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AB159768

Recombinant Human UBA52 protein (GST tag N-Terminus)

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Recombinant Human UBA52 protein (GST tag N-Terminus) is a Human Fragment protein, in the 29 to 128 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

UBCEP2, UBA52, Ubiquitin-ribosomal protein eL40 fusion protein, CEP52, Ubiquitin A-52 residue ribosomal protein fusion product 1

1 Images
SDS-PAGE - Recombinant Human UBA52 protein (GST tag N-Terminus) (AB159768)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human UBA52 protein (GST tag N-Terminus) (AB159768)

ab159768 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

P62987

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Complementary Products

Primary Antibodies

AB109227

Anti-UBA52 antibody [EPR4546]

20ul selling size|RabMAb|Recombinant

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-UBA52 antibody [EPR4546] (AB109227)

  • 0
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Proteins & Peptides

AB183239

Recombinant Human DUSP6 protein (His tag N-Terminus)

Western blot - Recombinant Human DUSP6 protein (His tag N-Terminus) (AB183239)

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Proteins & Peptides

AB126024

Recombinant Human Adenosine Receptor A2a protein

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Primary Antibodies

AB138492

Anti-Collagen I antibody [EPR7785]

BOND RX™ Validated|KO Validated|RabMAb|Recombinant|Lab Essentials

Immunohistochemistry (Frozen sections) - Anti-Collagen I antibody [EPR7785] (AB138492)

  • 4
  • 37
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Reactivity data

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

[{"sequence":"KIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLRQLAQKYNCDKMICRKCYARLHPRAVNCRKKKCGHTNNLRPKKKVK","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":128,"aminoAcidStart":29,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P62987","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

UBA52 also known as Ubiquitin A-52 Residue Ribosomal Protein Fusion Product 1 is a protein fusion of ubiquitin and ribosomal protein L40. It has a mass of approximately 15 kDa. UBA52 expresses widely in various tissues including the liver brain and heart playing a role in protein synthesis and ubiquitination. The ubiquitin domain of UBA52 gets translated and cleaved to participate in the ubiquitin-proteasome system while the ribosomal component integrates into the 60S subunit of the ribosome.
Biological function summary

UBA52 functions as both a ribosomal protein and a source of ubiquitin. This dual role enables it to participate in protein synthesis as part of the ribosome. Additionally it provides ubiquitin required for post-translational modification of proteins affecting protein stability and degradation. UBA52 is part of the ribosome complex and contributes to efficient protein translation while its ubiquitin segment influences protein turnover and cellular response to stress.

Pathways

UBA52 plays roles in protein translation and ubiquitin-mediated proteolysis. These pathways are essential for maintaining cellular homeostasis. In the context of protein synthesis UBA52 associates with other ribosomal proteins and supports the assembly of the ribosome facilitating mRNA translation. In the ubiquitin-proteasome pathway UBA52 contributes ubiquitin moieties used to tag proteins for degradation working with E2 and E3 ligases such as UBE2K and HUWE1 important for regulated proteolysis.

UBA52 is linked to conditions involving protein synthesis defects and improper protein degradation including cancer and neurodegenerative disorders. Changes in UBA52 expression or mutations can disrupt ribosome function affecting cellular proliferation and survival in cancers. Additionally impaired ubiquitin signaling has implications in neurodegenerative diseases where protein aggregates form due to faulty degradation. UBA52's connection to pathways with proteins like p53 in cancer and Parkin in neurodegeneration further illustrates its relevance across different pathologies.
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Specifications

Form

Liquid

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General info

Function

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.. Large ribosomal subunit protein eL40. Component of the 60S subunit of the ribosome (PubMed : 23169626, PubMed : 23636399, PubMed : 32669547, PubMed : 39048817, PubMed : 39103523). Ribosomal protein L40 is essential for translation of a subset of cellular transcripts, and especially for cap-dependent translation of vesicular stomatitis virus mRNAs (PubMed : 23169626, PubMed : 23636399, PubMed : 32669547, PubMed : 39048817, PubMed : 39103523).

Sequence similarities

In the N-terminal section; belongs to the ubiquitin family.. In the C-terminal section; belongs to the eukaryotic ribosomal protein eL40 family.

Post-translational modifications

Ubiquitin. Phosphorylated at Ser-65 by PINK1 during mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25474007, PubMed:25527291). Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25474007, PubMed:25527291). Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30 (PubMed:25527291).. Ubiquitin. Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones.. Ubiquitin. (Microbial infection) Mono-ADP-ribosylated at Thr-66 by the C.violaceum CteC virulence factor. ADP-ribosylation causes the shutdown of polyubiquitin synthesis and disrupts the recognition and reversal of polyubiquitin.. Large ribosomal subunit protein eL40. Trimethylation of Lys-98 ('Lys-22' of the mature chain) by SMYD5 promotes translation elongation and protein synthesis.

Subcellular localisation

Nucleus

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Product protocols

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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.. Large ribosomal subunit protein eL40. Component of the 60S subunit of the ribosome (PubMed : 23169626, PubMed : 23636399, PubMed : 32669547, PubMed : 39048817, PubMed : 39103523). Ribosomal protein L40 is essential for translation of a subset of cellular transcripts, and especially for cap-dependent translation of vesicular stomatitis virus mRNAs (PubMed : 23169626, PubMed : 23636399, PubMed : 32669547, PubMed : 39048817, PubMed : 39103523).
See full target information UBA52
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