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AB314717

Human Ubiquitin+1/UBB+1 ELISA Kit

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Human Ubiquitin+1/UBB+1 ELISA Kit is a Sandwich (quantitative) ELISA for the measurement of Human Ubiquitin+1/UBB+1 in Human in Cell Culture Media, Biofluids samples.

View Alternative Names

UBA80, UBCEP1, RPS27A, Ubiquitin-ribosomal protein eS31 fusion protein, Ubiquitin carboxyl extension protein 80

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Sandwich ELISA - Human Ubiquitin+1/UBB+1 ELISA Kit (AB314717)
  • sELISA

Supplier Data

Sandwich ELISA - Human Ubiquitin+1/UBB+1 ELISA Kit (AB314717)

Example of standard curve using ab314717. This standard curve is for demonstrative purposes only. A standard curve must be run with each assay.

Key facts

Detection method

Colorimetric

Sample types

Cell culture supernatant, Plasma, Serum

Reacts with

Human

Assay type

Sandwich (quantitative)

Sensitivity

= 30 pg/mL

Range

30 - 20000 pg/mL

Assay Platform

Pre-coated microplate (12 x 8 well strips)

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "sELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Human Ubiquitin+1/UBB+1 ELISA kit is an in vitro enzyme-linked immunosorbent assay for the quantitative measurement of human Ubiquitin+1/UBB+1 in serum (human Ubiquitin+1/UBB+1 concentration is low in normal serum/plasma and may not be detectable in this assay), plasma, and cell culture supernatants. This assay employs an antibody specific for human Ubiquitin+1/UBB+1 coated on a 96-well plate.

This ELISA kit shows no cross-reactivity with the following cytokines tested: human Angiogenin, BDNF, BLC, ENA-78, FGF-4, IL-1a, IL-1b, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL9, IL-11, IL-12 p70, IL-12 p40, IL-13, IL-15, I-309, IP-10, G-CSF, GM-CSF, IFN-g, Leptin (OB), MCP-1, MCP-2, MCP-3, MDC, MIP-1a, MIP-1 b, MIP-1 delta, PARC, PDGF, RANTES, SCF, TARC, TGF-b, TIMP-1, TIMP-2, TNF-a, TNF-b, TPO, VEGF.

Recovery

[ { "sample": "Serum", "range": "86 - 115 %", "average": "= 97.81" }, { "sample": "Plasma", "range": "74 - 94 %", "average": "= 85.95" }, { "sample": "Cell culture media", "range": "117 - 136 %", "average": "= 128.2" } ]

What's included?

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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
-20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.
Biological function summary

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.

Pathways

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.

Product protocols

Target data

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).
See full target information RPS27A
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