Analytical Data
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Gene name
Erap1
- Application
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Alternative Names
ARTS-1 Adipocyte-derived leucine aminopeptidase
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9EQH2
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Expression Region
731-930aa
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Molecular Weight
28.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Erap1, or endoplasmic reticulum aminopeptidase 1, is a crucial enzyme involved in the processing of peptides for presentation by major histocompatibility complex (MHC) class I molecules, playing a vital role in the immune response. It catalyzes the removal of amino acids from the N-terminus of precursor peptides, enhancing their binding affinity to MHC class I molecules and thereby influencing T cell recognition and activation. Research on Erap1 has gained momentum due to its implications in various diseases, particularly in autoimmune disorders and cancer. Abnormal Erap1 activity has been linked to altered immune responses, impacting the efficacy of immunotherapies. The recombinant protein form of Erap1 allows for detailed studies of its enzymatic properties, substrate specificity, and interaction with MHC molecules. Moreover, the generation of this recombinant protein facilitates investigations into its role in antigen processing and presents opportunities to develop novel therapeutic strategies targeting the immune system. Understanding the structure-function relationship of Erap1 through recombinant studies can provide insights into its mechanisms of action and potential as a biomarker for disease progression and response to treatment. As scientists continue to elucidate the functions of Erap1, this research bears the promise of enhancing our understanding of immune regulation and developing improved interventions for immune-related diseases.
