Anti-SMOX (aa 46-144) polyclonal antibody

Name: Anti-SMOX (aa 46-144) polyclonal antibody
SKU: DPABH-03123
Rating: 5 (1 reviews)

Rabbit anti-Human SMOX (aa 46-144) polyclonal antibody for IHC-P, ICC/IF

COA

SDS

Datasheet

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Human

Immunogen

Recombinant fragment corresponding to amino acids 46-144 of Human Spermine oxidase (Q9NWM0).

Conjugate

Unconjugated

Applications

Application Notes

IHC-P: 1/50 - 1/200; ICC/IF: 1 - 4 μg/ml;

Target

Alternative Names

SMOX; spermine oxidase; PAO; SMO; PAO-1; PAOH1; C20orf16; polyamine oxidase 1; flavin containing amine oxidase; flavin-containing spermine oxidase; putative cyclin G1 interacting protein;

Entrez Gene ID

54498

UniProt ID

Q9NWM0

Product Background

Antigen Description

Polyamines are ubiquitous polycationic alkylamines which include spermine, spermidine, putrescine, and agmatine. These molecules participate in a broad range of cellular functions which include cell cycle modulation, scavenging reactive oxygen species, and the control of gene expression. These molecules also play important roles in neurotransmission through their regulation of cell-surface receptor activity, involvement in intracellular signalling pathways, and their putative roles as neurotransmitters. This gene encodes an FAD-containing enzyme that catalyzes the oxidation of spermine to spermadine and secondarily produces hydrogen peroxide. Multiple transcript variants encoding different isoenzymes have been identified for this gene, some of which have failed to demonstrate significant oxidase activity on natural polyamine substrates. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism.

Pathway

Amine Oxidase reactions; Arginine and proline metabolism; Interconversion of polyamines; Metabolism of amino acids and derivatives

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Pharmacological Inhibition of Spermine Oxidase Reduces Neurodegeneration and Improves Retinal Function in Diabetic Mice

JOURNAL OF CLINICAL MEDICINE

Authors: Liu, Fang; Saul, Alan B.; Pichavaram, Prahalathan; Xu, Zhimin; Rudraraju, Madhuri; Somanath, Payaningal R.; Smith, Sylvia B.; Caldwell, Ruth B.; Narayanan, S. Priya

Abstract

Diabetic retinopathy (DR) is a significant cause of blindness in working-age adults worldwide. Lack of effective strategies to prevent or reduce vision loss is a major problem. Since the degeneration of retinal neurons is an early event in the diabetic retina, studies to characterize the molecular mechanisms of diabetes-induced retinal neuronal damage and dysfunction are of high significance. We have demonstrated that spermine oxidase (SMOX), a mediator of polyamine oxidation is critically involved in causing neurovascular damage in the retina. The involvement of SMOX in diabetes-induced retinal neuronal damage is completely unknown. Utilizing the streptozotocin-induced mouse model of diabetes, the impact of the SMOX inhibitor, MDL 72527, on neuronal damage and dysfunction in the diabetic retina was investigated. Retinal function was assessed by electroretinography (ERG) and retinal architecture was evaluated using spectral domain-optical coherence tomography. Retinal cryosections were prepared for immunolabeling of inner retinal neurons and retinal lysates were used for Western blotting. We observed a marked decrease in retinal function in diabetic mice compared to the non-diabetic controls. Treatment with MDL 72527 significantly improved the ERG responses in diabetic retinas. Diabetes-induced retinal thinning was also inhibited by the MDL 72527 treatment. Our analysis further showed that diabetes-induced retinal ganglion cell damage and neurodegeneration were markedly attenuated by MDL 72527 treatment. These results strongly implicate SMOX in diabetes-induced retinal neurodegeneration and visual dysfunction.

Preparation and properties of the SmOx/Rh(100) model surface

CHINESE SCIENCE BULLETIN

Authors: Ma, YS; Zhu, JF; Zhuang, SX; Jiang, ZQ; Zhou, WP; Zhai, RS; Bao, XH

Abstract

The preparation of SmOx/Rh(100) and CO adsorption on this model surface have been investigated with Auger electron spectroscopy (AES), X-ray photoelectron spectroscopy (XPS) and temperature programmed desorption spectroscopy (TDS). The oxygen adsorption on the SmRh alloy surface leads to the aggregation of Sm on the surface. The thermal treatment of this oxidized surface induces the further agglomeration of SmOx on the Rh(100) surface. Compared with CO TDS on the clean Rh(100) surface, three additional CO desorption peaks can be observed at 176, 331 and 600 K on the SmOx/Rh(100) surface. The CO desorption peak at 176 K may originate from CO adsorbed on SmOx islands, while the appearance of the CO adsorption peaks at 331 and 600 K, depending on the oxidation state of Sm, is attributed to CO species located at the interface of SmOx/Rh(100).