Analytical Data
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Gene name
ALG12
- Application
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Alternative Names
ALG12_HUMAN; Asparagine linked glycosylation 12 alpha 1 6 mannosyltransferase homolog
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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
Q9BV10
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Expression Region
1-488aa
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AA Sequence
MAGKGSSGRRPLLLGLLVAVATVHLVICPYTKVEESFNLQATHDLLYHWQDLEQYDHLEFPGVVPRTFLGPVVIAVFSSPAVYVLSLLEMSKFYSQLIVRGVLGLGVIFGLWTLQKEVRRHFGAMVATMFCWVTAMQFHLMFYCTRTLPNVLALPVVLLALAAWLRHEWARFIWLSAFAIIVFRVELCLFLGLLLLLALGNRKVSVVRALRHAVPAGILCLGLTVAVDSYFWRQLTWPEGKVLWYNTVLNKSSNWGTSPLLWYFYSALPRGLGCSLLFIPLGLVDRRTHAPTVLALGFMALYSLLPHKELRFIIYAFPMLNITAARGCSYLLNNYKKSWLYKAGSLLVIGHLVVNAAYSATALYVSHFNYPGGVAMQRLHQLVPPQTDVLLHIDVAAAQTGVSRFLQVNSAWRYDKREDVQPGTGMLAYTHILMEAAPGLLALYRDTHRVLASVVGTTGVSLNLTQLPPFNVHLQTKLVLLERLPRPS
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Molecular Weight
54.6 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
ALG12 is a key enzyme involved in the protein N-glycosylation process, which is crucial for proper protein folding, stability, and function in eukaryotic cells. This enzyme specifically catalyzes the transfer of a mannose residue to the growing oligosaccharide chain on nascent glycoproteins in the endoplasmic reticulum (ER). Dysfunctions or mutations in ALG12 can lead to congenital disorders of glycosylation (CDG), resulting in various developmental and metabolic issues. Researchers have focused on characterizing ALG12 to better understand its role in human health and disease, as well as its potential as a therapeutic target. Investigating ALG12's structure, function, and interactions within the glycosylation pathway can provide insights into the broader implications of glycosylation defects. Additionally, understanding ALG12’s mechanisms might pave the way for developing novel biochemical tools or therapeutic strategies for CDGs, emphasizing the importance of this enzyme in both fundamental biology and clinical implications.
