Recombinant Human E3 ubiquitin-protein ligase TRIP12(TRIP12),partial

Recombinant Human E3 ubiquitin-protein ligase TRIP12(TRIP12),partial

CSB-BP617924HU
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Size:100ug. Other sizes are also available. For further information, please contact us.

Research Areas:Epigenetics and Nuclear Signaling

Uniprot ID:Q14669

Gene Names:TRIP12

Organism:Homo sapiens (Human)

AA Sequence:ECCRPDHGYTHDSRAVKFLFEILSSFDNEQQRLFLQFVTGSPRLPVGGFRSLNPPLTIVRKTFESTENPDDFLPSVMTCVNYLKLPDYSSIEIMREKLLIAAREGQQSFHLS

Expression Region:1881-1992aa

Sequence Info:Partial

Source:Baculovirus

Tag Info:N-terminal 10xHis-tagged and C-terminal Myc-tagged

MW:16.9 kDa

Alternative Name(s):E3 ubiquitin-protein ligase for Arf (ULF) (HECT-type E3 ubiquitin transferase TRIP12) (Thyroid receptor-interacting protein 12) (TR-interacting protein 12) (TRIP-12)

Relevance:E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.

Reference:"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994)

Purity:Greater than 85% as determined by SDS-PAGE.

Form:Liquid or Lyophilized powder

Buffer:If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution:We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20?/-80?. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Storage:The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20?/-80?. The shelf life of lyophilized form is 12 months at -20?/-80?.

Notes:Repeated freezing and thawing is not recommended. Store working aliquots at 4? for up to one week.

Function:E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardeless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.

Involvement in disease:

Subcellular Location:Nucleus, nucleoplasm

Protein Families:UPL family, K-HECT subfamily

Tissue Specificity:

Paythway:Ubiquitinmediatedproteolysis

HGNC Database Link:https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12306

UniGene Database Link:https://www.ncbi.nlm.nih.gov/UniGene/clust.cgi?ORG=Hs&CID=572642

KEGG Database Link:https://www.genome.jp/dbget-bin/www_bget?hsa:9320

STRING Database Link:https://string-db.org/network/9606.ENSP00000283943

OMIM Database Link:https://www.omim.org/entry/604506604506604506

Lead Time Guidance:28-38 business days

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