Analytical Data
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基因名
CRAT
- Application
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别名
CRAT；CAT1；Carnitine O-acetyltransferase
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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
P43155
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表达区间
1-626aa
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氨基酸序列
MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE WWLKTAYLQY RQPVVIYSSP GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK VMIDNETLPV EYLGGKPLCM NQYYQILSSC RVPGPKQDTV SNFSKTKKPP THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS LQTNKEPVGI LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP IVTLLDYVIE YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK AMDDSSVTEH QKVELLRKAV QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD TSYAIAMHFH LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA ARLAHYLEKA LLDMRALLQS HPRAKL
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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
CRAT (Carnitine O-Octanoyltransferase) is an enzyme involved in the carnitine shuttle, which plays a critical role in the transport of fatty acids into mitochondria for oxidation and energy production. Research on CRAT has gained prominence due to its implications in various metabolic disorders, including obesity, type 2 diabetes, and cardiovascular diseases. Understanding the structure and function of CRAT can provide insights into the regulatory mechanisms of fatty acid metabolism, potentially leading to novel therapeutic strategies. Recent studies have focused on the recombinant expression of CRAT to investigate its enzymatic activity, stability, and interaction with substrates. By utilizing recombinant DNA technology, researchers can produce CRAT in sufficient quantities for in vitro assays and structural analysis, allowing for a better understanding of its catalytic properties. Moreover, alterations in the CRAT gene have been linked to metabolic dysregulation, highlighting the importance of studying CRAT not only as a metabolic enzyme but also as a potential biomarker for metabolic diseases. This research could pave the way for developing targeted interventions aimed at modulating CRAT activity to combat obesity and related metabolic conditions, addressing a pressing issue in modern healthcare. Overall, investigating CRAT as a recombinant protein could yield significant advancements in metabolic research and therapeutic development.
