GLRX2 Antibodies

Glutaredoxin-2, mitochondrial (GLRX2)

Glutathione-dependent oxidoreductase that eases the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis due to oxidative stress.

Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions.

Gene Information

Human
Gene Name:	GLRX2
Uniprot:	Q9NS18
Entrez:	51022

Family

Belongs to:
glutaredoxin family

Alternative Names

bA101E13.1 (GRX2 glutaredoxin (thioltransferase) 2); glutaredoxin 2; glutaredoxin-2, mitochondrial; GRX2bA101E13.1

Molecular Weight

Mass (kDA):
18.052 kDA

Genomic Context

Human
Location:	1q31.2
Sequence:	1; NC_000001.11 (193096465..193106114, complement)

Tissue Specificity

Widely expressed. Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta and lung. Not expressed in peripheral blood leukocytes.

Subcellular Localizations

[Isoform 1]: Mitochondrion.; [Isoform 2]: Nucleus.

Diseases

• Neoplasms
• Parkinson Disease
• Ischemia
• Heart Diseases
• Adenoma
• Brain Ischemia
• Melanoma
• Radiation Injuries, Experimental
• Spermatogenesis Arrest
• Parathyroid Neoplasms
• Testicular Injury
• Lung Diseases
• Carcinoma

• Lung Diseases, Interstitial
• Tumor Suppressor Gene Inactivation Process
• Usual Interstitial Pneumonitis
• Extrinsic Allergic Alveolitis
• Pituitary Diseases
• Sarcoidosis
• Mammary Neoplasms

Pathways

• Localization
• Cell Death
• Cell Proliferation
• Protein Deglutathionylation
• Mitochondrial Translocation
• Secretion
• Regulation Of Cell Death
• Response To Superoxide
• Osteoclast Differentiation
• Induction Of Apoptosis
• Insulin Secretion
• Brain Development
• Spermatogenesis

• Response To Oxidative Stress
• Oocyte Development
• Translation
• Cell Differentiation
• Iron-sulfur Cluster Assembly
• Exocytosis
• Excretion

PTMs

• Reduction
• Glutathionylation
• Oxidation

• Phosphorylation
• Deglutathionylation
• Nitrosylation

Research Areas

• Apoptosis

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/GLRX2

Boster Bio - Best Uses Of The GLRX2 Marker

This article will discuss Boster Bio's Anti-Glutaredoxin 2 marker. We'll talk about its advantages in terms of optimization, as well as troubleshooting. This guide will provide you with important information to optimize your experiments, improve your results, and make your life easier. Each researcher encounters problems and errors during their experiments. These troubleshooting guides can help identify and eliminate common sources.

Boster Bio

There are many ways you can use the GLRX2 marker in your research. It can be used to identify cell death and determine the state of the cells. The kit comes with a range of markers, including b-actin DCF-DA and cytochrome c as well as a-IREB2 and TUNEL. These markers were specifically designed for this purpose and are widely available.

Anti-Glutaredoxin 2/GLRX2 Marker

The GLRX2 marker is a glutathione-dependent hydrogen donor that regulates cellular redox processes. It also serves as a monothiol catalyst that is efficient and aids in controlling the production of superoxide by complex I. When glutathione levels are increased, they are reduced and the loss cardiolipin and cytochroma is halted. It is part of the glutaredoxin family. There are two types.

Boster Bio's Anti-Glutaredoxin GLRX2 marker can be used to detect a protein that binds to GLRX. The antibody reacts with GLRX2 in various biological specimens like human cells, mice rats, mice, and rats. It is also used for immunohistochemistry and is available for purchase at tebu-bio.

Optimization

The GLRX2 isoforms are two of the most well-known thiol-disulfide oxidereduct (TDOs). They are composed of an N-terminal homology domain as well tandem repeats of glutaredoxin-related domains, which protect cells from oxidative stress and apoptosis. GLRX2 is a crucial protein in cell and tissue metabolism, and plays a significant part in the synthesis of antioxidants.

Applications

The GLRX2 marker has recently been used to assess gene expression. Its main function is to measure the levels of glutaredoxin-1, serine/threonine kinase that regulates mitogen-activated and apoptotic protein kinase signaling. Its higher levels of expression have been associated with a lower risk of stroke in a rodent model, and may have a positive effect on the treatment of neuronal disorders.

The PEP-1GLRX1 protein is a defense against the death of cells caused by oxidative stress. It was expressed in the HT-22 cells which had been treated with hydrogen peroxide. The cells were incubated for one to five hours. The viability of the cell was determined by using MTT (methylene blue dye) and DCF-DA staining. Images were taken with an Eclipse microscope from Nikon. Cell viability was determined as a percentage of the untreated control cells.

The PEP-1-GLRX1 protein was produced by using plasmids that are cell-permeable. The transformed bacterial cells were cultured in lysogeny broth media at 37degC and induced by 0.5 mM isopropyl b-D-1-thiogalactopyranoside for 6 h. The harvested cells were then lysed and subjected to PD-10 column chromatography to measure protein levels.

Microglia activation is one of the major causes of degenerative brain diseases and has been utilized as a marker of ischemic neuronal damage. GFAP is a marker for astrocytes is produced by activated microglia. The PEP-1GLRX1 protein reduced levels of both GFAP and Iba-1 immunoreactive cells in mice, in contrast to the vehicle-treated group.

Since oxidative stress is a primary risk factor for neuronal diseases studies using the PEP-1GLRX1 protein to monitor brain ischemia have shown that the PEP-1GLRX1 protein transduced improves the viability of the HT-22 cells under stress of oxidative. Transduced PEP-1-GLRX1 significantly reduced intracellular ROS levels and DNA damage.