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BRAND / VENDOR: Abcam

Abcam, ab249915, Anti-UBLCP1 antibody [EPR11923] - BSA and Azide free

CATALOG NUMBER: ab249915
Regular price$0.99
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Product Description

Size: 100µg / 1mg
Rabbit Recombinant Monoclonal UBLCP1 antibody. Carrier free. Suitable for ICC/IF, IP, WB and reacts with Human samples. Cited in 1 publication.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR11923,
Isotype:IgG,
Carrier free:Yes,
Reacts with:Human,
Applications:WB, IP, 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:
ab249915 is the carrier-free version of
ab176340
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.
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification, Storage buffer-pH: 7.2 - 7.4Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-Do Not Freeze

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
UBLCP1 also known as Ubiquitin-Like Domain Containing CTD Phosphatase 1 is a phosphatase that primarily functions in dephosphorylation of substrate proteins. This protein has a molecular mass of approximately 44 kDa and is expressed in various human tissues but shows higher levels in the brain and skeletal muscle. UBLCP1 contains ubiquitin-like domains which indicate its potential interactions with other molecules containing ubiquitin or ubiquitin-like proteins influencing its mechanical roles inside cells.
Biological function summary
UBLCP1 plays a significant role in regulating cellular processes by removing phosphate groups from substrates which can affect protein activity cellular localization or interaction with other proteins. It does not work alone but associates with other molecules to form complexes that allow it to control different cellular processes effectively. One such interaction is with the RNA polymerase II where UBLCP1 may regulate transcription by dephosphorylating the C-terminal domain of RNA polymerase II.
Pathways
Several studies have linked UBLCP1 to key signaling pathways that control cell cycle and transcription regulation. It interacts with pathways involving RNA polymerase II influencing its activity during transcription. Additionally UBLCP1 shares interactions with components of the TGF-beta pathway though details of this relationship require further study. This connection could suggest a role in controlling growth and differentiation signals in cells.
Researchers associate UBLCP1 with neurodegenerative diseases including Alzheimer's disease given its higher expression in brain tissues and involvement in transcriptional regulation. Perturbations in UBLCP1's activity could affect proteins related to synaptic function and memory. Moreover UBLCP1 interaction with proteins like RNA polymerase II indicates that it may influence diseases where transcription is disrupted such as certain cancers. Further understanding of its mechanistic role could provide insights into novel therapeutic strategies.


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Collaboration

Tony Tang

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