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Recombinant Human XPC protein (His tag) is a Human Fragment protein, in the 496 to 734 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.

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Images

SDS-PAGE - Recombinant Human XPC protein (His tag) (AB236173), expandable thumbnail
  • Mass Spectrometry - Recombinant Human XPC protein (His tag) (AB236173), expandable thumbnail
  • Mass Spectrometry - Recombinant Human XPC protein (His tag) (AB236173), expandable thumbnail

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, MS

Biologically active

No

Amino acid sequence

S L P A A S S S S S S S K R G K K M C S D G E K A E K R S I A G I D Q W L E V F C E Q E E K W V C V D C V H G V V G Q P L T C Y K Y A T K P M T Y V V G I D S D G W V R D V T Q R Y D P V W M T V T R K C R V D A E W W A E T L R P Y Q S P F M D R E K K E D L E F Q A K H M D Q P L P T A I G L Y K N H P L Y A L K R H L L K Y E A I Y P E T A A I L G Y C R G E A V Y S R D C V H T L H S R D T W L K K A R V V R L G E V P Y K M V K G F S N R A R K A R L A E P Q L R E E N D L G L F G

Reactivity data

Application

SDS-PAGE

Reactivity

Reacts

Dilution info

-

Notes

-

Application

MS

Reactivity

Reacts

Dilution info

-

Notes

-

Target data

Function

Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex (PubMed:10734143, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19609301, PubMed:19941824, PubMed:20028083, PubMed:20649465, PubMed:20798892, PubMed:9734359). Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides (PubMed:10734143, PubMed:19609301, PubMed:20649465). This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity (PubMed:10734143, PubMed:19609301, PubMed:20649465). The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The orientation of XPC complex binding appears to be crucial for inducing a productive NER (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts (PubMed:20028083). XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1 (PubMed:20028083).In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT) (PubMed:29973595, PubMed:31527837). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes (PubMed:31527837).

Alternative names

Recommended products

Recombinant Human XPC protein (His tag) is a Human Fragment protein, in the 496 to 734 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Applications

SDS-PAGE, MS

Accession
Q01831-1
Animal free

No

Species

Human

Concentration
Loading...
Storage buffer

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

Sequence info

Amino acid sequence

S L P A A S S S S S S S K R G K K M C S D G E K A E K R S I A G I D Q W L E V F C E Q E E K W V C V D C V H G V V G Q P L T C Y K Y A T K P M T Y V V G I D S D G W V R D V T Q R Y D P V W M T V T R K C R V D A E W W A E T L R P Y Q S P F M D R E K K E D L E F Q A K H M D Q P L P T A I G L Y K N H P L Y A L K R H L L K Y E A I Y P E T A A I L G Y C R G E A V Y S R D C V H T L H S R D T W L K K A R V V R L G E V P Y K M V K G F S N R A R K A R L A E P Q L R E E N D L G L F G

Accession

Q01831

Protein length

Fragment

Predicted molecular weight

31.5 kDa

Amino acids

496 to 734

Nature

Recombinant

Tags

His tag N-Terminus

Specifications

Form

Liquid

General info

Function

Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex (PubMed:10734143, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19609301, PubMed:19941824, PubMed:20028083, PubMed:20649465, PubMed:20798892, PubMed:9734359). Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides (PubMed:10734143, PubMed:19609301, PubMed:20649465). This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity (PubMed:10734143, PubMed:19609301, PubMed:20649465). The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). The orientation of XPC complex binding appears to be crucial for inducing a productive NER (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892, PubMed:9734359). In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts (PubMed:20028083). XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1 (PubMed:20028083).

Sequence similarities

Belongs to the XPC family.

Post-translational modifications

Ubiquitinated upon UV irradiation; the ubiquitination requires the UV-DDB complex, appears to be reversible and does not serve as a signal for degradation (PubMed:15882621, PubMed:23751493). Ubiquitinated by RNF11 via 'Lys-63'-linked ubiquitination (PubMed:23751493). Ubiquitination by RNF111 is polysumoylation-dependent and promotes nucleotide excision repair (PubMed:23751493).

Subcellular localisation

Nucleus

Storage

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

Supplementary info

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

Activity summary

The Xeroderma Pigmentosum Complementation Group C (XPC) protein is essential for the nucleotide excision repair (NER) mechanism repairing DNA damage. XPC with a molecular weight of approximately 125 kDa recognises and binds to damaged DNA that has bulky adducts. It is expressed in various human tissues with higher expression levels in proliferating cells and skin. XPC plays a critical role in DNA testing and maintenance making it vital for maintaining genome stability.

Biological function summary

The XPC protein acts as a damage sensor within the NER pathway and functions as part of the XPC-HR23B complex. This complex identifies DNA helix distortions and signals for repair by recruiting other proteins to the damage site. XPC functions by unwinding the DNA and allowing necessary repair enzymes such as DNA helicases and nucleases to perform their functions. This repair process ensures that the DNA is intact and capable of proper transcription and cell replication.

Pathways

XPC operates within the nucleotide excision repair pathway which is essential for removing a wide range of DNA lesions caused by ultraviolet (UV) irradiation and chemical agents. It operates in conjunction with proteins such as XPA RPA and the TFIIH complex to execute DNA repair. XPC is also linked to the global genomic repair sub-pathway of NER where it plays a leading role in identifying DNA damage across the entire genome.

Associated diseases and disorders

Ineffective XPC function is associated with Xeroderma Pigmentosum (XP) a genetic disorder causing extreme sensitivity to UV light and increased skin cancer risk. Mutations in the XPC gene impede DNA repair efficiency leading to the accumulation of damage. XPC is also connected to skin cancer development as its malfunction can cause failure to repair UV-induced lesions. Other proteins like XPA and XPE also show connections to these disorders highlighting their critical roles in maintaining DNA integrity and preventing disease.

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3 product images

  • SDS-PAGE - Recombinant Human XPC protein (His tag) (ab236173), expandable thumbnail

    SDS-PAGE - Recombinant Human XPC protein (His tag) (ab236173)

    (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab236173.

  • Mass Spectrometry - Recombinant Human XPC protein (His tag) (ab236173), expandable thumbnail

    Mass Spectrometry - Recombinant Human XPC protein (His tag) (ab236173)

    Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab236173 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) XPC.

  • Mass Spectrometry - Recombinant Human XPC protein (His tag) (ab236173), expandable thumbnail

    Mass Spectrometry - Recombinant Human XPC protein (His tag) (ab236173)

    Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab236173 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) XPC.

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