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Recombinant Human PLG protein, GST-tagged

Cat.No. : PLG-9029H
Product Overview : Recombinant Human PLG(1 a.a. - 810 a.a.) fused with GST tag at N-terminal was expressed in Wheat Germ.
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Description : 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.
Source : Wheat Germ
Species : Human
Tag : GST
Form : 50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer.
Molecular Mass : 117 kDa
AA Sequence : MEHKEVVLLLLLFLKSGQGEPLDDY VNTQGASLFSVTKKQLGAGSIEECA AKCEEDEEFTCRAFQYHSKEQQCVI MAENRKSSIIIRMRDVVLFEKKVYL SECKTGNGKNYRGTMSKTKNGITCQ KWSSTSPHRPRFSPATHPSEGLEEN YCRNPDNDPQGPWCYTTDPEKRYDY CDILECEEECMHCSGENYDGKISKT MSGLECQAWDSQSPHAHGYIPSKFP NKNLKKNYCRNPDRELRPWCFTTDP NKRWELCDIPRCTTPPPSSGPTYQC LKGTGENYRGNVAVTVSGHTCQHWS AQTPHTHNRTPENFPCKNLDENYCR NPDGKRAPWCHTTNSQVRWEYCKIP SCDSSPVSTEQLAPTAPPELTPVVQ DCYHGDGQSYRGTSSTTTTGKKCQS WSSMTPHRHQKTPENYPNAGLTMNY CRNPDADKGPWCFTTDPSVRWEYCN LKKCSGTEASVVAPPPVVLLPDVET PSEEDCMFGNGKGYRGKRATTVTGT PCQDWAAQEPHRHSIFTPETNPRAG LEKNYCRNPDGDVGGPWCYTTNPRK LYDYCDVPQCAAPSFDCGKPQVEPK KCPGRVVGGCVAHPHSWPWQVSLRT RFGMHFCGGTLISPEWVLTAAHCLE KSPRPSSYKVILGAHQEVNLEPHVQ EIEVSRLFLEPTRKDIALLKLSSPA VITDKVIPACLPSPNYVVADRTECF ITGWGETQGTFGAGLLKEAQLPVIE NKVCNRYEFLNGRVQSTELCAGHLA GGTDSCQGDSGGPLVCFEKDKYILQ GVTSWGLGCARPNKPGVYVRVSRFV TWIEGVMRNN
Applications : Enzyme-linked Immunoabsorbent Assay; Western Blot (Recombinant protein); Antibody Production; Protein Array
Notes : Best use within three months from the date of receipt of this protein.
Storage : Store at -80 centigrade. Aliquot to avoid repeated freezing and thawing.
Gene Name : PLG plasminogen [ Homo sapiens ]
Official Symbol : PLG
Synonyms : PLG; plasminogen; plasmin; DKFZp779M0222;
Gene ID : 5340
mRNA Refseq : NM_000301
Protein Refseq : NP_000292
MIM : 173350
UniProt ID : P00747
Chromosome Location : 6q26
Pathway : Activation of Matrix Metalloproteinases, organism-specific biosystem; Angiopoietin receptor Tie2-mediated signaling, organism-specific biosystem; Blood Clotting Cascade, organism-specific biosystem; Complement and Coagulation Cascades, organism-specific biosystem; Complement and coagulation cascades, organism-specific biosystem; Complement and coagulation cascades, conserved biosystem; Degradation of the extracellular matrix, organism-specific biosystem;
Function : apolipoprotein binding; cell surface binding; peptidase activity; protein binding; protein domain specific binding; serine-type endopeptidase activity;

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (7)

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What is the clinical significance of PLG as a diagnostic or prognostic biomarker? 03/25/2021

PLG has been investigated as a potential diagnostic and prognostic biomarker for various diseases. For instance, altered PLG levels have been observed in cancer patients, serving as a potential marker for tumor progression and prognosis. Additionally, PLG has been implicated in cardiovascular diseases, where its levels can reflect the severity of certain conditions, such as thrombosis. Moreover, PLG may have utility as a biomarker in inflammatory disorders and neurological diseases. Further research is needed to validate the clinical utility of PLG as a biomarker and develop specific assays for its detection.

 What are the pathological implications of PLG dysregulation? 11/04/2018

Dysregulation of PLG has been associated with several pathological conditions. Decreased PLG levels or impaired activation can lead to impaired fibrinolysis, resulting in the formation of excessive blood clots. On the other hand, increased PLG activation or excessive Plasmin activity can promote tissue degradation, contributing to diseases such as chronic inflammation, cancer metastasis, and tissue damage. Moreover, PLG has been implicated in the pathogenesis of neurodegenerative disorders and cardiovascular diseases. Understanding the mechanisms underlying PLG dysregulation is crucial for designing therapeutic strategies to counteract its pathological implications.

What therapeutic strategies target PLG for the treatment of diseases? 08/10/2018

PLG-targeted therapeutic strategies have shown promise in various diseases. For example, agents that enhance PLG activation, such as tPA and uPA, have been employed to promote fibrinolysis and dissolve blood clots in conditions such as heart attacks and ischemic strokes. Conversely, inhibitors of PLG activation, such as PAIs, can be used to prevent excessive fibrinolysis and subsequent bleeding complications. Additionally, targeting PLG receptors or manipulating PLG interactions with other molecules may offer potential therapeutic avenues. However, further research is required to optimize these strategies and assess their efficacy and safety in clinical settings.

What is the full name and structure of the PLG protein? 06/08/2017

The PLG protein, also known as Plasminogen, is a single-chain glycoprotein composed of 790 amino acids. It consists of several domains, including a signal peptide, five kringle domains (K1-K5), and a serine protease domain. The signal peptide mediates protein secretion, while the kringle domains have numerous functions, such as binding to receptors and ligands. The serine protease domain is responsible for the conversion of Plasminogen to active Plasmin, a crucial enzyme in fibrinolysis and extracellular matrix remodeling processes.

What are the physiological functions of PLG in the human body? 04/27/2017

PLG plays a vital role in several physiological processes. Its primary function is as a precursor to Plasmin, which is involved in the degradation of blood clots (fibrinolysis). Plasmin also participates in tissue remodeling, wound healing, and cell migration. Additionally, PLG has been implicated in immune responses, angiogenesis, and cell adhesion. Its ability to interact with various receptors and bind to components of the extracellular matrix highlights its diverse and important functions in maintaining normal physiological homeostasis.

What is the biological function of PLG? 10/05/2016

PLG, also known as plasminogen, plays a crucial role in the fibrinolytic system. Its main biological function is to be converted into plasmin, an enzyme that breaks down fibrin clots. Plasminogen is activated by tissue plasminogen activator (tPA), which cleaves it into active plasmin. Plasmin then degrades fibrin clots, preventing the formation of thrombi and promoting the dissolution of existing blood clots. Additionally, PLG is involved in various physiological processes, such as wound healing, tissue remodeling, cell migration, and inflammation.

How is the activation of PLG regulated? 07/31/2016

The activation of PLG is tightly regulated to prevent undesired fibrinolysis. Activation can occur through two main pathways: the tissue-type Plasminogen Activator (tPA)-dependent pathway and the urokinase-type Plasminogen Activator (uPA)-dependent pathway. In the tPA-dependent pathway, tPA binds to a specific receptor on the cell surface and catalyzes the conversion of PLG to Plasmin. The uPA-dependent pathway involves uPA binding to a receptor, followed by the activation of PLG. Additionally, various regulatory proteins, such as Plasminogen Activator Inhibitors (PAIs), control PLG activation by inhibiting the activity of tPA and uPA.

Customer Reviews (3)

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Reviews
06/12/2022

    The tightly sealed packaging of this protein reagent ensures optimal preservation of its activity.

    11/18/2021

      I highly recommend this reagent for its simplified experimental workflow, saving time and experimental costs.

      08/10/2019

        Catering to diverse experimental needs, its outstanding performance facilitates diversity in scientific research.

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