Recombinant Human GABARAPL1 Protein, N-His

Reference: YHK36401
Product nameRecombinant Human GABARAPL1 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight16.21 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 TypeMet1-Lys117
Aliases /SynonymsEarly estrogen-regulated protein, Gamma-aminobutyric acid receptor-associated protein-like 1, GEC-1, GABARAPL1, Glandular epithelial cell protein 1, GEC1, GABA(A) receptor-associated protein-like 1
ReferenceYHK36401
NoteFor research use only.

Description of Recombinant Human GABARAPL1 Protein, N-His

Introduction

Recombinant Human GABARAPL1 Protein, also known as GABARAPL1, is a member of the GABARAP family of proteins. It is a highly conserved protein that plays a crucial role in autophagy, a cellular process that involves the degradation of damaged or unnecessary cellular components. GABARAPL1 is involved in the formation of autophagosomes, which are double-membrane vesicles that engulf cellular material for degradation. In this article, we will discuss the structure, activity, and applications of Recombinant Human GABARAPL1 Protein.

Structure of Recombinant Human GABARAPL1 Protein

GABARAPL1 is a 117 amino acid protein with a molecular weight of approximately 14 kDa. It has a conserved N-terminal domain and a C-terminal domain that is responsible for protein-protein interactions. The N-terminal domain contains a glycine residue, which is essential for the conjugation of GABARAPL1 to phosphatidylethanolamine (PE) during autophagosome formation. The C-terminal domain contains a conserved WXXL motif, which is involved in the binding of GABARAPL1 to other proteins.

Activity of Recombinant Human GABARAPL1 Protein

Recombinant Human GABARAPL1 Protein is involved in various cellular processes, including autophagy, apoptosis, and intracellular trafficking. It plays a crucial role in autophagy by facilitating the formation of autophagosomes. GABARAPL1 binds to PE on the autophagosomal membrane and recruits other proteins, such as LC3, to form the autophagosome. It also interacts with other proteins, such as p62, to promote the degradation of cargo within the autophagosome.

In addition to autophagy, GABARAPL1 is involved in apoptosis, a process of programmed cell death. It interacts with Bcl-2, a protein that regulates apoptosis, and promotes cell death. GABARAPL1 also plays a role in intracellular trafficking by interacting with proteins involved in vesicle transport, such as Rab proteins.

Applications of Recombinant Human GABARAPL1 Protein

Recombinant Human GABARAPL1 Protein has various applications in both research and therapeutic settings. It is commonly used as an antigen in antibody production for studying the role of GABARAPL1 in autophagy and other cellular processes. It is also used as a tool to study the interactions between GABARAPL1 and other proteins, such as LC3 and p62.

In therapeutic settings, GABARAPL1 has been studied as a potential target for cancer treatment. It has been shown to play a role in the survival of cancer cells and targeting GABARAPL1 may lead to cell death. Recombinant Human GABARAPL1 Protein has also been investigated as a potential therapeutic agent for neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease. It has been shown to enhance autophagy and promote the clearance of toxic protein aggregates, which are characteristic of these diseases.

Conclusion

Recombinant Human GABARAPL1 Protein is a highly conserved protein that plays a crucial role in autophagy, apoptosis, and intracellular trafficking. It has a conserved structure with an N-terminal domain responsible for PE conjugation and a C-terminal domain involved in protein-protein interactions. GABARAPL1 has various applications in research and therapeutic settings, making it a valuable tool for studying autophagy and its role in various diseases.

References

1. Zhao YG, et al. GABARAPs and LC3s have opposite roles in regulating UL

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