Recombinant Rat Plg protein, His & GST-tagged

• Cat.No.: Plg-6730R
• Product Overview: Recombinant Rat Plg aa. (Leu100~Gly434 (Accession # Q01177)) fused with N-terminal His & GST tag was produced in E. coli cells.

Specification

• Source: E. coli
• Species: Rat
• Tag: His&GST
• Form: Freeze-dried powder
• Molecular Mass: Predicted Molecular Mass: 67.9kDa.
• Protein length: Leu100~Gly434
• Endotoxin: <1.0EU per 1ug (determined by the LAL method)
• Purity: >95%
• Characteristic: The isoelectric point is 6.
• Applications: SDS-PAGE; WB; ELISA; IP.
• Stability: The thermal stability is described by the loss rate of the target protein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37°C for 48h, and no obvious degradation and precipitation were observed. (Referring from China Biological Products Standard, which was calculated by the Arrhenius equation.) The loss of this protein is less than 5% within the expiration date under appropriate storage condition.
• Storage: Avoid repeated freeze/thaw cycles. Store at 2-8°C for one month. Aliquot and store at -80°C for 12 months.
• Storage buffer: Supplied as lyophilized form in PBS, pH7.4, containing 5% trehalose, 0.01% sarcosyl.
• Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.

Gene Information

• Gene Name: Plg plasminogen [ Rattus norvegicus (Norway rat) ]
• Official Symbol: Plg
• Synonyms: Ab1-346; plasminogen
• Gene ID: 85253
• mRNA Refseq: NM_053491.2
• Protein Refseq: NP_445943.1
• UniProt ID: Q01177

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.

Q&As

What is the clinical significance of PLG as a diagnostic or prognostic biomarker?

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?

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?

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?

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?

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?

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?

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.