Analytical Data
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Gene name
LMAN2
- Application
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Alternative Names
GP36B; VIP36; C5orf8; Vesicular integral-membrane protein VIP36; Glycoprotein GP36b; Vesicular integral-membrane protein 36
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q12907
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Expression Region
Asp45~Arg322
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Molecular Weight
35kDa
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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
LMAN2 (Lectin-like Mannose-binding Protein 2) is a type II membrane protein that plays a crucial role in the endoplasmic reticulum (ER) quality control system, specifically in the glycoprotein trafficking process. Research on LMAN2 has gained attention due to its involvement in the transport of proteins within the secretory pathway and its implications in various diseases, including hereditary disorders characterized by protein misfolding. Its functional role as a mannose-binding lectin suggests that it may be essential for recognizing and sorting glycoproteins, ensuring that only properly folded and assembled proteins are secreted from the ER. Moreover, studies have shown that mutations in the LMAN2 gene can lead to significant cellular dysfunctions and contribute to diseases such as congenital disorders of glycosylation (CDG). Understanding the biochemical properties of LMAN2 and its interaction with other molecular chaperones is critical for elucidating the pathophysiology of these conditions. Recent advances in recombinant protein technology have enabled researchers to produce LMAN2 in sufficient quantities to investigate its structure and function, paving the way for potential therapeutic interventions. The study of LMAN2 not only provides insights into fundamental cellular processes but also holds promise for the development of novel strategies to address glycosylation-related diseases. With ongoing research, the full potential of LMAN2 as a biomarker or therapeutic target continues to unfold, underscoring the importance of this protein in cellular health and disease.
