Analytical Data
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基因名
PHKG2
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简介
As the catalytic subunit of phosphorylase b kinase (PHK), PHKG2 plays a crucial role in the neural and hormonal regulation of glycogenolysis (glycogen breakdown) by phosphorylating and activating glycogen phosphorylase. Furthermore, PHKG2 has a potential role in regulating testicular glycogenolysis. PHKG2 Protein, Human (sf9, GST) is the recombinant human-derived PHKG2 protein, expressed by sf9 insect cells , with N-GST labeled tag.
- Application
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别名
PHKG2; Phosphorylase b kinase gamma catalytic chain; liver/testis isoform; PHK-gamma-LT; PHK-gamma-T; PSK-C3; Phosphorylase kinase subunit gamma-2
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种属
Human
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表达系统
Baculovirus
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标签
N-GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P15735
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表达区间
T2-G406
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蛋白长度
Partial
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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
PHKG2, or phosphorylase kinase gamma 2, is a critical regulatory enzyme involved in glycogen metabolism. It's primarily expressed in skeletal muscle and plays a significant role in the activation of glycogen phosphorylase, which in turn controls the breakdown of glycogen into glucose during periods of energy demand. Understanding the molecular mechanisms governing PHKG2’s activity is crucial due to its implications in metabolic disorders such as diabetes and muscle-related diseases. Recent studies have also suggested that mutations in the PHKG2 gene can lead to glycogen storage diseases, affecting muscle function and overall metabolism. Research on PHKG2 recombinant proteins has gained momentum as it offers insights into its structure-function relationship, enzymatic regulation, and potential therapeutic applications. By utilizing recombinant technology, researchers can produce large quantities of PHKG2 for biochemical assays, structural studies, and potential drug development, enhancing our understanding of its role in health and disease. The elucidation of PHKG2’s function may pave the way for innovative strategies to manage metabolic disorders and improve muscle health.
