Rabbit Recombinant Multiclonal RPS27A antibody. Suitable for ICC, ChIP, WB and reacts with Human samples. Immunogen corresponding to Synthetic Peptide within Human RPS27A aa 1-100.
Preservative: 0.09% Sodium azide
Constituents: 99.91% PBS
ICC | ChIP | WB | |
---|---|---|---|
Human | Tested | Tested | Tested |
Species | Dilution info | Notes |
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Species Human | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info - | Notes 1 μL |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 2.00000-3.00000 µg/mL | Notes - |
Ubiquitin. Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. Small ribosomal subunit protein eS31. Component of the 40S subunit of the ribosome (PubMed:23636399, PubMed:9582194). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:23636399, PubMed:34516797).
UBA80, UBCEP1, RPS27A, Ubiquitin-ribosomal protein eS31 fusion protein, Ubiquitin carboxyl extension protein 80
Rabbit Recombinant Multiclonal RPS27A antibody. Suitable for ICC, ChIP, WB and reacts with Human samples. Immunogen corresponding to Synthetic Peptide within Human RPS27A aa 1-100.
Preservative: 0.09% Sodium azide
Constituents: 99.91% PBS
Recombinant multiclonals are a mixture of recombinant antibodies co-expressed from a library of heavy and light chains.
Recombinant multiclonal antibodies offer the sensitivity of polyclonal antibodies by recognising multiple epitopes, along with consistency of a recombinant antibody.
Ubiquitin is a small regulatory protein found in almost all tissues of eukaryotic organisms. It has a molecular weight of approximately 8.6 kilodaltons. It functions mechanically by attaching to proteins through a process called ubiquitination which involves the formation of an isopeptide bond. Ubiquitin molecules can form polyubiquitin chains through different lysine residues such as K48 and K63 that determine their function. These chains label substrate proteins for various fates including degradation. Ubiquitin is expressed ubiquitously in cells reflecting its essential role in maintaining protein homeostasis.
The ubiquitin system plays a critical role in regulating protein turnover and quality control within cells. It is part of a larger complex known as the ubiquitin-proteasome system (UPS) which is responsible for degrading proteins that need to be turned over. This process is essential for cell cycle control response to oxidative stress and DNA repair. Ubiquitin's role in tagging proteins for degradation or signaling allows cells to respond quickly to changes in their environment and maintain balance.
Ubiquitin functions in several important biological pathways including the Wnt and NF-kB pathways. In the Wnt signaling pathway ubiquitination modulates the stability of key components thereby affecting the pathway's overall activity. In the NF-kB signaling pathway ubiquitin labels inhibitor proteins for degradation which releases and activates NF-kB. These pathways highlight ubiquitin's interaction with proteins such as beta-catenin in Wnt and IkB in NF-kB illustrating how it regulates diverse cellular processes.
The dysfunction of the ubiquitin system is linked to neurodegenerative diseases and cancers. Ubiquitin-related defects in protein degradation can lead to the buildup of unwanted proteins contributing to conditions like Parkinson's disease. Connections with cancer are evident as ubiquitin controls cell cycle proteins and aberrant ubiquitination may drive tumor growth and progression. The protein p53 known to be controlled by ubiquitination plays a significant role in cancer related mechanisms when dysregulated. Understanding and targeting ubiquitin-related pathways may provide new therapeutic opportunities for treating these conditions.
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Immunofluorescent analysis of Ubiquitin in U2OS cells using a Ubiquitin Recombinant Rabbit Multiclonal Antibody (ab277768) followed by detection using an Alexa Fluor® 488-conjugated Goat anti-Rabbit secondary antibody (green) (Image A). Nuclei were stained using DAPI(Image B) and actin stained with Alexa Fluor® 594 phalloidin (red) (image C). Image D is a composite image showing cytoplasmic localization of Ubiquitin.
Chromatin immunoprecipitation analysis of Ubiquitin was performed using cross-linked chromatin from 1 x 106 HCT116 human colon carcinoma cells treated with serum for 0, 15, and 60 minutes. Immunoprecipitation was performed using a multiplex microplate Matrix ChIP assay (see reference for Matrix ChIP protocol: http://www.ncbi.nlm.nih.gov/pubmed/22098709) with 1.0 μL/μ100L well volume of a Ubiquitin Recombinant Rabbit Polyclonal Antibody (ab277768). Chromatin aliquots from ~1 x 105 cells were used per ChIP pull-down. Quantitative PCR data were done in quadruplicate using 1 μL of eluted DNA in 2 μL SYBR real-time PCR reactions containing primers to amplify -3.2kb upstream of the human FOS gene, or exon-4 of human FOS. PCR calibration curves were generated for each primer pair from a dilution series of sheared total genomic DNA. Quantitation of immunoprecipitated chromatin is presented as signal relative to the total amount of input chromatin. Results represent the mean +/- SEM for three experiments. A schematic representation of the FOS locus is shown above the data where boxes represent exons (grey boxes = translated regions, white boxes = untranslated regions), the zigzag lines represent introns, and the straight line represents upstream sequence. Regions amplified by FOS primers are represented by black bars. Data courtesy of the Innovators Program.
Western blot analysis of Ubiquitin in whole cell extracts from K562 (human chronic myelogenous leukemia lymphoblast cell line) cells using a Ubiquitin Recombinant Rabbit Polyclonal Antibody (ab277768) at a dilution of 2 μg/mL. Samples were detected using chemiluminescence (ECL). Results show a band at ~8.5kDa.
All lanes: Western blot - Anti-Ubiquitin antibody [10HCLC] (ab277768) at 2 µg/mL
All lanes: K562 (human chronic myelogenous leukemia cell line from bone marrow ) whole cell extract
Predicted band size: 26 kDa
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