Analytical Data
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Gene name
FLJ23356
- Application
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Alternative Names
FLJ23356; MDDGA12; POMK; Probable inactive protein kinase-like protein SgK196; Protein kinase like protein SgK196; Protein kinase-like protein SgK196; Protein O-mannose kinase; SG196_HUMAN; SGK196; Sugen kinase 196
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H5K3
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Expression Region
1-350aa
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AA Sequence
MEKQPQNSRRGLAPREVPPAVGLLLIMALMNTLLYLCLDHFFIAPRQSTVDPTHCPYGHFRIGQMKNCSPWLSCEELRTEVRQLKRVGEGAVKRVFLSEWKEHKVALSQLTSLEMKDDFLHGLQMLKSLQGTHVVTLLGYCEDDNTMLTEYHPLGSLSNLEETLNLSKYQNVNTWQHRLELAMDYVSIINYLHHSPVGTRVMCDSNDLPKTLSQYLLTSNFSILANDLDALPLVNHSSGMLVKCGHRELHGDFVAPEQLWPYGEDVPFHDDLMPSYDEKIDIWKIPDISSFLLGHIEGSDMVRFHLFDIHKACKSQTPSERPTAQDVLETYQKVLDTLRDAMMSQAREML
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Molecular Weight
66.4 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
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Protein Description
The FLJ23356 protein, a member of the growing family of recombinant proteins, has generated considerable interest in the fields of molecular biology and biotechnology due to its potential applications in therapeutic development and disease understanding. Initially identified through genomic databases, FLJ23356 has been linked to various cellular functions, including cell signaling and metabolic processes. Recent studies have highlighted its role in specific cellular pathways, suggesting that abnormalities in FLJ23356 expression may be implicated in certain diseases, including cancer and metabolic disorders. Research into its structure and function aims to elucidate its biological significance and interactions at the molecular level. Furthermore, recombinant production techniques have enabled scientists to generate purified FLJ23356 protein, facilitating in vitro studies that assess its enzymatic activity, binding characteristics, and interaction with other biomolecules. As a result, understanding the properties of FLJ23356 may not only provide insights into its physiological roles but also pave the way for its potential use as a biomarker or therapeutic target. Overall, research into FLJ23356 is an integral part of unlocking new advancements in protein engineering and personalized medicine, thereby expanding the toolkit available for addressing complex biological questions and improving health outcomes.











