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BRAND / VENDOR: Abcam

Abcam, ab174855, Anti-UAP1L1 antibody [EPR11586]

CATALOG NUMBER: ab174855
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Product Description

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal UAP1L1 antibody. Suitable for WB, ICC/IF, Flow Cyt (Intra) and reacts with Human samples. Cited in 2 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR11586,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:Flow Cyt (Intra), WB, ICC/IFSee 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 target UAP1L1 also known as UDP-N-acetylglucosamine pyrophosphorylase 2 or AGX2 is an enzyme with a molecular weight of approximately 63 kDa. This enzyme is responsible for catalyzing the conversion of UTP and N-acetylglucosamine-1-phosphate to UDP-N-acetylglucosamine an essential precursor for glycosylation processes. UAP1L1 expression occurs in various tissues including the liver and skeletal muscle but it is notably higher in testis tissue. Its activity impacts the synthesis of N-glycans and glycolipids important components of cellular membranes.
Biological function summary
UAP1L1 plays a significant role in cellular glycosylation. This process involves the addition of sugar moieties to proteins and lipids which is vital for proper folding stability and function of glycoproteins. UAP1L1 is not part of any known large enzyme complexes but it cooperates closely with other metabolic enzymes to maintain the pool of UDP-GlcNAc a high-energy substrate used in various biosynthetic pathways. It influences cellular homeostasis by regulating glycan biosynthesis.
Pathways
UAP1L1 is integral to the hexosamine biosynthetic pathway and the UDP-N-acetylglucosamine biosynthesis pathway. Through its enzymatic activity it contributes to maintaining cellular UDP-GlcNAc levels which correlate with key biosynthetic and signaling pathways including O-GlcNAcylation. UAP1L1 interacts with other enzymes like GFAT and OGT in these pathways highlighting its interconnected role in cellular metabolism growth and signaling.
Abnormal UAP1L1 function shows associations with metabolic and developmental disorders. Anomalies in hexosamine metabolism where UAP1L1 activity is important can lead to insulin resistance and contribute to the pathogenesis of type 2 diabetes. Alterations in glycosylation where UAP1L1 is a foundational player may also feature in congenital disorders of glycosylation. Proteins like OGT linked through pathways involving UAP1L1 dysregulation also relate to these diseases illustrating the interconnected nature of metabolic and glycosylation pathways in disease contexts.


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Collaboration

Tony Tang

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