Recombinant Mouse AHCY Protein Pre-coupled Magnetic Beads

• Cat.No.: AHCY-403M-B
• Product Overview: The Recombnant protein was conjugated to magnetic beads. This ready-to-use, pre-coupled magnetic beads are in uniform particle size and narrow size distribution with large surface area, which is conducive to convenient and fast capture target molecules with high specificity and achieve magnetic separation. This product can be equipped with automation equipment for high-throughput operations.

Specification

• Source: HEK293
• Species: Mouse
• Form: Solution
• Particle size: ~2 μm
• Beads Surface: Hydrophilic
• Capacity: > 200 pmol rabbit IgG/ mg beads
• Applications: Immunoassay, In vitro diagnostics, cell sorting, Immunoprecipitation/Co-precipitation, Protein/antibody separation and purification.
• Stability: Stable for at least 6 months from the date of receipt of the product under proper storage and handling conditions.
• Storage: 2-8℃. Do not to freeze thaw the Beads
• Concentration: 10mg beads/mL
• Storage Buffer: PBS buffer

Gene Information

• Gene Name: Ahcy S-adenosylhomocysteine hydrolase [ Mus musculus ]
• Official Symbol: AHCY
• Gene ID: 269378
• mRNA Refseq: NM_016661.3
• Protein Refseq: NP_057870.3
• UniProt ID: P50247

Reviews

03/16/2022

My experiments have never been smoother since I started using this protein.

10/03/2021

In our scientific pursuits, this lab protein has surpassed expectations, demonstrating exceptional quality and ease of use.

01/04/2020

I highly recommend this protein to fellow researchers. It's a true gem!

07/11/2019

We wholeheartedly endorse the lab protein product for its outstanding performance and its significant contribution to our research outcomes.

12/31/2018

This protein is like a reliable teammate in the lab – always delivering excellent results.

Q&As

What is the significance of AHCY in maintaining cellular methylation homeostasis?

By degrading SAH, AHCY ensures the availability of S-adenosylmethionine (SAM), a universal methyl donor essential for DNA, RNA, and protein methylation reactions.

Explain the involvement of AHCY in the pathogenesis of liver diseases, such as non-alcoholic fatty liver disease (NAFLD).

Dysregulation of AHCY and altered methylation patterns have been linked to the development and progression of NAFLD and other liver pathologies.

How does AHCY catalyze the hydrolysis of S-adenosylhomocysteine?

AHCY employs a zinc-dependent mechanism to cleave the N-ribosidic bond of SAH, generating adenosine and homocysteine as products.

Describe the AHCY-related therapeutic approaches for diseases linked to aberrant methylation patterns.

Targeting AHCY activity or SAM availability holds promise as a potential therapeutic strategy for conditions influenced by disrupted methylation.

How do genetic variations in AHCY contribute to disease susceptibility?

Single nucleotide polymorphisms (SNPs) in the AHCY gene can affect enzyme activity and SAH levels, potentially influencing disease risk, including cardiovascular disorders and neurodegenerative diseases.

What are the metabolic fates of homocysteine generated by AHCY activity?

Homocysteine can be remethylated to methionine through the folate-dependent pathway or transsulfurated to cysteine via the transsulfuration pathway.

Discuss the crosstalk between AHCY and folate metabolism in one-carbon metabolism.

AHCY activity is intimately connected with folate-mediated one-carbon metabolism, affecting the availability of methyl groups for various methylation reactions.

How is AHCY expression regulated in response to cellular demands?

AHCY expression can be modulated by transcriptional factors and epigenetic modifications, responding to changes in cellular methylation needs.

How does AHCY interact with other cellular pathways, such as the polyamine biosynthesis pathway?

AHCY indirectly influences polyamine biosynthesis by providing the methyl groups required for polyamine synthesis.

Describe the structural features of AHCY that contribute to its catalytic efficiency.

AHCY possesses a TIM-barrel fold with an active site that houses the zinc ion critical for its hydrolytic activity.