Analytical Data
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Gene name
GMPPB
- Application
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Alternative Names
GDP mannose pyrophosphorylase B; GDP-mannose pyrophosphorylase B; GMPPB; GMPPB_HUMAN; GTP-mannose-1-phosphate guanylyltransferase beta; KIAA1851
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y5P6
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Expression Region
1-360aa
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AA Sequence
MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQVLEKEMKAQEQRLGIRISMSHEEEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFVEKPQVFVSNKINAGMYILSPAVLRRIQLQPTSIEKEVFPIMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFLQSLRQKQPERLCSGPGIVGNVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDARIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVNDELYLNGASVLPHKSIGESVPEPRIIM
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Molecular Weight
66.3 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
Related Products
Protein Description
GMPPB (GDP-mannose pyrophosphorylase B) is an essential enzyme involved in the synthesis of GDP-mannose, a critical nucleotide sugar that serves as a substrate for glycosylation processes in eukaryotic cells. Mutations in the GMPPB gene have been implicated in a rare neuromuscular disorder known as GMPPB myopathy, which underscores the importance of this enzyme in human health. The study of GMPPB and its recombinant protein form has gained particular attention due to the enzyme's role in various biological functions, including protein glycosylation, cell signaling, and the synthesis of polysaccharides. Researchers aim to explore the enzyme's structure and function to better understand its biochemical pathways and potential therapeutic applications. Recombinant GMPPB can facilitate the development of novel treatments for genetic disorders related to glycan biosynthesis and may aid in the design of enzyme replacement therapies. Furthermore, the production of GMPPB in a recombinant form allows for a more accessible supply for biochemical assays and drug discovery processes, thereby expanding its applicability in both basic and applied research settings. Overall, the investigation of GMPPB recombinant protein is pivotal for elucidating its biological roles and could potentially lead to significant advancements in the treatment of GMPPB-related conditions.
