Recombinant Human ATF6 Protein, N-His-SUMO

Reference: YHD31203
Product nameRecombinant Human ATF6 Protein, N-His-SUMO
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight21.15 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeSer548-Asp622
Aliases /SynonymsATF6-alpha, Cyclic AMP-dependent transcription factor ATF-6 alpha, cAMP-dependent transcription factor ATF-6 alpha, ATF6, Activating transcription factor 6 alpha
ReferenceYHD31203
NoteFor research use only.

Description of Recombinant Human ATF6 Protein, N-His-SUMO

Introduction

Recombinant proteins have become essential tools in the fields of biotechnology and medicine due to their ability to mimic naturally occurring proteins and perform specific functions. One such protein is the Recombinant Human ATF6 Protein, which plays a crucial role in cellular stress response. In this article, we will dive into the structure, activity, and application of this important protein.

Structure of Recombinant Human ATF6 Protein

The ATF6 protein is a transcription factor that belongs to the activating transcription factor (ATF) family. It is encoded by the ATF6 gene and is found in the endoplasmic reticulum (ER) of cells. The recombinant form of this protein is produced through genetic engineering techniques, where the gene is inserted into a suitable expression vector and expressed in a host organism, typically bacteria or yeast.

The recombinant human ATF6 protein has a molecular weight of approximately 90 kDa and is composed of 670 amino acids. It consists of a DNA-binding domain, a leucine zipper domain, and a transmembrane domain. The DNA-binding domain is responsible for binding to specific DNA sequences, while the leucine zipper domain allows for dimerization with other ATF6 proteins. The transmembrane domain anchors the protein to the ER membrane.

Activity of Recombinant Human ATF6 Protein

The main function of ATF6 is to regulate the unfolded protein response (UPR) in the ER. This response is activated when the ER is under stress, such as an accumulation of misfolded proteins. The recombinant human ATF6 protein is able to bind to specific DNA sequences and activate the expression of genes involved in the UPR, thus promoting the proper folding and processing of proteins in the ER.

Additionally, ATF6 has been shown to have anti-apoptotic properties, meaning it can prevent cell death. This is important in situations where cells are under stress and at risk of dying, such as during a viral infection or exposure to toxins.

Application of Recombinant Human ATF6 Protein

The recombinant human ATF6 protein has various applications in both research and medicine. One of its main uses is in the study of the UPR and its role in cellular stress response. By manipulating the expression of ATF6, researchers can better understand the mechanisms of the UPR and its impact on various diseases.

Furthermore, the recombinant protein has potential therapeutic applications. As mentioned earlier, ATF6 has anti-apoptotic properties, making it a potential target for drug development in diseases where cell death is a major factor, such as neurodegenerative disorders and certain types of cancer.

Another potential application is in the production of biologics, such as therapeutic antibodies, which require proper folding and processing in the ER. By using recombinant human ATF6, researchers can optimize the production of these biologics and improve their efficacy.

Conclusion

The recombinant human ATF6 protein is a crucial player in the cellular stress response and has various applications in research and medicine. Its structure, activity, and potential therapeutic uses make it a valuable tool in the biotechnology and pharmaceutical industries. As our understanding of the UPR and its role in disease continues to grow, the importance of this protein will only increase.

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