Analytical Data
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基因名
SHMT1
- Application
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别名
Serine Hydroxymethyltransferase Cytosolic; SHMT; Glycine Hydroxymethyltransferase; Serine Methylase; SHMT1
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种属
Human
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表达系统
HEK293
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标签
C-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
AAH07979.1
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表达区间
M3-F483
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氨基酸序列
MPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASFFPLPGLPDF
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蛋白长度
Full Length of Mature Protein
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分子量
55.0 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
SHMT1 (Serine Hydroxymethyltransferase 1) is a vital enzyme involved in the folate and amino acid metabolism, playing a crucial role in the conversion of serine to glycine and the interconversion of tetrahydrofolate derivatives. This enzyme is particularly significant in cellular processes like DNA synthesis and repair, which are essential for normal cell function and proliferation. Dysregulation or mutations in SHMT1 have been associated with various diseases, including cancer, demonstrating its potential as a therapeutic target. The recombinant expression of SHMT1 allows for the detailed study of its structure, function, and regulation, providing insights into its role in metabolic pathways and disease mechanisms. By producing SHMT1 in a controlled laboratory setting, researchers can investigate its kinetics, substrate specificity, and interaction with other biomolecules. Additionally, understanding its enzymatic properties may lead to the development of small molecule inhibitors or modulators, offering new avenues for treatment strategies in conditions where SHMT1 activity is altered. This research underscores the importance of SHMT1 in metabolic regulation and highlights the potential of recombinant proteins in elucidating biological functions and therapeutic applications.
