Analytical Data
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基因名
T-PA
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简介
The T-PA protein encoded by this gene is a secreted serine protease that converts plasminogen into plasmin, a key enzyme involved in tissue remodeling and cell migration. The proteolytic process produces heavy and light chains, forming heterodimeric enzymes. T-PA Protein, Human (HEK293) is the recombinant human-derived T-PA protein, expressed by HEK293 , with tag free.
- Application
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别名
T-PA; TPA; t-plasminogen activator; Tissue plasminogen activator
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种属
Human
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表达系统
HEK293
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标签
Tag Free
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
NP_000921.1
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表达区间
I311-P562
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氨基酸序列
IKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP
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蛋白长度
Partial
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分子量
35 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
Tissue Plasminogen Activator (T-PA) is a serine protease produced by endothelial cells, playing a crucial role in the fibrinolytic system by converting plasminogen into plasmin, which digests fibrin and facilitates clot breakdown. The study of T-PA gained momentum in the 1980s when its therapeutic potential for treating thrombotic disorders, such as myocardial infarction and stroke, became apparent. Scientists began exploring the possibility of recombinant T-PA, allowing for large-scale production and more efficient treatment protocols. The introduction of recombinant DNA technology enabled the expression of the T-PA gene in various host cells, significantly advancing our understanding of its structure and function. Over the years, numerous studies have focused on optimizing the production and efficacy of T-PA, leading to the development of modified versions with improved pharmacokinetics and reduced side effects. This research has established T-PA as a gold standard in thrombolytic therapy. Furthermore, ongoing investigations into its biological properties and potential applications beyond thrombolysis, including implications in cancer therapy and wound healing, continue to expand the horizons of T-PA research, making it a pivotal protein in both clinical and biomedical studies.
