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Brand: ProteoGenix

Recombinant Human ATF6 Protein, N-His-SUMO & C-Strep

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
23.62 kDa

329.00

+ 329 loyalty points
Ala547–Ser632
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Recombinant Human ATF6 Protein, N-His-SUMO & C-Strep

Recombinant Human ATF6 Protein, N-His-SUMO & C-Strep

Product name Recombinant Human ATF6 Protein, N-His-SUMO & C-Strep
Origin species Human
Expression system Prokaryotic expression
Molecular weight 23.62 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°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)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Ala547-Ser632
Aliases /Synonyms ATF6-alpha, Cyclic AMP-dependent transcription factor ATF-6 alpha, cAMP-dependent transcription factor ATF-6 alpha, ATF6, Activating transcription factor 6 alpha
Reference ARO-P12554
Note For research use only.
Molecular Constructor
Ala547–Ser632

Introduction

Recombinant Human ATF6 Protein is a highly specialized protein that plays a crucial role in the cellular stress response. This protein is a key regulator of the unfolded protein response (UPR), a cellular mechanism that is activated in response to the accumulation of misfolded proteins in the endoplasmic reticulum (ER). In this article, we will explore the structure, activity, and applications of this important protein.

Structure of Recombinant Human ATF6 Protein

The ATF6 protein is a transcription factor that belongs to the basic leucine zipper (bZIP) family. It is composed of 670 amino acids and has a molecular weight of approximately 78 kDa. The protein is composed of several functional domains, including a DNA-binding domain, a transmembrane domain, and a cytoplasmic domain.

The DNA-binding domain is responsible for binding to specific DNA sequences in the promoter regions of target genes. The transmembrane domain anchors the protein to the ER membrane, while the cytoplasmic domain is responsible for regulating the activity of the protein.

Activity of Recombinant Human ATF6 Protein

Under normal conditions, ATF6 is present in an inactive form in the ER membrane. However, when the ER is under stress, ATF6 is cleaved by specific enzymes, releasing the cytoplasmic domain into the cytoplasm. This activated form of ATF6 then translocates to the nucleus where it binds to specific DNA sequences and activates the transcription of genes involved in the UPR.

The main function of ATF6 is to upregulate the expression of chaperone proteins, which help in the proper folding of misfolded proteins in the ER. It also promotes the degradation of irreversibly misfolded proteins, preventing them from accumulating and causing cellular damage.

Application of Recombinant Human ATF6 Protein

The unique structure and activity of Recombinant Human ATF6 Protein make it a valuable tool in various scientific applications. Some of the key applications of this protein include:

  • Studying the UPR: Recombinant Human ATF6 Protein can be used to study the UPR pathway and its role in cellular stress response. By overexpressing or silencing the protein, researchers can gain insights into the mechanisms underlying this pathway.
  • Drug discovery: As ATF6 is involved in the UPR, it is a potential target for developing drugs that can modulate the cellular stress response. Recombinant Human ATF6 Protein can be used to screen for compounds that can activate or inhibit the protein’s activity.
  • Production of therapeutic proteins: The UPR is a critical pathway for the production of recombinant proteins in mammalian cells. By manipulating the activity of ATF6, researchers can improve the yield and quality of therapeutic proteins produced in cell culture systems.

Conclusion

In conclusion, Recombinant Human ATF6 Protein is a crucial player in the cellular stress response. Its unique structure and activity make it a valuable tool for studying the UPR pathway and its applications in various fields of research. With further studies and advancements in technology, this protein has the potential to be a key target for therapeutic interventions in diseases associated with ER stress.

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