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BRAND / VENDOR: Abcam

Abcam, ab172608, Anti-hnRNP U/p120 antibody [EPR12279]

CATALOG NUMBER: ab172608
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Product Description

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal hnRNP U/p120 antibody. Suitable for IHC-P, WB, ICC/IF and reacts with Human samples. Cited in 3 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR12279,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:IHC-P, 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:
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.
Heterogeneous nuclear ribonucleoprotein U (hnRNP U) also known as p120 is a multifunctional protein involved in various cellular processes. This protein has an approximate molecular mass of 120 kDa. It is expressed widely in different tissues predominantly within the nuclear compartment of cells. HnRNP U functions mainly in relation to RNA binding and regulation including alternative splicing RNA stability and RNA transport. Its ability to interact with both RNA and DNA attributes to a role in chromatin structure regulation and transcriptional control.
Biological function summary
HnRNP U plays a significant role in organizing chromatin architecture and facilitating transcription regulation. It often associates with other hnRNPs to form ribonucleoprotein complexes which are central in RNA metabolism. Importantly hnRNP U's capacity to interact with chromatin allows it to participate in chromatin remodeling which is necessary for processes such as embryonic development and cellular differentiation. It modifies the transcriptional landscape by influencing the accessibility of transcription factors to their DNA targets.
Pathways
HnRNP U integrates into pathways controlling gene expression and RNA processing. It is notably involved in pathways such as signal transduction and DNA damage response. This protein associates with the transcription machinery influencing the expression of genes responsive to cellular stress and proliferation signals. It interacts with proteins like p53 in the DNA damage response pathway which suggests a role in maintaining genomic stability by coordinating chromatin remodeling and transcription in response to stress.
HnRNP U connects with pathological conditions such as cancer and neurodegenerative diseases. Its altered expression or mutation can disrupt chromatin structure leading to abnormal gene expression patterns. In cancer hnRNP U correlates with aberrant signaling pathways and may interact with oncoproteins driving tumor progression. In neurodegenerative disorders its association with RNA-binding proteins like TDP-43 suggests a role in the misregulation of RNA processing events contributing to neuronal dysfunction. Understanding hnRNP U's diverse functions helps clarify its potential as a therapeutic target.


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Collaboration

Tony Tang

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