Analytical Data
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基因名
AGRN
- Application
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别名
AGRN;AGRIN;Agrin
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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
O00468
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表达区间
1868-2065aa
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氨基酸序列
VDTLAFDGRTFVEYLNAVTESELANEIPVPETLDSGALHSEKALQSNHFELSLRTEATQGLVLWSGKATERADYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPKAYGTGFVGCLRDVVVGRHPLHLLEDAVTKPELRPC
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分子量
27.3 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
AGRN, or agrin, is a proteoglycan primarily known for its role in neuromuscular junction (NMJ) formation and maintenance. As a key component of the basal lamina, AGRN plays a crucial role in the clustering of acetylcholine receptors at the NMJ, facilitating effective synaptic transmission. Research into AGRN has expanded beyond the NMJ, uncovering its involvement in various cellular processes, such as synaptic plasticity and cellular signaling. Its potential implications in neurological disorders, including myasthenia gravis and spinal muscular atrophy, have prompted extensive studies into its structure and function. Additionally, the exploration of recombinant AGRN proteins has gained significant attention due to their promising applications in regenerative medicine and therapeutics. Understanding the molecular mechanisms underlying AGRN's function through recombinant approaches can lead to innovative strategies for treating neuromuscular diseases. Furthermore, because of its intricate interactions with other proteins and the extracellular matrix, the study of recombinant AGRN allows researchers to dissect its roles in cellular communication and tissue organization. This growing body of research underscores the significance of AGRN not only as a fundamental component of neuromuscular physiology but also as a potential target for novel therapeutic interventions.












