S-Adenosylhomocysteine (SAH) ELISA Kit

Name: S-Adenosylhomocysteine (SAH) ELISA Kit
SKU: DEIA-FN1319
Rating: 5 (1 reviews)

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

COA

SDS

Datasheet

Summary

Sample

plasma, serum, lysates or other biological fluid samples

Detection Method

cELISA

Intended Use

CD SAH ELISA Kit is a competitive enzyme immunoassay developed for the detection and quantitation of SAH in plasma, serum, lysates or other biological fluid samples. The kit has a detection sensitivity limit of 0.2 μM free SAH. Each kit provides sufficient reagents to perform up to 96 assays including standard curve and unknown samples.

Contents of Kit

Box 1 (shipped at room temperature)
1. 96 Well Protein Binding Plate: One strip well 96 well plate.
2. Secondary Antibody, HRP Conjugate (1000×): One 20 μL vial.
3. Assay Diluent: One 50 mL bottle.
4. 10× Wash Buffer: One 100 mL bottle.
5. Substrate Solution: One 12 mL amber bottle.
6. Stop Solution: One 12 mL bottle.
Box 2 (shipped on dry ice)
1. SAH Conjugate (1000×): One 20 μL vial.
2. SAH Standard: One 20 μL vial of 1.25 mM free s-adenosylhomocysteine.
3. Anti-SAH Antibody (500×): One 15 μL vial.

Storage

Upon receipt, store SAH Conjugate and SAH Standard at -80°C. Store the rest of the kit at 4°C

General Description

S-adenosylmethionine (SAM) is a methyl donor involved in the transfer of a methyl group to DNA, proteins, phospholipids, RNA, and neurotransmitters. Reactions that break down and regenerate SAM have been named the SAM cycle (Figure 1). SAM-dependent methylases use SAM as a substrate to yield S-adenosylhomocysteine (SAH), which is further broken down to homocysteine and adenosine by s-adenosylhomocysteine hydrolase. The homocysteine can be regenerated to methionine and finally SAM by methionine synthases.
Donation of the SAM methyl group converts SAM into SAH, the latter being a potent inhibitor of methylation. For this reason, the SAM/SAH ratio has been used as an index of methylation potential in a cell. SAH in plasma has been found to be a more sensitive indicator for vascular disease risk than homocysteine. In addition, distinct classes of riboswitches that recognize SAH but not SAM and regulate gene expression have been discovered.

Figure 1. The SAM cycle.

Standard Curve

The following figures demonstrate typical SAH ELISA Kit results. One should use the data below for reference only. This data should not be used to interpret actual results.

Figure 2: SAH Standard Curve.

Figure 3: SAH Detection in Human Serum and Plasma.

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Alzheimer's disease pathogenesis: Is there a role for folate?

MECHANISMS OF AGEING AND DEVELOPMENT

Authors: Robinson, Natassia; Grabowski, Peter; Rehman, Ishtiaq

Abstract

Epigenetic modifications, including changes in DNA methylation, have been implicated in a wide range of diseases including neurological diseases such as Alzheimer's. The role of dietary folate in providing methyl groups required for maintenance and modulation of DNA methylation makes it a nutrient of interest in Alzheimer's. Late onset Alzheimer's disease is the most common form of dementia and at present its aetiology is largely undetermined. From epidemiological studies, the interactions between folate, B-vitamins and homocysteine as well as the long latency period has led to difficulties in interpretation of the data, thus current evidence exploring the role of dietary folate in Alzheimer's is contradictory and unresolved. Therefore, examining the effects at a molecular level and exploring potential epigenetic mechanisms could increase our understanding of the disease and aetiology. The aim of this review is to examine the role that folate could play in Alzheimer's disease neuropathology and will focus on the effects of folate on DNA methylation which link to disease pathology, initiation and progression.

Targeting Cystathionine Beta-Synthase Misfolding in Homocystinuria by Small Ligands: State of the Art and Future Directions

CURRENT DRUG TARGETS

Authors: Majtan, Tomas; Pey, Angel L.; Ereno-Orbea, June; Alfonso Martinez-Cruz, Luis; Kraus, Jan P.

Abstract

Classical homocystinuria (HCU) is the most common loss-of-function inborn error of sulfur amino acids metabolism. HCU is caused by a deficiency in enzymatic degradation of homocysteine, a toxic intermediate of methionine transformation to cysteine, chiefly due to missense mutations in the cystathionine beta-synthase (CBS) gene. As with many other inherited disorders, the pathogenic mutations do not target key catalytic residues, but rather introduce structural perturbations leading to an enhanced tendency of the mutant CBS to misfold and either to form non-functional aggregates or to undergo proteasome-dependent degradation. Thus correction of CBS misfolding represents an alternative therapeutic approach for HCU. In this review, we summarize the complex nature of CBS, its multidomain architecture, the interplay between the three cofactors required for CBS function (heme, pyridoxal- 5'-phosphate (PLP) and S-adenosyl-L-methionine) as well as the intricate allosteric regulatory mechanism only recently explained thanks to advances in CBS crystallography. While roughly half of the patients responds to treatment with a PLP precursor pyridoxine, many studies suggested usefulness of small chemicals, such as chemical and pharmacological chaperones or proteasome inhibitors, rescuing mutant CBS activity in cellular and animal models of HCU. Non-specific chemical chaperones and proteasome inhibitors assist in mutant CBS folding process and/or prevent its rapid degradation, thus resulting in increased steady state levels of the enzyme and CBS activity. Recent increased interest in the field and available structural information will hopefully yield CBS-specific compounds by using high-throughput screening and computational modeling of novel ligands improving folding, stability and activity of CBS.