Analytical Data
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基因名
MAZ
- Application
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别名
Pur-1;Purine-binding transcription factor;Serum amyloid A-activating factor-1 (SAF-1);Transcription factor Zif87ZF87;Zinc finger protein 801
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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
P56270
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表达区间
1-477aa
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氨基酸序列
MFPVFPCTLLAPPFPVLGLDSRGVGGLMNSFPPPQGHAQNPLQVGAELQSRFFASQGCAQSPFQAAPAPPPTPQAPAAEPLQVDLLPVLAAAQESAAAAAAAAAAAAAVAAAPPAPAAASTVDTAALKQPPAPPPPPPPVSAPAAEAAPPASAATIAAAAATAVVAPTSTVAVAPVASALEKKTKSKGPYICALCAKEFKNGYNLRRHEAIHTGAKAGRVPSGAMKMPTMVPLSLLSVPQLSGAGGGGGEAGAGGGAAAVAAGGVVTTTASGKRIRKNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSYHVRSHDGAVHKPYNCSHCGKSFSRPDHLNSHVRQVHSTERPFKCEKCEAAFATKDRLRAHTVRHEEKVPCHVCGKMLSSAYISDHMKVHSQGPHHVCELCNKGTGEVCPMAAAAAAAAAAAAAAVAAPPTAVGSLSGAEGVPVSSQPLPSQPW
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分子量
52.1 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
The MAZ (Myc-Associated Zinc Finger Protein) is a crucial transcription factor primarily involved in regulating the expression of various genes associated with cellular growth, differentiation, and apoptosis. Research on MAZ has gained significant attention due to its pivotal role in oncogenesis and its potential as a therapeutic target in cancer treatment. Elevated levels of MAZ have been correlated with several malignancies, including breast, prostate, and colorectal cancers, indicating its contribution to tumor progression and poor prognosis. Moreover, MAZ interacts with the c-Myc pathway, which is a well-known regulator of cell proliferation and metabolism. Understanding the structure and functional dynamics of MAZ, particularly its restructured protein forms, provides insights into the mechanistic pathways by which it influences gene expression. Recent studies employing advanced techniques such as X-ray crystallography, NMR spectroscopy, and cryo-electron microscopy have revealed the structural intricacies of MAZ, facilitating the identification of potential small molecule inhibitors. Additionally, elucidating the protein's interaction networks has shed light on its multifaceted role in cancer biology. This ongoing research aims to develop novel strategies for targeting MAZ's activity, which could lead to innovative therapeutic approaches in oncology, enhancing treatment efficacy and patient outcomes. The continued exploration of MAZ's function and its restructured protein forms is expected to yield significant advances in our understanding of cancer mechanisms and pave the way for future clinical applications.
