Analytical Data
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基因名
CHAD
- Application
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别名
Cartilage leucine rich Protein; Cartilage leucine-rich Protein; Chad; CHAD_HUMAN; Chondroadherin; Chondroadherin proteoglycan; SLRR4A
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q13111
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表达区间
1-395aa
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氨基酸序列
MVRPMLLLSLGLLAGLLPALAACPQNCHCHSDLQHVICDKVGLQKIPKVSEKTKLLNLQRNNFPVLAANSFRAMPNLVSLHLQHCQIREVAAGAFRGLKQLIYLYLSHNDIRVLRAGAFDDLTELTYLYLDHNKVTELPRGLLSPLVNLFILQLNNNKIRELRAGAFQGAKDLRWLYLSENALSSLQPGALDDVENLAKFHVDRNQLSSYPSAALSKLRVVEELKLSHNPLKSIPDNAFQSFGRYLETLWLDNTNLEKFSDGAFLGVTTLKHVHLENNRLNQLPSNFPFDSLETLALTNNPWKCTCQLRGLRRWLEAKASRPDATCASPAKFKGQHIRDTDAFRSCKFPTKRSKKAGRH
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分子量
65.89 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
Research on CHAD (Cationic Histone-Associated Domain) recombinant proteins has gained significant attention due to their potential roles in various biological processes. CHAD proteins, characterized by their interaction with histones and involvement in chromatin remodeling, play critical roles in regulating gene expression and cellular functions. These proteins are implicated in several physiological and pathological conditions, including cancer, where epigenetic modifications can lead to tumor progression. The ability to produce recombinant CHAD proteins allows for detailed structural and functional analyses, enabling researchers to explore their mechanisms of action and interactions within the cellular environment. By employing advanced techniques such as site-directed mutagenesis and protein crystallography, scientists aim to elucidate the structural basis of CHAD function, which may reveal new therapeutic targets for interventions in diseases linked to dysregulated gene expression. Additionally, the study of CHAD recombinant proteins can also provide insights into the evolutionary conservation of protein interactions and their significance across different organisms. The continued investigation into CHAD proteins not only enhances our understanding of fundamental biological processes but also paves the way for innovative strategies in biotechnology and medicine.
