Analytical Data
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Gene name
LMAN1
- Application
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Alternative Names
F5F8D; FMFD1; MCFD1; MR60; Gp58; Protein ERGIC-53; Coagulation Factor V-Factor VIII Combined Deficiency; Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 53
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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 90% as determined by SDS-PAGE.
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Uniprot
P49257
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Expression Region
Pro198~Cys475
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Molecular Weight
36kDa
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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
LMAN1, or Lectin Mannose-Binding 1, is a crucial protein involved in the endoplasmic reticulum (ER) quality control system, which ensures the proper folding and transport of glycoproteins. Mutations or dysfunctions in LMAN1 are associated with several pathological conditions, most notably congenital disorders of glycosylation (CDGs). These are a group of genetic diseases that arise due to defects in glycosylation, leading to a wide range of clinical symptoms, including neurological deficits and immunological issues. Research on LMAN1 recombinant proteins is significant as it aids in understanding the molecular mechanisms behind glycoprotein trafficking and processing within the ER. Additionally, studying LMAN1 facilitates the development of therapeutic strategies for CDGs and offers insights into broader implications of glycosylation in diseases such as cancer and metabolic disorders. By producing and analyzing LMAN1 recombinant proteins, researchers can explore their structural and functional properties, assess their interactions with other cellular components, and investigate how alterations in LMAN1 activity may influence glycoprotein maturation and degradation. This line of investigation not only enhances our comprehension of LMAN1's role in cellular biology but also opens new avenues for potential medical interventions targeting glycosylation-related disorders. Overall, the study of LMAN1 and its recombinant forms is paramount in the fields of glycobiology and medical research, promising advancements in understanding and treating complex diseases associated with glycosylation defects.
