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Anti-Glutathione Peroxidase 4/GPX4 Antibody Picoband™ (monoclonal, 6I4E7)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, FC |
|---|---|
| Primary Accession | P36969 |
| Host | Mouse |
| Isotype | Mouse IgG2b |
| Reactivity | Human |
| Clonality | Monoclonal |
| Format | Lyophilized |
| Description | Anti-Glutathione Peroxidase 4/GPX4 Antibody Picoband™ (monoclonal, 6I4E7) . Tested in Flow Cytometry, WB applications. This antibody reacts with Human. |
| Reconstitution | Adding 0.2 ml of distilled water will yield a concentration of 500 µg/ml. |
| Gene ID | 2879 |
|---|---|
| Other Names | Phospholipid hydroperoxide glutathione peroxidase GPX4, PHGPx, 1.11.1.12, Glutathione peroxidase 4, GPx-4, GSHPx-4, 1.11.1.9, GPX4 {ECO:0000303|PubMed:9705830, ECO:0000312|HGNC:HGNC:4556} |
| Calculated MW | 19 kDa |
| Application Details | Western blot, 0.25-0.5 µg/ml, Human Flow Cytometry, 1-3 µg/1x10^6 cells, Human |
| Contents | Each vial contains 4 mg Trehalose, 0.9 mg NaCl and 0.2 mg Na2HPO4. |
| Clone Names | Clone: 6I4E7 |
| Immunogen | E.coli-derived human Glutathione Peroxidase 4/GPX4 recombinant protein (Position: A30-F197). |
| Purification | Immunogen affinity purified. |
| Storage | At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing. |
| Name | GPX4 {ECO:0000303|PubMed:9705830, ECO:0000312|HGNC:HGNC:4556} |
|---|---|
| Function | Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (By similarity). Can also reduce cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (By similarity). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron- dependent accumulation of lipid reactive oxygen species (PubMed:24439385). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (By similarity). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (By similarity). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (By similarity). Required for normal sperm development and male fertility (By similarity). Essential for maturation and survival of photoreceptor cells (By similarity). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (By similarity). Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (PubMed:11115402). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down- regulator of the cellular 15-lipoxygenase pathway (By similarity). Can reduce fatty acid-derived hydroperoxides (PubMed:11115402, PubMed:36608588). Can also reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide (PubMed:17630701, PubMed:36608588). |
| Cellular Location | [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:O70325} |
| Tissue Location | Present primarily in testis. Expressed in platelets (at protein level) (PubMed:11115402). |
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Provided below are standard protocols that you may find useful for product applications.
Background
Glutathione peroxidase 4, also known as GPX4, is an enzyme that in humans is encoded by the GPX4 gene. This gene encodes a member of the glutathione peroxidase protein family. Glutathione peroxidase catalyzes the reduction of hydrogen peroxide, organic hydroperoxide, and lipid peroxides by reduced glutathione and functions in the protection of cells against oxidative damage. Human plasma glutathione peroxidase has been shown to be a selenium-containing enzyme and the UGA codon is translated into a selenocysteine. The encoded protein has been identified as a moonlighting protein based on its ability to serve dual functions as a peroxidase as well as a structural protein in mature spermatozoa. Through alternative splicing and transcription initiation, rat produces proteins that localize to the nucleus, mitochondrion, and cytoplasm. In humans, alternative transcription initiation and the cleavage sites of the mitochondrial and nuclear transit peptides need to be experimentally verified. Alternative splicing results in multiple transcript variants.
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