Analytical Data
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Gene name
Meprin alpha/MEP1A
- Application
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Alternative Names
PPHA; PABA Peptide Hydrolase; Endopeptidase-2; N-benzoyl-L-tyrosyl-P-amino-Benzoic Acid Hydrolase Subunit Alpha; PABA Peptide Hydrolase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q16819
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Expression Region
His213~Val506
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Molecular Weight
39kDa
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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
Meprin alpha, encoded by the MEP1A gene, is a metalloendopeptidase that belongs to the astacin family of proteases. It is widely expressed in various tissues, particularly in the kidneys and intestines, and plays a crucial role in extracellular matrix remodeling, immune response modulation, and protein processing. Dysregulation of Meprin alpha has been implicated in several pathological conditions, including renal diseases, inflammation, and cancer. The enzyme’s ability to cleave a diverse range of substrates makes it a significant player in many biological processes. Research has increasingly focused on recombinant forms of Meprin alpha (rMeprin alpha) to better understand its functional mechanisms and potential therapeutic applications. By producing rMeprin alpha, scientists aim to investigate its substrate specificity, catalytic activity, and interaction with other proteins. Furthermore, recombinant proteins can be utilized in drug development, enabling the design of inhibitors that could mitigate the enzyme’s pathological effects in diseases. Overall, the study of recombinant Meprin alpha presents promising opportunities for advancing our understanding of its biological roles and therapeutic potential.
