Analytical Data
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Gene name
ADAMTS14
- Application
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Alternative Names
ADAMTS14；A disintegrin and metalloProteinase with thrombospondin motifs 14
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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
Q8WXS8
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Expression Region
253-555aa
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AA Sequence
HAKPGSYSIEVLLVVDDSVVRFHGKEHVQNYVLTLMNIVDEIYHDESLGVHINIALVRLIMVGYRQSLSLIERGNPSRSLEQVCRWAHSQQRQDPSHAEHHDHVVFLTRQDFGPSGYAPVTGMCHPLRSCALNHEDGFSSAFVIAHETGHVLGMEHDGQGNGCADETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSYDCLLDDPFDPAWPQPPELPGINYSMDEQCRFDFGSGYQTCLAFRTFEPCKQLWCSHPDNPYFCKTKKGPPLDGTECAPGKWCFKGHCIWKSPEQTYGQDGGW
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Molecular Weight
40.2 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
ADAMTS14 (A Disintegrin and Metalloproteinase with Thrombospondin Motifs 14) is a member of the ADAMTS family of extracellular matrix proteins, which play pivotal roles in various physiological and pathological processes through their ability to cleave proteoglycans and modulate interactions within the extracellular matrix. This protein has garnered attention due to its potential implications in several diseases, particularly in the context of inflammatory conditions and cancer. Research has indicated that ADAMTS14 is involved in the regulation of cartilage homeostasis and may contribute to the pathogenesis of osteoarthritis. Furthermore, studies have shown that it can influence tumor progression by altering the tumor microenvironment and affecting cell migration. The recombinant production of ADAMTS14 has emerged as a valuable tool to elucidate its biological function and therapeutic potential. By enabling large-scale synthesis and purification of this protein, researchers aim to investigate its enzymatic activity, substrate specificity, and interactions with other matrix components. Understanding the molecular mechanisms underlying ADAMTS14 activity may provide insights into its role in disease processes and identify potential targets for therapeutic intervention. The exploration of ADAMTS14 as a recombinantly produced protein is thus a critical area of research, contributing to a broader understanding of extracellular matrix dynamics and its implications in health and disease.
