Analytical Data
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Gene name
LUM
- Application
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Alternative Names
LUM;LDC;SLRR2D;Lumican
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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
P51884
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Expression Region
1-338aa
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AA Sequence
MSLSAFTLFLALIGGTSGQYYDYDFPLSIYGQSSPNCAPECNCPESYPSA MYCDELKLKSVPMVPPGIKYLYLRNNQIDHIDEKAFENVTDLQWLILDHN LLENSKIKGRVFSKLKQLKKLHINHNNLTESVGPLPKSLEDLQLTHNKIT KLGSFEGLVNLTFIHLQHNRLKEDAVSAAFKGLKSLEYLDLSFNQIARLP SGLPVSLLTLYLDNNKISNIPDEYFKRFNALQYLRLSHNELADSGIPGNS FNVSSLVELDLSYNKLKNIPTVNENLENYYLEVNQLEKFDIKSFCKILGP LSYSKIKHLRLDGNRISETSLPPDMYECLRVANEVTLN
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Molecular Weight
63 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
LUM (Lumican) is a small leucine-rich proteoglycan primarily found in the extracellular matrix of connective tissues, playing a crucial role in cellular processes including cell growth, migration, and tissue organization. Its significance in the regulation of collagen fibrillogenesis has made it a focal point in research related to various pathological conditions such as fibrosis, cancer, and cardiovascular diseases. Understanding LUM's structure and function, particularly through the study of recombinant protein, offers valuable insights into its biological mechanics and therapeutic potential. The production of LUM as a recombinant protein allows for the detailed investigation of its interactions with other extracellular matrix components and cell surface receptors, facilitating a deeper understanding of its role in health and disease. Moreover, given the emerging interest in extracellular matrix components as targets in regenerative medicine and tissue engineering, studying LUM provides opportunities to develop novel therapeutic strategies aimed at modulating its activity to improve tissue repair and regeneration. This ongoing research underscores LUM's relevance not only as a biomarker for certain diseases but also as a potential target for innovative treatments, highlighting the importance of thorough scientific exploration in the field of proteoglycans and their complex roles in human physiology.
