Analytical Data
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Gene name
ADAMTS9
- Application
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Alternative Names
ADAMTS9；KIAA1312；A disintegrin and metalloProteinase with thrombospondin motifs 9
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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
Q9P2N4
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Expression Region
293-643aa
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AA Sequence
RFVEVLVVADNRMVSYHGENLQHYILTLMSIVASIYKDPSIGNLINIVIVNLIVIHNEQDGPSISFNAQTTLKNFCQWQHSKNSPGGIHHDTAVLLTRQDICRAHDKCDTLGLAELGTICDPYRSCSISEDSGLSTAFTIAHELGHVFNMPHDDNNKCKEEGVKSPQHVMAPTLNFYTNPWMWSKCSRKYITEFLDTGYGECLLNEPESRPYPLPVQLPGILYNVNKQCELIFGPGSQVCPYMMQCRRLWCNNVNGVHKGCRTQHTPWADGTECEPGKHCKYGFCVPKEMDVPVTDGSWGSWSPFGTCSRTCGGGIKTAIRECNRPEPKNGGKYCVGRRMKFKSCNTEPCL
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Molecular Weight
46.8 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
ADAMTS9, a member of the A Disintegrin and Metalloproteinase with Thrombospondin Motifs (ADAMTS) family, has garnered significant attention in recent biomedical research due to its pivotal role in various physiological and pathological processes. This enzymatic protein is primarily involved in the regulation of extracellular matrix (ECM) components, particularly in the cleavage of aggrecan, a key proteoglycan in cartilage. Dysregulation of ADAMTS9 has been implicated in several conditions, including osteoarthritis, cancer progression, and cardiovascular diseases. As a result, understanding the functional mechanisms and molecular pathways associated with ADAMTS9 becomes critical for potential therapeutic applications. The generation of recombinant ADAMTS9 protein provides a valuable tool for researchers to dissect its role in ECM dynamics and to explore its interactions with other matrix components. Moreover, investigating the structural characteristics of ADAMTS9 through recombinant technology could lead to insights into its enzymatic activity and regulatory mechanisms. This research could pave the way for the development of targeted therapies aimed at modulating ADAMTS9 activity, thereby offering new strategies to combat diseases linked to ECM dysregulation. In summary, the study of recombinant ADAMTS9 protein not only enhances our understanding of its biological functions but also holds promise for novel interventions in various health conditions stemming from ECM disturbances.
