Analytical Data
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Gene name
KAT2A
- Application
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Alternative Names
KAT2A；GCN5；GCN5L2；Histone acetyltransferase KAT2A
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92830
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Expression Region
362-837aa
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AA Sequence
MLEEEIYGANSPIWESGFTMPPSEGTQLVPRPASVSAAVVPSTPIFSPSM GGGSNSSLSLDSAGAEPMPGEKRTLPENLTLEDAKRLRVMGDIPMELVNE VMLTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLTPK ANRRVLLWLVGLQNVFSHQLPRMPKEYIARLVFDPKHKTLALIKDGRVIG GICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHNILYFL TYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPY TELSHIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIPVESVPGI RETGWKPLGKEKGKELKDPDQLYTTLKNLLAQIKSHPSAWPFMEPVKKSE APDYYEVIRFPIDLKTMTERLRSRYYVTRKLFVADLQRVIANCREYNPPD SEYCRCASALEKFFYFKLKEGGLIDKDYKDDDDK
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Molecular Weight
55 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
KAT2A, also known as lysine acetyltransferase 2A, is a crucial enzyme involved in the dynamic regulation of histone acetylation, a key process in gene expression and cellular functions. Research on KAT2A has gained significant attention due to its implications in various biological processes, including differentiation, cell proliferation, and metabolism. Furthermore, aberrant KAT2A activity has been linked to several diseases, most notably cancer, where altered acetylation patterns can lead to uncontrolled cell growth and proliferation. The study of recombinant KAT2A proteins enables researchers to better understand the enzyme's structural and functional characteristics, facilitating the identification of specific substrates and the underlying mechanisms of acetylation. Advances in recombinant protein techniques have allowed for the production of KAT2A in sufficient quantities, enabling detailed biochemical assays and high-throughput screening for potential therapeutic inhibitors. As such, ongoing research focused on KAT2A is not only critical for elucidating its role in normal cellular physiology but also holds promise for developing targeted cancer therapies that modulate its activity. Understanding KAT2A's interactions and regulation could pave the way for novel strategies to manipulate acetylation pathways therapeutically.
