Analytical Data
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Gene name
METAP2/Methionine aminopeptidase 2
- Application
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Alternative Names
Initiation factor 2-associated 67 kDa glycoprotein (p67) (p67eIF2) (Peptidase M) (MAP 2) (MetAP 2) (MNPEP) (P67EIF2)
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Species
Human
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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
P50579
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Expression Region
2-478aa
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Molecular Weight
59.8 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
Methionine aminopeptidase 2 (MetAP2) is a pivotal enzyme involved in protein maturation, specifically by catalyzing the removal of the N-terminal methionine residue from newly synthesized proteins. This activity plays a crucial role in modulating protein function and stability, thus influencing various cellular processes, including signal transduction and cell proliferation. The significance of MetAP2 extends beyond basic biology; it has been implicated in various pathological conditions, including cancer and viral infections, making it a potential therapeutic target. Recent studies have highlighted its role in angiogenesis, where inhibition of MetAP2 leads to the suppression of new blood vessel formation, presenting a promising approach for cancer treatment. The production of recombinant MetAP2 proteins has facilitated in-depth studies of its structure-function relationships and interactions with different ligands. By generating high-purity MetAP2, researchers can explore its catalytic mechanisms and inhibitory effects in detail, paving the way for the development of specific MetAP2 inhibitors. Such inhibitors may serve as innovative therapeutic agents, particularly in oncology, where they could limit tumor growth and metastasis by disrupting the vascular supply. The ongoing research efforts to generate and characterize recombinant MetAP2 proteins thus provide invaluable insights that could translate into novel strategies for combating diseases associated with dysregulated protein processing and angiogenesis.
