Analytical Data
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基因名
ADAMTS13
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简介
The ADAMTS13 protein, a metalloproteinase, has a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 motif. It cleaves von Willebrand Factor and defects in this gene cause thrombotic thrombocytopenic purpura. Alternative splicing generates multiple transcript variants. ADAMTS13 is broadly expressed in various tissues, including the liver, testis, and 24 other tissues. ADAMTS13 Protein, Human (CHO, His) is the recombinant human-derived ADAMTS13, expressed by CHO, with C-10*His labeled tag. The total length of ADAMTS13 Protein, Human (CHO, His) is 655 a.a..
- Application
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别名
ADAM-TS 13; ADAM-TS13; ADAMTS-13von Willebrand factor-cleaving protease; vWF-CP; vWF-cleaving protease; A Disintegrin-like and Metalloproteinase Domain with Thrombospondin Motifs 13
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种属
Human
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表达系统
CHO
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标签
C-10*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
NP_620594
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表达区间
Q34-W688
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氨基酸序列
QQSCLQALEPQAVSSYLSPGAPLKGRPPSPGFQRQRQRQRRAAGGILHLELLVAVGPDVFQAHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWSQTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAPGSGCGPSGHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVWDPPRPQPGSAGHPPDAQPGLYYSANEQCRVAFGPKAVACTFAREHLDMCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKGRCRSLVELTPIAAVHGRWSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACEKTQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLSLCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTCSPRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVRIGGRYVVAGKMSISPNTTYPSLLEDGRVEYRVALTEDRLPRLEEIRIWGPLQEDADIQVYRRYGEEYGNLTRPDITFTYFQPKPRQAWVW
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蛋白长度
Partial
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分子量
90 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
ADAMTS13 (A Disintegrin and Metalloproteinase with Thrombospondin Motifs 13) is a critical enzyme responsible for the cleavage of von Willebrand factor (VWF), a key player in platelet adhesion and aggregation during hemostasis. Dysregulation or deficiency of ADAMTS13 has been linked to thrombotic thrombocytopenic purpura (TTP), a severe condition characterized by the formation of microclots that can lead to organ damage and potentially life-threatening complications. The recombinant form of ADAMTS13 has emerged as a promising therapeutic candidate aimed at restoring normal VWF processing and mitigating the pathological consequences of its deficiency. Research into the recombinant protein focuses on its production, purification, and functional characterization to ensure that it retains the necessary enzymatic activity to effectively regulate VWF levels in the bloodstream. Studies have shown that administering recombinant ADAMTS13 can help reverse the symptoms of TTP and prevent exacerbation of the condition. Additionally, ongoing investigations are exploring its potential applications in other thrombotic disorders, highlighting the enzyme's importance in maintaining vascular homeostasis. As such, the development of recombinant ADAMTS13 holds significant potential not only for treating patients with TTP but also for broader applications in managing various vascular pathologies associated with dysregulated thrombus formation. This research underscores the critical role of enzyme therapy in advancing treatment strategies for thrombotic conditions.
