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AB241043

Cystathionine beta Synthase Assay Kit

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(1 Publication)

Cystathionine beta Synthase Assay Kit (ab241043) uses cysteine and homocysteine as substrates to produce H2S.

Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
3 Images
Functional Studies - Cystathionine beta Synthase Assay Kit (AB241043)
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Functional Studies - Cystathionine beta Synthase Assay Kit (AB241043)

CβS specific activity.

CβS specific activity in HepG2 cell lysate and Liver lysate. Assays were performed following the kit protocol.

Functional Studies - Cystathionine beta Synthase Assay Kit (AB241043)
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Functional Studies - Cystathionine beta Synthase Assay Kit (AB241043)

CβS Standard Curve.

CβS Standard Curve.

Functional Studies - Cystathionine beta Synthase Assay Kit (AB241043)
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Functional Studies - Cystathionine beta Synthase Assay Kit (AB241043)

CβS activity in Liver Lysate.

CβS activity in Liver Lysate (20 μg) & Positive Control (1.5 μg).

Key facts

Detection method

Fluorescent

Sample types

Tissue, Suspension cells, Cell culture supernatant, Adherent cells

Assay Platform

Microplate reader

Reactivity data

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Product details

Cystathionine beta Synthase Assay Kit (ab241043) utilizes cysteine and homocysteine as substrates to produce H2S. Hydrogen sulfide reacts with the azido-functional group of the fluorescent probe yielding a fluorescent amino group (Ex/Em = 368/460 nm). The assay is highly sensitive, has a simple easy-to-follow protocol, and can detect as low as 1.45 mU of CBetaS activity.

Other Notes
This product was previously called K998 Biovision Cystathionine Synthase Activity Assay Kit (Fluorometric). Biovision was acquired by Abcam in 2021.

The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

What's included?

{ "values": { "100Test": { "sellingSize": "100 Test", "publicAssetCode":"ab241043-100Test", "assetComponentDetails": [ { "size":"1 x 500 µL", "name":"SAM Cofactor", "number":"AB241043-CMP03", "productcode":"" }, { "size":"1 x 1 Vial", "name":"Reducing Agent I", "number":"AB241043-CMP08", "productcode":"" }, { "size":"1 x 0.5 mL", "name":"H2S Probe", "number":"AB241043-CMP06", "productcode":"" }, { "size":"1 x 4 mL", "name":"CβS Substrate", "number":"AB241043-CMP07", "productcode":"" }, { "size":"1 x 50 µL", "name":"CβS Positive Control", "number":"AB241043-CMP05", "productcode":"" }, { "size":"1 x 25 mL", "name":"CβS Assay Buffer", "number":"AB241043-CMP04", "productcode":"" }, { "size":"1 x 0.5 mL", "name":"Cofactor 1", "number":"AB241043-CMP02", "productcode":"" }, { "size":"1 x 100 µL", "name":"AMC Standard", "number":"AB241043-CMP01", "productcode":"" } ] } } }

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Please refer to protocols

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Cystathionine beta-synthase (CBS) is an enzyme that catalyzes the conversion of homocysteine and serine into cystathionine. It is sometimes referred to as CBS monelyne or cystathionine synthase. CBS is a heme-containing protein with a molecular mass of approximately 63 kDa. It is expressed widely in tissues including the liver brain and kidney. The activity of CBS is regulated by various factors including the availability of cofactors like pyridoxal 5'-phosphate and adenosine triphosphate (ATP).
Biological function summary

The enzyme CBS plays a role in the transsulfuration pathway where it helps in the metabolism of homocysteine. CBS is a part of a larger complex in some tissues where it interacts with other enzymes involved in sulfur amino acid metabolism. This function is important in maintaining cellular sulfur amino acid balance and protecting cells from oxidative stress caused by elevated levels of homocysteine.

Pathways

CBS functions in the transsulfuration pathway which connects the methionine cycle and the synthesis of glutathione. This pathway is essential for detoxification and antioxidant protection. CBS interrelates with other proteins like cystathionine gamma-lyase (CGL) within this pathway. The interplay between CBS and CGL ensures the conversion of homocysteine to cysteine which is a precursor for the synthesis of glutathione.

CBS deficiency is linked to homocystinuria a disorder characterized by high levels of homocysteine in the blood and urine. Symptoms include cardiovascular problems and developmental delays. Furthermore alterations in CBS activity relate to cardiovascular diseases due to hyperhomocysteinemia. Within these conditions CBS interacts with other proteins involved in homocysteine metabolism such as methionine synthase which also contributes to the complexity of these disorders.

Product protocols

Target data

Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (PubMed : 20506325, PubMed : 23974653, PubMed : 23981774). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity).
See full target information CBS

Alternative Names

Cystathionine beta-synthase, Beta-thionase, Serine sulfhydrase, CBS

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

The Journal of nutrition 151:1407-1415 PubMed33758914

2021

Letrozole-Induced Polycystic Ovary Syndrome Attenuates Cystathionine-β Synthase mRNA and Protein Abundance in the Ovaries of Female Sprague Dawley Rats.

Applications

Unspecified application

Species

Unspecified reactive species

Amanda E Bries,Joseph L Webb,Brooke Vogel,Claudia Carrillo,Aileen F Keating,Samantha K Pritchard,Gina Roslan,Joshua W Miller,Kevin L Schalinske
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