Analytical Data
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基因名
CTH
- Application
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别名
CTH;Cystathionine gamma-lyase
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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
P32929
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表达区间
1-405aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS
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分子量
47 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
CTH recombinant proteins have garnered significant attention in recent years due to their potential applications in various fields, including medicine, biotechnology, and molecular biology. CTH, or cystathionine gamma-lyase, is an enzyme involved in the transsulfuration pathway, which plays a crucial role in the metabolism of sulfur-containing amino acids. This pathway is essential for the synthesis of important biomolecules, such as cysteine and hydrogen sulfide, both of which are vital for cellular function and signaling. Disruptions in CTH activity have been linked to various diseases, including cardiovascular disorders, neurodegenerative diseases, and cancer, making it a promising target for therapeutic interventions. The ability to produce CTH as a recombinant protein allows for detailed studies of its structure, function, and regulation, facilitating the development of novel diagnostic and therapeutic strategies. Additionally, understanding the biochemical properties of CTH can aid in the exploration of its role in cellular homeostasis and disease progression. Research into CTH recombinant proteins not only enhances our fundamental understanding of enzymatic processes but also opens new avenues for innovative treatments that harness the biological activities of this important enzyme. As such, ongoing studies focus on optimizing the production and characterization of CTH recombinant proteins, aiming to unlock their full potential in both scientific research and clinical applications.
