)
Mode of Action
Zymogen; precursor to the serine protease plasmin
Structure
Single chain, 24 intra chain disulfide bridges, 5 kringle regions.

Percent carbohydrate: ~2%
Preparation and Storage
May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Other Notes
Small volumes of PLG protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
PLG protein
Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4mM (1,2). The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10e-6M) and four low affinity (Kd=5x10e-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of plasminogen with fibrin and a2-antiplasmin is mediated by these lysine binding sites. Native glu-plasminogen (Mr=88,000) is readily converted to Lys-77-plasminogen (Mr=83,000) by plasmin hydrolysis of the Lys76-Lys77 peptide bond. Elastase catalyzed cleavage of the Val441-Val442 peptide bond of glu-plasminogen yields a functionally active zymogen termed Val-442 plasminogen or mini-plasminogen.

The conversion of plasminogen to plasmin occurs by a variety of mechanisms, but all result in hydrolysis of the Arg560-Val561 peptide bond of plasminogen, yielding two chains which remain covalently associated by a disulfide bond.
NCBI/Uniprot data below describe general gene information for PLG. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
NCBI Official Full Name
Plasminogen
NCBI Official Synonym Full Names
plasminogen
NCBI Official Symbol
NCBI Protein Information
plasminogen
UniProt Protein Name
Plasminogen
Protein Family
UniProt Gene Name
UniProt Entry Name
PLMN_HUMAN
NCBI Summary for PLG
The protein encoded by this gene is a secreted blood zymogen that is activated by proteolysis and converted to plasmin and angiostatin. Plasmin dissolves fibrin in blood clots and is an important protease in many other cellular processes while angiostatin inhibits angiogenesis. Defects in this gene are likely a cause of thrombophilia and ligneous conjunctivitis. Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Dec 2009]
UniProt Comments for PLG
Plasminogen: 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. Defects in PLG are the cause of plasminogen deficiency (PLGD). PLGD is characterized by decreased serum plasminogen activity. Two forms of the disorder are distinguished: type 1 deficiency is additionally characterized by decreased plasminogen antigen levels and clinical symptoms, whereas type 2 deficiency, also known as dysplasminogenemia, is characterized by normal, or slightly reduced antigen levels, and absence of clinical manifestations. Plasminogen deficiency type 1 results in markedly impaired extracellular fibrinolysis and chronic mucosal pseudomembranous lesions due to subepithelial fibrin deposition and inflammation. The most common clinical manifestation of type 1 deficiency is ligneous conjunctivitis in which pseudomembranes formation on the palpebral surfaces of the eye progresses to white, yellow-white, or red thick masses with a wood-like consistency that replace the normal mucosa. Belongs to the peptidase S1 family. Plasminogen subfamily.

Protein type: Protease; Secreted; Motility/polarity/chemotaxis; Secreted, signal peptide; EC 3.4.21.7

Chromosomal Location of Human Ortholog: 6q26

Cellular Component: extracellular space; cell surface; extrinsic to external side of plasma membrane; plasma membrane; extracellular region

Molecular Function: protein domain specific binding; protein binding; serine-type peptidase activity; serine-type endopeptidase activity; apolipoprotein binding; receptor binding

Biological Process: platelet activation; extracellular matrix organization and biogenesis; tissue remodeling; muscle maintenance; myoblast differentiation; extracellular matrix disassembly; negative regulation of cell proliferation; fibrinolysis; negative regulation of fibrinolysis; cellular protein metabolic process; platelet degranulation; proteolysis involved in cellular protein catabolic process; tissue regeneration; positive regulation of fibrinolysis; blood coagulation; transmembrane transport

Disease: Plasminogen Deficiency, Type I
Precautions
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Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

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