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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human ERAP1 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 50.12 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
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 | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Gly529-Met941 |
Aliases /Synonyms | Aminopeptidase PILS, ARTS1, Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator, PILS-AP, Endoplasmic reticulum aminopeptidase 1, ARTS-1, A-LAP, Puromycin-insensitive leucyl-specific aminopeptidase, APPILS, ERAP1, KIAA0525, Adipocyte-derived leucine aminopeptidase |
Reference | ARO-P11788 |
Note | For research use only. |
Recombinant Human ERAP1 Protein is a type of recombinant protein that has been produced through genetic engineering techniques. It is a member of the aminopeptidase family and plays a crucial role in the immune system by processing and trimming antigenic peptides for presentation to immune cells. In this article, we will explore the structure, activity, and applications of Recombinant Human ERAP1 Protein.
Recombinant Human ERAP1 Protein is a 94 kDa protein that consists of 941 amino acids. It has a distinct domain structure, with a catalytic domain at the N-terminus and a non-catalytic domain at the C-terminus. The catalytic domain contains the active site responsible for peptide trimming, while the non-catalytic domain is thought to be involved in protein-protein interactions.
The crystal structure of Recombinant Human ERAP1 Protein has been determined, revealing a homodimeric structure with each monomer containing a zinc ion at the active site. The zinc ion is essential for the enzymatic activity of ERAP1, as it facilitates the binding and hydrolysis of peptide bonds.
Recombinant Human ERAP1 Protein is an aminopeptidase that is primarily involved in antigen processing. It is responsible for trimming the N-terminal ends of peptides to generate optimal epitopes for presentation to immune cells. This process is crucial for the activation of T cells and the initiation of an immune response.
ERAP1 has a preference for peptides with basic or hydrophobic residues at the N-terminus, and it has been shown to trim peptides of varying lengths, from 8 to 16 amino acids. It also has the ability to trim peptides that are already bound to major histocompatibility complex (MHC) class I molecules, a process known as peptide editing.
In addition to its role in antigen processing, Recombinant Human ERAP1 Protein has also been shown to have other functions, such as regulation of blood pressure and angiogenesis, through its interactions with other proteins.
Recombinant Human ERAP1 Protein has a wide range of applications in both research and clinical settings. Its role in antigen processing makes it a valuable tool for studying immune responses and developing vaccines. It has also been used in the development of therapeutic strategies for autoimmune diseases and cancer, as well as in the diagnosis and treatment of infectious diseases.
In research, Recombinant Human ERAP1 Protein is commonly used to study its enzymatic activity and its interactions with other proteins. It has also been used to investigate the role of ERAP1 polymorphisms in various diseases, as well as to understand the mechanisms of peptide trimming and editing.
In clinical settings, Recombinant Human ERAP1 Protein has been used in diagnostic tests for autoimmune diseases, such as ankylosing spondylitis and psoriasis. It has also been studied as a potential therapeutic target for these diseases, as well as for cancer and viral infections.
In summary, Recombinant Human ERAP1 Protein is a crucial component of the immune system, involved in antigen processing and presentation. Its distinct structure and enzymatic activity make it a valuable tool for studying immune responses and developing therapeutic strategies. With its wide range of applications in both research and clinical settings, Recombinant Human ERAP1 Protein continues to be a topic of interest in the scientific community.
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