Murine Plasminogen Matched Antibody Pair

Name: Murine Plasminogen Matched Antibody Pair
SKU: ABPR-L032
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Sample

Plasma

Species Reactivity

Murine

Detection Method

Sandwich ELISA

Intended Use

This antibody pair set comes with matched antibody pair to detect and quantify protein level of Murine PLG

Contents of Kit

1. Capture Antibody (yellow): 0.4 ml of polyclonal affinity-purified anti-Pg antibody for coating plates.
2. Detecting Antibody (red): 0.4 ml of affinity-purified peroxidase conjugated polyclonal anti-Pg antibody for detection of captured Pg.
Note: Reagents are sufficient for at least 4×96 well plates using recommended protocols. Antibodies are supplied in a 50% (v/v) glycerol solution for storage at –10 to -20°C. Keep vials tightly capped. Do not store in frost-free freezers.

Storage

-10 to -20°C

General Description

Plasminogen (Pg) is synthesized in the liver and circulates in plasma at a concentration of ~200 μg/ml (~2.3 μM). Plasminogen is a single-chain glycoprotein of ~88 kDa that consists of a catalytic domain followed by five kringle structures. Within these kringle structures are four low-affinity lysine binding sites and one high-affinity lysine binding site. It is through these lysine binding sites that plasminogen binds to fibrin and to α2 Antiplasmin. Native plasminogen (glu-plasminogen) exists in two variants that differ in their extent of glycosylation, and each variant has up to six isoelectric forms with respect to sialic acid content, for a total of 12 molecular forms. Activation of glu-plasminogen by the plasminogen activators urokinase (UPA), or tissue plasminogen activator (tPA) occurs by cleavage after residue Arg560 to produce the two-chain active serine protease plasmin. In a positive feedback reaction, the plasmin generated cleaves an ~8 kDa peptide from glu-plasminogen, producing lys77-plasminogen which has a higher affinity for fibrin and when bound is a preferred substrate for plasminogen activators such as urokinase. Additional activators of plasminogen include kallikrein and activated factor XII. The primary inhibitor of plasmin in plasma is α2 Antiplasmin. Other physiological inhibitors of plasmin include α2 macroglobulin and antithrombin.

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Documents

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References

Large-scale identification of functional microRNA targeting reveals cooperative regulation of the hemostatic system

JOURNAL OF THROMBOSIS AND HAEMOSTASIS

Authors: Nourse, J.; Braun, J.; Lackner, K.; Huettelmaier, S.; Danckwardt, S.

Abstract

Background: microRNAs (miRNAs) confer robustness to complex molecular networks regulating biological functions. However, despite the involvement of miRNAs in almost all biological processes, and the importance of the hemostatic system for a multitude of actions in and beyond blood coagulation, the role of miRNAs in hemostasis is poorly defined. Objectives: Here we comprehensively illuminate miRNA-mediated regulation of the hemostatic system in an unbiased manner. Methods: In contrast to widely applied association studies, we used an integrative screening approach that combines functional aspects of miRNA silencing with biophysical miRNA interaction based on RNA pull-downs (miTRAP) coupled to next-generation sequencing. Results: Examination of a panel of 27 hemostasis-associated gene 3'UTRs revealed the majority to possess substantial Dicer-dependent silencing capability, suggesting functional miRNA targeting. miTRAP revealed 150 specific miRNA interactions with 14 3'UTRs, of which 52, involving 40 miRNAs, were functionally confirmed. This includes cooperative miRNA regulation of key hemostatic genes comprising procoagulant (F7, F8, F11, FGA, FGG and KLKB1) and anticoagulant (SERPINA10, PROZ, SERPIND1 and SERPINC1) as well as fibrinolytic (PLG) components. Bioinformatic analysis of miRNA functionality reveals established and potential novel links between the hemostatic system and other pathologies, such as cancer, bone metabolism and renal function. Conclusions: Our findings provide, along with an in-vivo proof of concept, deep insights into the network of miRNAs regulating the hemostatic system and present a foundation for biomarker discovery and novel targeted therapeutics for correction of de-regulated hemostasis and associated processes in the future. A repository of the miRNA targetome covering 14 hemostatic components is provided.

Plasminogen and the Plasminogen receptor, Plg-R-KT, regulate efferocytosis and macrophage reprogramming

FASEB JOURNAL

Authors: Vago, Juliana Priscila; Sugimoto, Michelle Amantea; Baik, Nagyung; Parmer, Robert J.; Miles, Lindsey A.; Sousa, Lirlandia Pires

Abstract