Analytical Data
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Gene name
LMAN2
- Application
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Alternative Names
LMAN2；C5orf8；Vesicular integral-membrane Protein VIP36
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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
Q12907
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Expression Region
45-322aa
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AA Sequence
DITDGNSEHLKREHSLIKPYQGVGSSSMPLWDFQGSTMLTSQYVRLTPDERSKEGSIWNHQPCFLKDWEMHVHFKVHGTGKKNLHGDGIALWYTRDRLVPGPVFGSKDNFHGLAIFLDTYPNDETTERVFPYISVMVNNGSLSYDHSKDGRWTELAGCTADFRNRDHDTFLAVRYSRGRLTVMTDLEDKNEWKNCIDITGVRLPTGYYFGASAGTGDLSDNHDIISMKLFQLMVEHTPDEESIDWTKIEPSVNFLKSPKDNVDDPTGNFRSGPLTGWR
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Molecular Weight
36.0 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
LMAN2, or Lectin Mannose-binding Protein 2, is a critical component of the cellular transport system responsible for the proper folding and glycosylation of proteins in the endoplasmic reticulum (ER). Recent studies have highlighted its role in the trafficking of glycoproteins and its involvement in various cellular processes, including immune response and tumor progression. Given the importance of glycosylation in protein function and the potential links between LMAN2 dysfunction and diseases such as cancer and metabolic disorders, the recombinant expression of LMAN2 has gained attention. Researchers aim to produce LMAN2 as a recombinant protein to elucidate its structural and functional properties, facilitating a better understanding of its role in protein processing and its implications in health and disease. By generating recombinant LMAN2, scientists can delve into its binding mechanisms, interaction with glycoproteins, and the impact of its dysregulation on cellular pathways. This research could ultimately lead to novel therapeutic strategies aimed at ameliorating conditions associated with LMAN2 anomalies.
