TRIB1 (NM_025195) Human Tagged ORF Clone Lentiviral Particle
SKU
RC209219L2V
Lenti ORF particles, TRIB1 (mGFP-tagged) - Human tribbles homolog 1 (Drosophila) (TRIB1), 200ul, >10^7 TU/mL
Product Data | |
Type | Human Tagged ORF Clone Lentiviral Particle |
---|---|
Tag | mGFP |
Target Symbol | TRIB1 |
Synonyms | C8FW; GIG-2; GIG2; SKIP1; TRB-1; TRB1 |
Vector | pLenti-C-mGFP |
Mammalian Cell Selection | None |
Sequence Data |
ORF Nucleotide Sequence
The ORF insert of this clone is exactly the same as(RC209219).
|
ACCN | NM_025195 |
ORF Size | 1116 bp |
OTI Disclaimer | The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info |
OTI Annotation | This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. |
Shipping | Dry Ice |
Reference Data | |
RefSeq | NM_025195.2 |
RefSeq Size | 3649 bp |
RefSeq ORF | 1119 bp |
Locus ID | 10221 |
UniProt ID | Q96RU8 |
Cytogenetics | 8q24.13 |
Domains | pkinase, S_TKc |
Protein Families | Druggable Genome, Protein Kinase |
MW | 41 kDa |
Summary | Adapter protein involved in protein degradation by interacting with COP1 ubiquitin ligase (PubMed:27041596). The COP1-binding motif is masked by autoinhibitory interactions with the protein kinase domain (PubMed:26455797). Serves to alter COP1 substrate specificity by directing the activity of COP1 toward CEBPA (PubMed:27041596). Binds selectively the recognition sequence of CEBPA (PubMed:26455797). Regulates myeloid cell differentiation by altering the expression of CEBPA in a COP1-dependent manner (By similarity). Controls macrophage, eosinophil and neutrophil differentiation via the COP1-binding domain (By similarity). Interacts with MAPK kinases and regulates activation of MAP kinases, but has no kinase activity (PubMed:15299019, PubMed:26455797).[UniProtKB/Swiss-Prot Function] |
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