Analytical Data
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基因名
GALNTL5
- Application
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别名
GALNTL5; GALNT15Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5; Polypeptide GalNAc transferase 15; GalNAc-T15; pp-GaNTase 15; Protein-UDP acetylgalactosaminyltransferase 15; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 15
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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
Q7Z4T8
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表达区间
1-443aa
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氨基酸序列
MRNAIIQGLFYGSLTFGIWTALLFIYLHHNHVSSWQKKSQEPLSAWSPGKKVHQQIIYGSEQIPKPHVIVKRTDEDKAKSMLGTDFNHTNPELHKELLKYGFNVIISRSLGIEREVPDTRSKMRLQKHYPARLPTASIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSPLVRGTFDWNLQFKWDNVFSYEMDGPEGSTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKQTGKPSTIISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRLGCKSFQWYLDNVFPELEASVNSL
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分子量
77.9 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
GALNTL5, a member of the polypeptide N-acetylgalactosaminyltransferase (GALNT) family, plays a crucial role in O-glycosylation, a post-translational modification essential for various biological processes. O-glycosylation is involved in protein stability, cellular signaling, and interactions between cells and their environments. Research into GALNTL5 has gained attention due to its potential implications in cancer biology, as altered glycosylation patterns can contribute to tumor progression and metastasis. Increased expression of GALNTL5 has been linked to certain malignancies, indicating that it may serve as a biomarker for cancer diagnosis and prognosis. Moreover, understanding the enzymatic mechanisms by which GALNTL5 modifies glycoproteins could reveal novel therapeutic targets for treating diseases characterized by aberrant glycosylation. The recombinant production of GALNTL5 enables a detailed investigation of its enzymatic activity and substrate specificity, offering insights into its biological functions and potential applications in biotechnology and medicine. As researchers continue to explore the structure-function relationships of GALNTL5, the discovery of small molecules or modulators to manipulate its activity could pave the way for innovative treatments targeting glycosylation-related disorders. Thus, GALNTL5 represents a significant focus within glycobiology, linking glycosylation to critical physiological and pathological processes.
