Analytical Data
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Gene name
METAP2
- Application
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Alternative Names
METAP2；MNPEP；P67EIF2；Methionine aminopeptidase 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P50579
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Expression Region
1-478aa
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AA Sequence
MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSA AGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKK KKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRT TSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKL EDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI DFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDV GEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGG EATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTK HLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDI KGSYTAQFEHTILLRPTCKEVVSRGDDY
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Molecular Weight
70 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
Related Products
Protein Description
METAP2 (Methionine Aminopeptidase 2) is a crucial enzyme involved in the processing of nascent peptides by removing the N-terminal methionine, which plays a vital role in protein maturation and regulation. Research into METAP2 has garnered significant attention due to its implications in various biological processes and diseases. Notably, METAP2 is implicated in cancer progression, as it can affect the stability of oncogenic proteins and influence cellular signaling pathways. Loss of METAP2 function has been associated with increased cellular stress responses and altered apoptosis, contributing to tumorigenesis. Additionally, METAP2 has been identified as a potential target for therapeutic interventions, with small-molecule inhibitors being developed to modulate its activity in cancer therapy. Understanding the structure-function relationship of METAP2 and its role in protein metabolism can provide insights into its potential as a biomarker for disease and a target for drug development. Recent advances in recombinant protein technology have enabled the production of METAP2 for detailed biochemical studies, allowing researchers to investigate its enzymatic properties and interactions with various substrates. This knowledge is essential for the development of METAP2-targeted therapies and for elucidating its role in cancer and other pathologies, thereby advancing our understanding of cellular homeostasis and disease mechanisms.
