ALR Polyclonal Antibody
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- 背景知识
Application ![]()
| WB, IHC-P |
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Primary Accession | P55789 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 23449 Da |
Gene ID | 2671 |
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Other Names | GFER; ALR; HERV1; HPO; FAD-linked sulfhydryl oxidase ALR; Augmenter of liver regeneration; hERV1; Hepatopoietin |
Dilution | WB~~Western Blot: 1/500 - 1/2000. IHC-p: 1:100-1:300. ELISA: 1/20000. Not yet tested in other applications. IHC-P~~Western Blot: 1/500 - 1/2000. IHC-p: 1:100-1:300. ELISA: 1/20000. Not yet tested in other applications. |
Format | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.09% (W/V) sodium azide. |
Storage Conditions | -20℃ |
Name | GFER |
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Synonyms | ALR, HERV1, HPO |
Function | [Isoform 1]: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. |
Cellular Location | [Isoform 1]: Mitochondrion intermembrane space. Mitochondrion |
Tissue Location | Ubiquitously expressed. Highest expression in the testis and liver and low expression in the muscle |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re- oxidized by donating electrons to cytochrome c or molecular oxygen.

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