Analytical Data
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Gene name
MELK
- Application
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Alternative Names
MELK；KIAA0175；Maternal embryonic leucine zipper kinase
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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
Q14680
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Expression Region
1-340aa
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AA Sequence
MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCG
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Molecular Weight
44.3 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
MELK (Maternal Embryonic Leucine Zipper Kinase) is a serine/threonine protein kinase that plays a crucial role in cell proliferation, survival, and differentiation, making it a significant focus of cancer research. Initially identified as a gene regulated during embryonic development, MELK has been linked to various malignancies, particularly in aggressive cancer types characterized by high mitotic activity and poor prognosis. Its overexpression in tumors has been correlated with enhanced cancer cell growth and resistance to apoptosis, driving interest in MELK as a potential therapeutic target. Research into MELK has expanded to explore its function in stem cell maintenance and differentiation, further establishing its importance in both normal and pathological processes. These studies have prompted investigations into MELK's structural properties and its potential as a drug target, with several small-molecule inhibitors under development. Additionally, understanding the molecular mechanisms by which MELK influences tumorigenesis may provide valuable insights for novel cancer treatment strategies. The ongoing exploration of MELK's biological functions underscores the need for comprehensive studies that not only elucidate its role in cancer but also pave the way for targeted therapies aimed at inhibiting MELK activity in various malignancies.
