Analytical Data
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Gene name
SMYD2
- Application
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Alternative Names
SMYD2；KMT3C；N-lysine methyltransferase SMYD2
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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
Q9NRG4
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Expression Region
1-433aa
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AA Sequence
MRAEGLGGLE RFCSPGKGRG LRALQPFQVG DLLFSCPAYA YVLTVNERGN HCEYCFTRKE GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW NPSETVRLTA RILAKQKIHP ERTPSEKLLA VKEFESHLDK LDNEKKDLIQ SDIAALHHFY SKHLGFPDND SLVVLFAQVN CNGFTIEDEE LSHLGSAIFP DVALMNHSCC PNVIVTYKGT LAEVRAVQEI KPGEEVFTSY IDLLYPTEDR NDRLRDSYFF TCECQECTTK DKDKAKVEIR KLSDPPKAEA IRDMVRYARN VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC LYMQDWEGAL QYGQKIIKPY SKHYPLYSLN VASMWLKLGR LYMGLEHKAA GEKALKKAIA IMEVAHGKDH PYISEIKQEI ESH
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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
SMYD2 (SET and MYND domain containing 2) is a histone methyltransferase that plays a crucial role in various cellular processes, including gene expression regulation, cell proliferation, and differentiation. Its dysregulation has been implicated in several cancers, particularly in promoting tumor growth and metastasis. As a member of the SMYD family, SMYD2 catalyzes the methylation of lysine residues on histones, which is pivotal for epigenetic modifications that regulate chromatin structure and gene activity. Recent studies have highlighted the significance of SMYD2 in the context of oncogenic pathways, making it a potential target for cancer therapy. Research efforts are focused on understanding the precise molecular mechanisms by which SMYD2 influences tumor biology, including its interactions with other proteins and its role in modulating the epigenetic landscape. Furthermore, developing SMYD2 inhibitors is a promising strategy for targeting cancer cells that exhibit aberrant SMYD2 activity. The exploration of SMYD2's structure-function relationship through recombinant protein studies is essential for elucidating its enzymatic activity and for the design of specific inhibitors. As a result, the investigation into SMYD2 not only enhances our understanding of cancer biology but also offers new avenues for therapeutic intervention, highlighting its importance in medical research and drug development.
