Analytical Data
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基因名
GALNT12
- Application
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别名
Colorectal cancer susceptibility to 1; CRCS1; FLJ21212; GalNAc T12; GalNAc-T12; GalNAcT12; GALNT 12; Galnt12; GLT12_HUMAN; Polypeptide GalNAc transferase 12; Polypeptide N acetylgalactosaminyltransferase 12; Polypeptide N-acetylgalactosaminyltransferase 12; pp GaNTase 12; pp-GaNTase 12; Protein UDP acetylgalactosaminyltransferase 12; Protein-UDP acetylgalactosaminyltransferase 12
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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
Q8IXK2
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表达区间
1-272aa
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氨基酸序列
MAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSHVGHVFPKQAPYSRNKALANSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKLQCKDFKWFLETVYPELHVPEDRPGSFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCHGMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCEETAPENQKFILQEDGSLFHEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKERML
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分子量
55.66 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
GALNT12, a member of the polypeptide N-acetylgalactosaminyltransferase family, has garnered significant interest in recent years due to its potential role in glycosylation and its implications in cancer biology. Glycosylation, the process of adding sugar molecules to proteins, is crucial for various cellular functions, including cell signaling, adhesion, and immune response. GALNT12 specifically catalyzes the addition of N-acetylgalactosamine (GalNAc) to serine and threonine residues on target proteins, which is an essential step in the synthesis of O-linked glycoproteins. Aberrant expression and activity of GALNT12 have been linked to several types of cancers, including colorectal cancer, suggesting that it may play a role in tumor progression and metastasis. Understanding the structure and function of GALNT12, including its substrate specificity and regulatory mechanisms, can provide insights into its biological significance and therapeutic potential. Additionally, the production and characterization of recombinant GALNT12 protein is vital for elucidating its enzymatic properties and for exploring its role in glycosylation pathways. As researchers continue to investigate the function of GALNT12, the findings may reveal novel biomarkers for cancer diagnosis and targets for therapeutic intervention, highlighting the importance of this enzyme in both fundamental biochemistry and clinical applications.
