Analytical Data
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Gene name
EXT2
- Application
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Alternative Names
SOTV; Multiple exostoses protein 2; Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q93063
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Expression Region
Pro47~Phe253
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Molecular Weight
30kDa
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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
EXT2, or exostosin-2, is a gene that plays a crucial role in the synthesis of heparan sulfate, a glycosaminoglycan essential for various biological processes including cell signaling, growth, and extracellular matrix formation. Mutations in EXT2 are associated with multiple hereditary exostoses (MHE), a genetic disorder characterized by the formation of benign bone tumors and a predisposition to osteosarcoma. Research into EXT2 recombinant proteins has gained momentum as scientists aim to understand its functional mechanisms and interactions within biochemical pathways. The study of EXT2 reconstituted in vitro offers insights into its role in heparan sulfate biosynthesis, which is critical for normal cellular functions and the development of skeletal tissues. By creating and characterizing recombinant EXT2, researchers aspire to unravel the pathways through which EXT2 mutations lead to MHE and related disorders. Additionally, exploring EXT2's interaction with other proteins involved in glycosaminoglycan synthesis can provide further clarity on its significance in both health and disease. This research not only helps in understanding the molecular underpinnings of MHE but also paves the way for potential therapeutic strategies targeting the dysregulated pathways associated with EXT2 mutations. The ongoing investigations into EXT2's structure and function are vital for developing options for prevention and treatment of conditions stemming from its dysfunction.
