| Field | Specification |
|---|---|
| Alternative Names | KTM6A, EZH2, PRC2, Enhancer Of Zeste Homolog 2; RBAP48, Retinoblastoma Binding Protein 4 (RBBP4), NURF55, Chromatin Assembly Factor 1 Subunit C, CAF1 p48; Embryonic Ectoderm Development, hEED, EED, WAIT-1; SUZ12, Suppressor Of Zeste 12 Homolog, CHET9, JJA |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Shipping | |
| Species | |
| Storage | |
| UniProt # |
Scientific Background
EZH2 is the catalytic subunit of the PRC2/EED-EZH2 complex, which methylates Lys9 (H3K9me) and Lys27 (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate Lys27 of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Compared to EZH2-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems.
Product Description
Insect Cells (Sf9) ExpressionRecombinant EZH2/EED/SUZ12/RbAp48/AEBP2 Human protein is produced using a validated Insect Cells (Sf9) 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 | Q15910 |
|---|---|
| Expression System | Insect Cells (Sf9) |
| Amino Acids / Region | 2-end (all components) |
| Affinity Tag | N-terminal FLAG-tag(EED), N-terminal His-tag (other components) |
| Molecular Weight | 325 kDa (complex) |
| Formulation | 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 200 mM imidazole, and 20% glyce… |
| Storage | At least 6 months at -80°C. |
| Biosafety Level | Not applicable (BSL-1) |
Specific Activity
0.08 pmol/min/µg
Safety & Handling
Avoid freeze/thaw cycles.
This protein was produced in Insect Cells (Sf9). 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 2-end (all components). 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 the study of enzyme kinetics, 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.
- Morin, R., et al. (2010). Nature Genetics 42, 181 - 185.
- Varambally, S. et al. (2008). Science 322 (5908), 1695-1699.
- Rakotobe, D. et al. (2008). Virol. J. 5, 32.
- Application Reference(s): 1. Arcand, M., et al., ""Development of High-Throughput Assays to Study Methylases, Demethylases and Deacetylases."" Poster presented as part of the BioTechniques Fall 2011 Epigenetics Meeting.
- Yap, D.B, et al., "Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethlyation." (2010). Blood. 117: 2451-2459.
Research budgets are tight — we get it. That's why we've put together a fresh round of exclusive promotions designed to help you stock up on the reagents, kits, and consumables your lab depends on, without stretching your budget.
🔬 What's on offer right now:
10% Off Pre-Designed siRNA Sets
20% Off Transmembrane Proteins
50% Off Lab Consumables + Free Shipping
$99 Pipette Filler Promotion Package
BlasTaq 2X qPCR MasterMix - 50% OFF Limited Time Offer
DENARASE® Endonuclease — 10% Off One Order