| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | UHRF1, Ubiquitin-Like With PHD And Ring Finger Domains, RING Finger Protein 106, RNF106, Np95, ICBP90 |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Shipping | |
| Species | |
| Storage | |
| UniProt # |
Scientific Background
Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, it also plays a key role in chromatin modification. The protein binds to specific DNA sequences, and recruits a histone deacetylase to regulate gene expression. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML.
Product Description
E. coli ExpressionRecombinant UHRF1 Human protein is produced using a validated E. coli expression system and supplied in aqueous buffer solution. Suitable for enzyme kinetics, inhibitor screening, binding assays, structural studies, and related biochemical research applications.
Protein Specifications
| UniProt ID | Q96T88 |
|---|---|
| Expression System | E. coli |
| Amino Acids / Region | 108-286 |
| Affinity Tag | N-terminal His-tag |
| Molecular Weight | 21.6 kDa |
| Formulation | 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 10 mM β-mercaptoethanol, 250 mM… |
| Storage | At least 6 months at -80°C. |
| Biosafety Level | Not applicable (BSL-1) |
Safety & Handling
Avoid freeze/thaw cycles.
This protein was produced in E. coli. Expression system selection determines post-translational processing, disulfide bond formation, and co-factor incorporation — all of which affect enzymatic activity. Insect cell (Sf9) systems are preferred for kinases and multi-subunit enzymes that require phosphorylation or chaperone assistance; E. coli is used for structurally simpler proteins.
This protein spans amino acids 108-286. Confirm the region includes your domain of interest — the active site, binding pocket, or substrate recognition sequence — before placing your order. Refer to the UniProt database for domain annotation.
Purity is assessed by SDS-PAGE; see the Certificate of Analysis. A gel image is provided with each lot. BPS Bioscience performs rigorous QC on each lot, including purity assessment and functional activity testing where applicable. Contact technical support if purity ≥99% is required for biophysical measurements.
Useful for protein binding assays, screening inhibitors, and selectivity profiling. Refer to the product datasheet for validated protocols and recommended assay conditions. Contact BioHippo technical support for application-specific guidance.
At least 6 months at -80°C. Avoid repeated freeze-thaw cycles — prepare single-use working aliquots. Add BSA or glycerol to aliquots if storing diluted enzyme is necessary. Typical stability is at least 6 months at −80°C.
BioHippo offers flexible sourcing for qualified research institutions and partners.
- Bulk quantities: Large-scale orders for HTS campaigns or structural studies.
- Custom constructs: Alternative tag positions, truncation variants, or point mutants may be available upon request.
- Biotinylated variants: Avi-Tag site-specific biotinylation is available for SPR/BLI surface capture applications.
- Extended QC data: Activity assay data, SEC-HPLC profiles, or additional purity methods available on request.
Contact BioHippo customer support for custom requirements.
- Kofunato, Y., et al., Oncol Rep.
- 2012 Dec; 28(6):1997-2002.
- Jazirehi, A.R., et al., Epigenomics.
- 2012 Jun;4(3):251-252. Application Reference(s):
- De Vos, M., et al. Poly(ADP-ribose) polymerase 1 (PARP1) associates with E3 ubiquitin-protein ligase UHRF1 and modulates UHRF1 biological functions. J Biol Chem. 2014 Jun 6;289(23):16223-38. (2014)
