Abcam, ab177157, Anti-AHAS antibody [EPR12843]

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal AHAS antibody. Suitable for WB, Flow Cyt (Intra) and reacts with Human samples. Cited in 1 publication.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR12843,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:Flow Cyt (Intra), WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
Species reactivity
Mouse, Rat: We have preliminary internal testing data to indicate this antibody may not react with these species.
Please
contact us
for more information.
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purity-Tissue culture supernatant, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The acetohydroxyacid synthase (AHAS) also known as acetolactate synthase (ALS) is an enzyme that plays an important role in the biosynthesis of branched-chain amino acids. With a molecular mass of approximately 170 kDa AHAS catalyzes the first common step in the biosynthetic pathways of valine leucine and isoleucine. This enzyme is widely expressed in plants bacteria and fungi. AHAS is a holoenzyme that consists of a large catalytic subunit and a smaller regulatory subunit showing its complex structure and diverse regulatory control.
Biological function summary
AHAS facilitates the condensation of two pyruvate molecules to form acetolactate or a pyruvate and ketoisovalerate to form acetohydroxybutyrate. This condensation reaction is a critical step in the synthesis of all three branched-chain amino acids which are essential components for protein construction in various organisms. As a part of a multi-enzyme complex the activity of AHAS is also modulated by feedback mechanisms from the end products of its pathway ensuring the balance in amino acid production and cellular homeostasis.
Pathways
AHAS integrates into the branched-chain amino acid biosynthesis pathway directly taking its place at the start. This pathway connects to amino acid metabolism which is essential for protein synthesis. AHAS is intertwined with proteins like dihydroxyacid dehydratase and branched-chain aminotransferase which continue the pathway downstream. These interactions highlight AHAS's significance in creating amino acids necessary for organismal growth and development.
AHAS relates prominently to conditions involving imbalances in amino acid metabolism. Alterations in AHAS function can lead to metabolic disorders such as maple syrup urine disease although it primarily involves branched-chain alpha-keto acid dehydrogenase complex. In some cases herbicides target AHAS poisoning the mechanism in plants and disrupting their growth. Understanding the function of AHAS helps us to comprehend the architecture of metabolic diseases and assists in designing therapeutic approaches even though the direct connection with human metabolic disorders remains mainly indirect.