Analytical Data
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基因名
ADAMTS9
- Application
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别名
ADAMTS9;KIAA1312;A disintegrin and metalloProteinase with thrombospondin motifs 9
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9P2N4
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表达区间
293-643aa
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氨基酸序列
RFVEVLVVADNRMVSYHGENLQHYILTLMSIVASIYKDPSIGNLINIVIVNLIVIHNEQDGPSISFNAQTTLKNFCQWQHSKNSPGGIHHDTAVLLTRQDICRAHDKCDTLGLAELGTICDPYRSCSISEDSGLSTAFTIAHELGHVFNMPHDDNNKCKEEGVKSPQHVMAPTLNFYTNPWMWSKCSRKYITEFLDTGYGECLLNEPESRPYPLPVQLPGILYNVNKQCELIFGPGSQVCPYMMQCRRLWCNNVNGVHKGCRTQHTPWADGTECEPGKHCKYGFCVPKEMDVPVTDGSWGSWSPFGTCSRTCGGGIKTAIRECNRPEPKNGGKYCVGRRMKFKSCNTEPCL
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分子量
46.8 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.












