XPC Protein (AA 496-734) (His tag)

Catalog No. ABIN5710632

Product Details

Target: XPC (Xeroderma Pigmentosum, Complementation Group C (XPC))

Protein Type: Recombinant

Protein Characteristics: AA 496-734

Origin: Human

Source: Escherichia coli (E. coli)

Purification tag / Conjugate: This XPC protein is labelled with His tag.

Application: SDS-PAGE (SDS)

Sequence: SLPAASSSSS SSKRGKKMCS DGEKAEKRSI AGIDQWLEVF CEQEEKWVCV DCVHGVVGQP LTCYKYATKP MTYVVGIDSD GWVRDVTQRY DPVWMTVTRK CRVDAEWWAE TLRPYQSPFM DREKKEDLEF QAKHMDQPLP TAIGLYKNHP LYALKRHLLK YEAIYPETAA ILGYCRGEAV YSRDCVHTLH SRDTWLKKAR VVRLGEVPYK MVKGFSNRAR KARLAEPQLR EENDLGLFG

Purification: SDS-PAGE

Purity: > 90 %

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 0.1-2 mg/mL

Buffer: 20 mM Tris-HCl based buffer, pH 8.0

Storage: -80 °C,4 °C,-20 °C

Storage Comment: Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target: XPC (Xeroderma Pigmentosum, Complementation Group C (XPC))

Alternative Name: XPC (XPC Products)

Synonyms: RAD4 Protein, XP3 Protein, XPCC Protein, XPC complex subunit, DNA damage recognition and repair factor Protein, xeroderma pigmentosum, complementation group C Protein, XPC Protein, Xpc Protein

Background: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. 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. 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.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. 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. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. 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. 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. 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 chically and structurally diverse DNA adducts. 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.

Molecular Weight: 31.6 kDa

UniProt: Q01831

Pathways: p53 Signaling, DNA Damage Repair