Recombinant Human General Transcription And Dna Repair Factor Iih Helicase Subunit Xpb (ERCC3) Protein (GST)

Name: Recombinant Human General Transcription And Dna Repair Factor Iih Helicase Subunit Xpb (ERCC3) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-00637P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human General Transcription And Dna Repair Factor Iih Helicase Subunit Xpb (ERCC3) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P19447
Target Symbol	ERCC3
Synonyms	(TFIIH subunit XPB)(Basic transcription factor 2 89 kDa subunit)(BTF2 p89)(DNA excision repair protein ERCC-3)(DNA repair protein complementing XP-B cells)(TFIIH basal transcription factor complex 89 kDa subunit)(TFIIH 89 kDa subunit)(TFIIH p89)(Xeroderma pigmentosum group B-complementing protein)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MGKRDRADRDKKKSRKRHYEDEEDDEEDAPGNDPQEAVPSAAGKQVDESGTKVDEYGAKDYRLQMPLKDDHTSRPLWVAPDGHIFLEAFSPVYKYAQDFLVAIAEPVCRPTHVHEYKLTAYSLYAAVSVGLQTSDITEYLRKLSKTGVPDGIMQFIKLCTVSYGKVKLVLKHNRYFVESCHPDVIQHLLQDPVIRECRLRNSEGEATELITETFTSKSAISKTAESSGGPSTSRVTDPQGKSDIPMDLFDFYEQMDKDEEEEEETQTVSFEVKQEMIEELQKRCIHLEYPLLAEYDFRNDSVNPDINIDLKPTAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTAACTVRKRCLVLGNSAVSVEQWKAQFKMWSTIDDSQICRFTSDAKDKPIGCSVAISTYSMLGHTTKRSWEAERVMEWLKTQEWGLMILDEVHTIPAKMFRRVLTIVQAHCKLGLTATLVREDDKIVDLNFLIGPKLYEANWMELQNNGYIAKVQCAEVWCPMSPEFYREYVAIKTKKRILLYTMNPNKFRACQFLIKFHERRNDKIIVFADNVFALKEYAIRLNKPYIYGPTSQGERMQILQNFKHNPKINTIFISKVGDTSFDLPEANVLIQISSHGGSRRQEAQRLGRVLRAKKGMVAEEYNAFFYSLVSQDTQEMAYSTKRQRFLVDQGYSFKVITKLAGMEEEDLAFSTKEEQQQLLQKVLAATDLDAEEEVVAGEFGSRSSQASRRFGTMSSMSGADDTVYMEYHSSRSKAPSKHVHPLFKRFRK
Expression Range	1-782aa
Protein Length	Full Length
Mol. Weight	115.6 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/ERCC3, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/ERCC3 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Subcellular Location	Nucleus.
Protein Families	Helicase family, RAD25/XPB subfamily
Database References	HGNC: 3435 OMIM: 133510 KEGG: hsa:2071 STRING: 9606.ENSP00000285398 UniGene: PMID: 28813025 An essential role of MYC-ERCC3 interactions in PDAC. PMID: 27384421 similar to tumors arising in the background of homologous repair defects, mutations in nucleotide excision repair genes such as ERCC3 could constitute potential therapeutic targets in a subset of hereditary breast cancers. PMID: 27655433 results reveal a previously unknown role for transcription factor IIH in ATR kinase activation in non-replicating, non-cycling cells PMID: 28592488 Study shows that: mRNA synthesis is sensitive to the inhibition of the ATPase activity of XPB; mRNA synthesis accommodates the depletion of XPB; XPB-depleted TFIIH participates in mRNA synthesis, and finally, XPB ATPase overcomes transcription initiation block imposed by its helicase motifs. PMID: 28157507 findings suggest that benzene exposure may be associated with hypermethylation in ERCC3, and that genetic variants in EPHX1 may play an important role in epigenetic changes and hematotoxicity among benzene-exposed workers PMID: 23797950 The crystal structure of the C-terminal half of the XPB subunit of TFIIH (residues 494-782) is reported, containing XPB helicase domain (HD)2 and a C-terminal extension which shares structural similarity with RIG-I. PMID: 23385459 Phenotype-specific adverse effects of XPD mutations on human prenatal development implicate impairment of TFIIH-mediated functions in placenta. PMID: 22234153 reduction in ERCC3 by siRNA interference in human melanocytes in vitro reduced their tyrosinase production ability PMID: 22615732 These results indicated that persistent HBV infection might trigger NER impairment in part through upregulation of miR-192, which suppressed the levels of ERCC3 and ERCC4. PMID: 21672525 Results show that a deficiency in functional XPB paradoxically renders cells more sensitive to the genotoxic effects of oxidative stress while reducing the cytotoxic effects. PMID: 19840190 The phosphorylation of the androgen receptor by TFIIH directs the ubiquitin/proteasome process. PMID: 21157430 The C1D gene has been identified as one of the major genes whose expression is significantly upregulated by restoring XPB function. PMID: 20530579 results demonstrated that a) XP-G/CS mutations affect the disassembly state of TFIIH resulting in the dissociation of CAK, but not XPD from core TFIIH PMID: 20543986 TFIIH core subunit p89, but not other subunits of TFIIH, associates with the centrosomes and the adjacent parts of the mitotic spindle during mitosis. PMID: 20208140 p52 mediates function within the transcription/repair factor TFIIH. PMID: 12080057 Reduced level of the repair/transcription factor TFIIH in trichothiodystrophy. PMID: 12393803 TFIIH from trichothiodystrophy patients, but not from xeroderma pigmentosum patients, exhibit a significant in vitro basal transcription defect in addition to a reduced intercellular concentration. PMID: 12820975 High XRB mRNA levels is associated with Clear cell tumors of epithelial ovarian cancer PMID: 14614013 identification of a new, evolutionarily conserved, core TFIIH subunit is essential for our understanding of TFIIH function in transcription, DNA repair and human disease PMID: 15220921 Reduced expression of ERCC3 was correlated with esophageal cancer progression PMID: 15375507 data support an additional role for XPB in promoting the incision of the damaged DNA fragment and reveal a point of nucleotide excision repair regulation on TFIIH without interference in its transcription activity PMID: 15549133 Single Nucleotide Polymorphism in the ERCC3 is associated with lung cancer PMID: 16835333 XPB could inhibit the proliferation of hepatoma cells and had a positive effect on the expression of p53 and p21(waf1/cip1) but a negative effect on c-myc. PMID: 16914395 Multiple proteins both known and unknown to interact with RAD52 were identified by the "dual-tagging" proteomic method. PMID: 19338310 Single Nucleotide Polimorphisms in VEGF and ERCC3 were associated with alterations in White Blood Cells and WBC subtype counts in workers exposed to benzene, even at relatively low levels of exposure below 1 ppm. PMID: 19773279

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.