General transcription factor IIH subunit 5 Recombinant Protein | GTF2H5 recombinant protein

Recombinant Human General transcription factor IIH subunit 5

Cat. Num. AAA1265178

• Gene Names: GTF2H5; TTD; TFB5; TTD3; TTDA; TFIIH; TTD-A; TGF2H5; C6orf175; bA120J8.2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: General transcription factor IIH subunit 5; Recombinant Human General transcription factor IIH subunit 5; General transcription factor IIH polypeptide 5TFB5 ortholog; TFIIH basal transcription factor complex TTD-A subunit; GTF2H5 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-71aa; Full Length
• Sequence: MVNVLKGVLIECDPAMKQFLLYLDESNALGKKFIIQDIDDTHVFVIAELVNVLQERVGELMDQNAFSLTQK
• Sequence Length: 71

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for GTF2H5 recombinant protein

Component of the TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell.

Product Categories/Family for GTF2H5 recombinant protein

Epigenetics and Nuclear Signaling

References

A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A and stabilizes TFIIH.Giglia-Mari G., Coin F., Ranish J.A., Hoogstraten D., Theil A., Wijgers N., Jaspers N.G.J., Raams A., Argentini M., van der Spek P.J., Botta E., Stefanini M., Egly J.-M., Aebersold R., Hoeijmakers J.H.J., Vermeulen W.Nat. Genet. 36:714-719(2004) The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.Science 316:1160-1166(2007) Crystal structure of the human TFIIH.Northeast structural genomics consortium (NESG) Submitted (FEB-2005) to the PDB data bank

NCBI and Uniprot Product Information

• NCBI GI #: 46359855
• NCBI GeneID: 404672
• NCBI Accession #: NP_997001.1
• NCBI GenBank Nucleotide #: NM_207118.2
• UniProt Accession #: Q6ZYL4; Q0P5V8
• Molecular Weight: 35.1 kDa
• NCBI Official Full Name: general transcription factor IIH subunit 5
• NCBI Official Synonym Full Names: general transcription factor IIH subunit 5
• NCBI Official Symbol: GTF2H5
• NCBI Official Synonym Symbols: TTD; TFB5; TTD3; TTDA; TFIIH; TTD-A; TGF2H5; C6orf175; bA120J8.2
• NCBI Protein Information: general transcription factor IIH subunit 5
• UniProt Protein Name: General transcription factor IIH subunit 5
• Protein Family: General transcription factor
• UniProt Gene Name: GTF2H5
• UniProt Synonym Gene Names: C6orf175; TTDA
• UniProt Entry Name: TF2H5_HUMAN

NCBI Description

This gene encodes a subunit of transcription/repair factor TFIIH, which functions in gene transcription and DNA repair. This protein stimulates ERCC3/XPB ATPase activity to trigger DNA opening during DNA repair, and is implicated in regulating cellular levels of TFIIH. Mutations in this gene result in trichothiodystrophy, complementation group A. [provided by RefSeq, Mar 2009]

Uniprot Description

GTF2H5: Component of the TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell. Defects in GTF2H5 are a cause of trichothiodystrophy photosensitive (TTDP). TTDP is an autosomal recessive disease characterized by sulfur-deficient brittle hair and nails, ichthyosis, mental retardation, impaired sexual development, abnormal facies and cutaneous photosensitivity correlated with a nucleotide excision repair (NER) defect. Neonates with trichothiodystrophy and ichthyosis are usually born with a collodion membrane. The severity of the ichthyosis after the membrane is shed is variable, ranging from a mild to severe lamellar ichthyotic phenotype. There are no reports of skin cancer associated with TTDP. Belongs to the TFB5 family.

Protein type: DNA repair, damage; DNA-binding

Chromosomal Location of Human Ortholog: 6q25.3

Cellular Component: nucleolus; nucleoplasm

Molecular Function: rDNA binding

Biological Process: DNA repair; gene expression; mRNA capping; negative regulation of gene expression, epigenetic; nucleotide-excision repair; nucleotide-excision repair, DNA incision; nucleotide-excision repair, preincision complex assembly; positive regulation of viral transcription; regulation of gene expression, epigenetic; regulation of transcription, DNA-dependent; RNA elongation from RNA polymerase I promoter; RNA elongation from RNA polymerase II promoter; rRNA processing; termination of RNA polymerase I transcription; transcription from RNA polymerase I promoter; transcription from RNA polymerase II promoter; transcription initiation from RNA polymerase I promoter; transcription initiation from RNA polymerase II promoter; transcription-coupled nucleotide-excision repair; viral reproduction

Disease: Trichothiodystrophy 3, Photosensitive