Analytical Data
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Gene name
ALG10
- Application
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Alternative Names
ALG10; ALG10A; Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1.2-glucosyltransferase
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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
Q5BKT4
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Expression Region
1-473aa
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AA Sequence
MAQLEGYYFSAALSCTFLVSCLLFSAFSRALREPYMDEIFHLPQAQRYCEGHFSLSQWDPMITTLPGLYLVSIGVIKPAIWIFGWSEHVVCSIGMLRFVNLLFSVGNFYLLYLLFCKVQPRNKAASSIQRVLSTLTLAVFPTLYFFNFLYYTEAGSMFFTLFAYLMCLYGNHKTSAFLGFCGFMFRQTNIIWAVFCAGNVIAQKLTEAWKTELQKKEDRLPPIKGPFAEFRKILQFLLAYSMSFKNLSMLLLLTWPYILLGFLFCAFVVVNGGIVIGDRSSHEACLHFPQLFYFFSFTLFFSFPHLLSPSKIKTFLSLVWKRRILFFVVTLVSVFLVWKFTYAHKYLLADNRHYTFYVWKRVFQRYETVKYLLVPAYIFAGWSIADSLKSKSIFWNLMFFICLFTVIVPQKLLEFRYFILPYVIYRLNIPLPPTSRLICELSCYAVVNFITFFIFLNKTFQWPNSQDIQRFMW
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Molecular Weight
55.6 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
ALG10 is an important gene that encodes a protein belonging to the family of oligosaccharyltransferases, which play a crucial role in the process of N-glycosylation. This post-translational modification is vital for the proper folding, stability, and function of many glycoproteins, particularly those involved in critical cellular processes. Research on ALG10 has gained attention due to its involvement in several pathological conditions, including congenital disorders of glycosylation (CDGs), which can lead to various symptoms ranging from developmental delays to organ dysfunction. In recent years, recombinant ALG10 proteins have been produced to study their function and the mechanisms underlying N-glycosylation. This includes investigating how mutations in the ALG10 gene can disrupt glycosylation pathways, leading to disease phenotypes. Advances in recombinant DNA technology and protein expression systems have facilitated the production of ALG10 and its glycosylated forms, allowing researchers to uncover its biochemical properties and interactions with other cellular components. Furthermore, understanding ALG10’s role in glycosylation could open up new avenues for therapeutic interventions in diseases linked to glycosylation defects. Overall, the study of recombinant ALG10 protein is not only essential for basic biochemical research but also holds potential clinical implications in enhancing our understanding of glycosylation-related diseases.
