Analytical Data
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基因名
SYF2
- Application
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别名
CBPIN; CCNDBP1 interactor; CCNDBP1-interactor; DKFZp564O2082; fSAP29; Functional spliceosome associated protein 29; GCIP interacting protein p29; GCIPIP; NTC31; P29; Pre mRNA splicing factor SYF2; Pre-mRNA-splicing factor syf2; syf2; SYF2 homolog; SYF2 homolog RNA splicing factor (S. cerevisiae); SYF2 homolog RNA splicing factor; SYF2_HUMAN
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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
O95926
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表达区间
2-243 aa
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氨基酸序列
AAIAASEVL VDSAEEGSLA AAAELAAQKR EQRLRKFREL HLMRNEARKL NHQEVVEEDK RLKLPANWEA KKARLEWELK EEEKKKECAA RGEDYEKVKL LEISAEDAER WERKKKRKNP DLGFSDYAAA QLRQYHRLTK QIKPDMETYE RLREKHGEEF FPTSNSLLHG THVPSTEEID RMVIDLEKQI EKRDKYSRRR PYNDDADIDY INERNAKFNK KAERFYGKYT AEIKQNLERG TAV
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分子量
28.7 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
SYF2 protein, a member of the splicing factor family, plays a significant role in the regulation of RNA splicing and cellular gene expression. Its involvement in essential biological processes has garnered attention in recent years, particularly concerning its implications in various diseases, including cancer. Research has shown that alterations in the expression and function of splicing factors like SYF2 can lead to aberrant splicing patterns, resulting in the production of dysfunctional proteins that contribute to tumorigenesis and other pathological conditions. Understanding the structure and function of SYF2 at the molecular level is crucial for elucidating its role in splicing regulation and cellular homeostasis. Recent advancements in recombinant protein technology have enabled the production and characterization of SYF2, facilitating in-depth studies of its biochemical properties and interaction with other splicing components. This research not only enhances our understanding of splicing mechanisms but also opens avenues for therapeutic interventions targeting splicing dysregulation in diseases where SYF2 is implicated. Thus, the study of SYF2 recombinant protein is pivotal for both basic biological research and potential clinical applications, highlighting its importance in the field of molecular biology and medicine.
