Analytical Data
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基因名
GAMT
- Application
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别名
PIG2; TP53I2; Guanidinoacetate Methyltransferase; Guanidinoacetate Transmethylase; Methionine-Guanidinoacetic Transmethylase; Guanidoacetate Methyltransferase
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种属
Mouse
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
O35969
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表达区间
Ser2~His236
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分子量
30kDa
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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
GAMT (guanidinoacetate N-methyltransferase) is an important enzyme involved in the biosynthesis of creatine, which plays a crucial role in energy metabolism within muscle and brain tissues. Research into GAMT has garnered attention due to its connection to various metabolic disorders, particularly GAMT deficiency, a rare genetic condition that leads to elevated levels of guanidinoacetate and subsequently causes neurological impairment. Understanding the structure and function of GAMT through recombinant protein studies is vital for elucidating its role in cellular metabolism and the pathogenesis of related disorders. Recombinant GAMT proteins, produced through techniques such as bacterial expression systems, can be instrumental for investigating the enzyme’s kinetic properties, substrate specificity, and regulatory mechanisms. Furthermore, insights gained from such studies can pave the way for potential therapeutic interventions, including enzyme replacement strategies or small molecule modulators. The ongoing research into GAMT recombinant proteins not only enhances our fundamental understanding of this enzyme but also holds promise for addressing the clinical challenges faced by individuals with GAMT deficiency and similar metabolic conditions.
