Analytical Data
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基因名
R497Q
- Application
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别名
R497Q；
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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
P00750
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表达区间
36-562aa
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氨基酸序列
SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTQSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP
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分子量
62.9 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
The R497Q variant of the receptor protein tyrosine phosphatase (RPTP) has emerged as a significant focus in the field of molecular biology and genetics due to its potential implications in various diseases, particularly those related to disrupted cell signaling pathways. Receptor protein tyrosine phosphatases play critical roles in regulating cellular communication, differentiation, and metabolism, and mutations in these proteins can lead to pathological conditions, including cancers and neurological disorders. The R497Q mutation is of particular interest as it alters the enzymatic activity of RPTP, potentially affecting its ability to modulate key signaling cascades. Research surrounding this recombinant protein focuses on elucidating the structural changes induced by the R497Q mutation, understanding its biological consequences, and exploring therapeutic approaches that could mitigate its deleterious effects. By employing techniques such as site-directed mutagenesis, protein expression systems, and biochemical assays, scientists aim to uncover the relationship between the R497Q variant and its biological functions, laying the groundwork for future studies that could improve our understanding of related diseases. This research not only advances basic science but also holds promise for the development of targeted therapies that could correct or compensate for the dysfunctional signaling caused by the mutation.
