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AB239559

Recombinant Human C4orf27 protein (Tagged)

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Recombinant Human C4orf27 protein (Tagged) is a Human Full Length protein, in the 1 to 346 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

C4orf27, HPF1, Histone PARylation factor 1

3 Images
Mass Spectrometry - Recombinant Human C4orf27 protein (Tagged) (AB239559)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human C4orf27 protein (Tagged) (AB239559)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab239559 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) C4orf27.

Mass Spectrometry - Recombinant Human C4orf27 protein (Tagged) (AB239559)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human C4orf27 protein (Tagged) (AB239559)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab239559 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) C4orf27.

SDS-PAGE - Recombinant Human C4orf27 protein (Tagged) (AB239559)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human C4orf27 protein (Tagged) (AB239559)

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab239559.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

10x His tag N-Terminus SUMO tag N-Terminus Myc tag C-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

Q9NWY4

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

storage-buffer

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Reactivity data

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

[{"linker":null,"sequence":"MVGGGGKRRPGGEGPQCEKTTDVKKSKFCEADVSSDLRKEVENHYKLSLPEDFYHFWKFCEELDPEKPSDSLSASLGLQLVGPYDILAGKHKTKKKSTGLNFNLHWRFYYDPPEFQTIIIGDNKTQYHMGYFRDSPDEFPVYVGINEAKKNCIIVPNGDNVFAAVKLFLTKKLREITDKKKINLLKNIDEKLTEAARELGYSLEQRTVKMKQRDKKVVTKTFHGAGLVVPVDKNDVGYRELPETDADLKRICKTIVEAASDEERLKAFAPIQEMMTFVQFANDECDYGMGLELGMDLFCYGSHYFHKVAGQLLPLAYNLLKRNLFAEIIEEHLANRSQENIDQLAA","proteinLength":"Full Length","predictedMolecularWeight":"59.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":346,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9NWY4","tags":[{"tag":"10x His","terminus":"N-Terminus"},{"tag":"SUMO","terminus":"N-Terminus"},{"tag":"Myc","terminus":"C-Terminus"}]}]
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Properties and storage information

Form
Liquid
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

C4orf27 also known as UPF0710 protein C4orf27 is a protein encoded by the C4orf27 gene. It has a molecular mass of approximately 14 kDa. The C4orf27 protein's mechanical function is not fully understood but it is believed to have a role in cellular processes due to its conserved sequences. Expression of C4orf27 is observed in various tissues including the liver kidney and brain suggesting its involvement in multiple physiological functions.
Biological function summary

The function of C4orf27 remains unspecified but appears to be involved in cellular homeostasis and metabolism. It is hypothesized to participate in intracellular signaling pathways although it does not form part of any well-studied protein complex. Researchers continue to investigate its specific biological roles and interactions within the cell due to its broad expression pattern.

Pathways

C4orf27 may interact with cellular signaling and metabolic pathways. While its direct involvement in specific pathways remains under study it shows potential interactions with pathways such as the mitochondrial function and oxidative phosphorylation. Proteins such as COX4I1 involved in the electron transport chain may relate to C4orf27 through these pathways suggesting a role in energy utilization and cellular stress responses.

Research is ongoing to understand C4orf27's contributions to pathological states. Initial studies suggest associations with metabolic disorders and neurodegenerative diseases such as Alzheimer's disease. It may interact with proteins like APP (Amyloid precursor protein) through oxidative stress pathways possibly linking it to the pathogenesis of neurodegeneration. Further research will clarify the relevance of C4orf27 in these diseases aiming to discover potential therapeutic implications.
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General info

Function

Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response (PubMed : 28190768, PubMed : 29480802, PubMed : 29954836, PubMed : 32028527, PubMed : 32939087, PubMed : 33186521, PubMed : 33589610, PubMed : 33683197, PubMed : 34108479, PubMed : 34210965, PubMed : 34486521, PubMed : 34625544, PubMed : 34732825, PubMed : 34795260, PubMed : 34874266). Initiates the repair of double-strand DNA breaks : recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins (PubMed : 28190768, PubMed : 29480802, PubMed : 29954836, PubMed : 32028527, PubMed : 32939087, PubMed : 33589610, PubMed : 33683197, PubMed : 34486521, PubMed : 34625544, PubMed : 34732825, PubMed : 34795260, PubMed : 34874266). Serine ADP-ribosylation of target proteins, such as histones, promotes decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed : 27067600, PubMed : 28190768, PubMed : 32939087, PubMed : 33589610). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed : 29480802). HPF1 acts by completing the active site of PARP1 and PARP2 : forms a composite active site composed of residues from HPF1 and PARP1 or PARP2 (PubMed : 32028527, PubMed : 33589610). While HPF1 promotes the initiation of serine ADP-ribosylation, it restricts the polymerase activity of PARP1 and PARP2 in order to limit the length of poly-ADP-ribose chains (PubMed : 33683197, PubMed : 34732825, PubMed : 34795260). HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1 (PubMed : 29954836, PubMed : 30257210).

Sequence similarities

Belongs to the HPF1 family.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response (PubMed : 28190768, PubMed : 29480802, PubMed : 29954836, PubMed : 32028527, PubMed : 32939087, PubMed : 33186521, PubMed : 33589610, PubMed : 33683197, PubMed : 34108479, PubMed : 34210965, PubMed : 34486521, PubMed : 34625544, PubMed : 34732825, PubMed : 34795260, PubMed : 34874266). Initiates the repair of double-strand DNA breaks : recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins (PubMed : 28190768, PubMed : 29480802, PubMed : 29954836, PubMed : 32028527, PubMed : 32939087, PubMed : 33589610, PubMed : 33683197, PubMed : 34486521, PubMed : 34625544, PubMed : 34732825, PubMed : 34795260, PubMed : 34874266). Serine ADP-ribosylation of target proteins, such as histones, promotes decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed : 27067600, PubMed : 28190768, PubMed : 32939087, PubMed : 33589610). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed : 29480802). HPF1 acts by completing the active site of PARP1 and PARP2 : forms a composite active site composed of residues from HPF1 and PARP1 or PARP2 (PubMed : 32028527, PubMed : 33589610). While HPF1 promotes the initiation of serine ADP-ribosylation, it restricts the polymerase activity of PARP1 and PARP2 in order to limit the length of poly-ADP-ribose chains (PubMed : 33683197, PubMed : 34732825, PubMed : 34795260). HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1 (PubMed : 29954836, PubMed : 30257210).
See full target information HPF1
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