LSD1 Protein, Human (sf9, His-GST)

The LSD1 protein is a histone demethylase that modifies histone H3 by demethylating “Lys-4” (H3K4me) and “Lys-9” (H3K9me). It acts as a coactivator or corepressor, oxidizing substrates via FAD to generate imines that are subsequently hydrolyzed. LSD1 Protein, Human (sf9, His-GST) is the recombinant human-derived LSD1 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of LSD1 Protein, Human (sf9, His-GST) is 681 a.a., with molecular weight of ~93 kDa.

LSD1, a histone demethylase, exhibits the unique capability to demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, functioning as a versatile coactivator or corepressor depending on the cellular context. Acting through FAD-mediated oxidation and subsequent imine hydrolysis, LSD1 can demethylate mono- and di-methylated H3K4me, thus contributing to the regulation of epigenetic transcriptional activation. In the absence of RCOR1/CoREST, LSD1 alone is unable to demethylate H3K4me on nucleosomes. Additionally, LSD1 serves as a coactivator for androgen receptor (AR)-dependent transcription, participating in the demethylation of H3K9me, a marker associated with epigenetic transcriptional repression. Moreover, LSD1 plays a pivotal role in suppressing neuronal genes and orchestrates the repression of E-cadherin/CDH1, CDN7, and KRT8 through its involvement in the RCOR/GFI/KDM1A/HDAC complex. Beyond histone demethylation, LSD1's diverse interactions extend to demethylating p53/TP53, stabilizing DNMT1, and modifying SOX2. The intricate regulatory role of LSD1 spans embryogenesis, gastrulation, and multilineage blood cell development, emphasizing its significance in shaping the epigenetic landscape and influencing various cellular processes.

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Human

Sf9 insect cells

N-His;N-GST

O60341-1 (S172-M852)

23028  [NCBI]

SGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM

Approximately 93 kDa

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris, 500 mM NaCl, 2 mM DTT, pH 8.0, 10% Glycerol . Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.