Analytical Data
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基因名
recQ
- Application
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别名
recQ；RECQ1；RECQL1；ATP-dependent DNA helicase Q1
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种属
E.coli
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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
P15043
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表达区间
1-609aa
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氨基酸序列
MAQAEVLNLE SGAKQVLQET FGYQQFRPGQ EEIIDTVLSG RDCLVVMPTG GGKSLCYQIP ALLLNGLTVV VSPLISLMKD QVDQLQANGV AAACLNSTQT REQQLEVMTG CRTGQIRLLY IAPERLMLDN FLEHLAHWNP VLLAVDEAHC ISQWGHDFRP EYAALGQLRQ RFPTLPFMAL TATADDTTRQ DIVRLLGLND PLIQISSFDR PNIRYMLMEK FKPLDQLMRY VQEQRGKSGI IYCNSRAKVE DTAARLQSKG ISAAAYHAGL ENNVRADVQE KFQRDDLQIV VATVAFGMGI NKPNVRFVVH FDIPRNIESY YQETGRAGRD GLPAEAMLFY DPADMAWLRR CLEEKPQGQL QDIERHKLNA MGAFAEAQTC RRLVLLNYFG EGRQEPCGNC DICLDPPKQY DGSTDAQIAL STIGRVNQRF GMGYVVEVIR GANNQRIRDY GHDKLKVYGM GRDKSHEHWV SVIRQLIHLG LVTQNIAQHS ALQLTEAARP VLRGESSLQL AVPRIVALKP KAMQKSFGGN YDRKLFAKLR KLRKSIADES NVPPYVVFND ATLIEMAEQM PITASEMLSV NGVGMRKLER FGKPFMALIR AHVDGDDEE
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分子量
68 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
RecQ helicases are a family of enzymes essential for maintaining genomic stability and are involved in various DNA metabolic processes, including replication, repair, and recombination. Disturbances in these helicases are linked to several human diseases, including cancer, premature aging syndromes, and genetic disorders such as Bloom syndrome, Werner syndrome, and Rothmund-Thomson syndrome. The RecQ proteins function by unwinding DNA structures, which is crucial for resolving DNA secondary structures and ensuring proper chromosome segregation during cell division. The study of RecQ helicases has gained momentum due to their pivotal role in preventing genomic instability, a hallmark of many malignancies. Researchers aim to elucidate the mechanisms of RecQ action, its interactions with other proteins, and its overall role in cellular processes to better understand its involvement in cancer and other diseases. Furthermore, these studies may offer insights into potential therapeutic strategies that target RecQ helicases for cancer treatment or to ameliorate the effects of associated disorders. Investigating the biochemical properties of RecQ helicases, including their catalytic activities and regulatory mechanisms, has significant implications for both fundamental biology and clinical applications.
