Analytical Data
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基因名
ASH2L
- Application
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别名
ASH2-like protein
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种属
Human
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9UBL3
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表达区间
1-534aa
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分子量
76.2 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
ASH2L (Absent, Small, or Homeotic 2-like protein) is a crucial component of the MLL (Mixed-Lineage Leukemia) family of histone methyltransferases, which play essential roles in transcriptional regulation and chromatin remodeling. The study of ASH2L has gained significant attention due to its involvement in various biological processes, including development, cell differentiation, and the maintenance of stem cell properties. Abnormal expression or mutations of ASH2L have been linked to several cancers, particularly acute leukemia, making it a target of interest for understanding tumorigenesis and identifying potential therapeutic strategies. Moreover, ASH2L functions as a cofactor, facilitating the methylation of histone H3 at lysine 4, a modification associated with active gene transcription. This has placed ASH2L at the center of research aimed at elucidating the molecular mechanisms underlying epigenetic regulation. Recent advances in molecular biology techniques have enabled researchers to explore the structural and functional aspects of ASH2L in greater detail, paving the way for innovative approaches in cancer treatment and regenerative medicine. Studying ASH2L and its interactions within the context of various protein complexes is critical to unraveling the complexities of gene regulation and developing targeted therapeutic interventions in malignancies driven by dysregulated epigenetic modifications.
