| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | KDM1A, AOF2, lysine (K)-specific demethylase 1A, amine oxidase (flavin containing) domain 2, LSD |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Shipping | |
| Species | |
| Storage | |
| UniProt # |
Scientific Background
Variant 2 Human LSD1 [also known as KDM1A (lysine (K)-specific demethylase 1A) or AOF2, amine oxidase (flavin containing) domain 2)] GenBank Accession No. NM_015013, a.a. 158-end, MW=77.9 kDa, expressed in an E. coli expression system with N-terminal GST-tag and PreScission Protease site. GST-tag was cleaved after affinity purification.
Product Description
E. coli ExpressionRecombinant LSD1 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 | O60341 |
|---|---|
| Expression System | E. coli |
| Amino Acids / Region | 158-end |
| Molecular Weight | 77.9 kDa |
| Formulation | 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 1 mM DTT, 1 mM EDTA, 0.05% Twee… |
| Storage | At least 6 months at -80°C. |
| Biosafety Level | Not applicable (BSL-1) |
Specific Activity
≥20.6 pmol/min/µg
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 158-end. 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.
- Lan, F., et al., Nature. 448, 7154, 718-722, 2007.
- Forneris, F., et al., J. Biol. Chem. 282, 28, 20070-20074, 2007. Application References:
- A scintillation proximity assay for histone demethylases (2014)
- Crystal structure of the histone lysine specific demethylase LSD1 complexed with tetrahydrofolate (2014)
- Structural basis for histone mimicry and hijacking of host proteins by influenza virus protein NS1 (2014)
- A novel selective LSD1/KDM1A inhibitor epigenetically blocks herpes simplex virus lytic replication and reactivation from latency (2013)
- Discovery of ML324, a JMJD2 demethylase inhibitor with demonstrated antiviral activity (2013)
- Septins promote dendrite and axon development by negatively regulating microtubule stability via HDAC6-mediated deacetylation (2013)