Analytical Data
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基因名
PPP1R14C
- Application
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别名
PPP1R14C; KEPI; Protein phosphatase 1 regulatory subunit 14C; Kinase-enhanced PP1 inhibitor; PKC-potentiated PP1 inhibitory protein; Serologically defined breast cancer antigen NY-BR-81
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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
Q8TAE6
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表达区间
2-165 aa
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氨基酸序列
SVATGSSET AGGASGGGAR VFFQSPRGGA GGSPGSSSGS GSSREDSAPV ATAAAAGQVQ QQQQRRHQQG KVTVKYDRKE LRKRLVLEEW IVEQLGQLYG CEEEEMPEVE IDIDDLLDAD SDEERASKLQ EALVDCYKPT EEFIKELLSR IRGMRKLSPP QKKSV
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分子量
17.8 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
PPP1R14C, a member of the protein phosphatase 1 regulatory subunit family, plays a crucial role in modulating the activity of protein phosphatase 1 (PP1), an essential enzyme involved in various cellular processes, including cell division, muscle contraction, and neuronal signaling. The regulation of PP1 by its regulatory subunits is critical for maintaining cellular homeostasis and orchestrating cellular responses. Specifically, PPP1R14C has been implicated in the regulation of smooth muscle contraction and may influence vascular function. Recent studies have focused on the potential therapeutic implications of manipulating PPP1R14C activity, particularly in the context of cardiovascular diseases and smooth muscle-related disorders. With advances in recombinant protein technology, researchers have been generating PPP1R14C recombinant proteins to study its structure, binding interactions, and functional mechanisms. This research aims to elucidate how PPP1R14C regulates PP1 and identify its downstream targets. Understanding the molecular dynamics of PPP1R14C could provide insights into its role in disease pathogenesis and highlight its potential as a drug target for modulating PP1 activity in various pathological conditions. The ongoing exploration of PPP1R14C, through the lens of biochemistry and molecular biology, promises to uncover new therapeutic avenues that harness the power of regulating phosphatase activity in cells.
