Analytical Data
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Gene name
GMDS
- Application
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Alternative Names
GMDS;GDP-mannose 4.6 dehydratase
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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
O60547
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Expression Region
1-372aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAHAPARCPSARGSGDGEMGKPRNVALITG ITGQDGSYLAEFLLEKGY EVHGIVRRSSSFNTGRIEHLYKNPQAHIEG NMKLHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDLAEY TAD VDGVGTLRLLDAVKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPR SPYGAAKLYAYWIVVNFREAYN LFAVNGILFNHESPRRGANFVTRKIS RSVAKIYLGQLECFSLGNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVI ATGEVHSVREFVEKSFLHIGKTIVWEGKNENEVGRCKETGKVHVTVDLK YYRPTEVDFLQGDCTKAKQKLNWKPR VAFDELVREMVHADVELMRTNP NA
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Molecular Weight
44 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
GMDS (GDP-mannose 4,6-dehydratase) is an enzyme that plays a critical role in the biosynthesis of GDP-mannose, a precursor for various glycosylation processes essential for proper cellular function. Research into GMDS has gained traction due to its potential implications in human health and disease. Alterations in glycosylation pathways have been associated with a range of conditions, including congenital disorders, cancer, and infectious diseases. Understanding the structure and function of GMDS can provide insights into these pathways and their dysregulation. Additionally, the recombinant production of GMDS offers a valuable tool for studying its enzymatic mechanisms and interactions with other cellular components. By utilizing techniques such as molecular cloning and protein expression systems, researchers can produce GMDS in significant quantities, facilitating enzymatic assays and structural studies. Moreover, GMDS as a potential therapeutic target highlights the significance of continued research in this area. Investigating the enzyme’s regulation, substrate specificity, and interaction with other glycosylation-related enzymes could reveal novel strategies for therapeutic interventions. Overall, the ongoing research on GMDS recombinant protein not only enhances our understanding of glycosylation but may also lead to innovative approaches for treating various diseases resulting from glycosylation defects.
