Analytical Data
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Gene name
PMM2
- Application
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Alternative Names
PMM2;Phosphomannomutase 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
O15305
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Expression Region
1-246aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAAPGPALCLFDVDGTLTAPRQKITKEMDD FLQKLRQKIKIGVVGGSDFEKVQEQLGNDVVEKYDYVFPENGLVAYKDGK LLCRQNIQSHLGEALIQDLINYCLSYIAKIKLPKKRGTFIEFRNGMLNVS PIGRSCSQEERIEFYELDKKENIRQKFVADLRKEFAGKGLTFSIGGQISF DVFPDGWDKRYCLRHVENDGYKTIYFFGDKTMPGGNDHEIFTDPRTMGYS VTAPEDTRRICELLFS
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Molecular Weight
30 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
PMM2 (phosphomannomutase 2) is an essential enzyme involved in the glycosylation pathway, particularly in the synthesis of GDP-mannose, a critical sugar nucleotide required for the proper functioning of various glycoproteins and glycolipids. Mutations in the PMM2 gene lead to congenital disorders of glycosylation (CDG), specifically CDG-Ib, characterized by a range of developmental and metabolic abnormalities. Understanding the structure and function of PMM2 is vital for elucidating the molecular mechanisms underlying these disorders. Recent research has focused on the recombinant expression of PMM2 in various systems to facilitate detailed biochemical and structural studies. By producing the enzyme in a controlled environment, scientists can investigate its catalytic properties, substrate specificity, and regulatory mechanisms. Such studies are essential for developing potential therapeutic strategies, including enzyme replacement therapy and small molecule drugs aimed at correcting the enzymatic deficiencies associated with PMM2 mutations. Furthermore, advances in protein engineering techniques allow for the modification of PMM2 to enhance its stability and activity, paving the way for innovative treatment approaches for patients suffering from PMM2-related diseases. Overall, the study of recombinant PMM2 not only enhances our understanding of glycosylation pathways but also holds promise for the development of targeted therapies for CDG-Ib and related conditions.
