Analytical Data
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Gene name
LOXL1
- Application
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Alternative Names
LOXL1；LOXL；Lysyl oxidase homolog 1
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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
Q08397
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Expression Region
292-574aa
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AA Sequence
DPGPEAAQA HGGDPRLGWY PPYANPPPEA YGPPRALEPP YLPVRSSDTP PPGGERNGAQ QGRLSVGSVY RPNQNGRGLP DLVPDPNYVQ ASTYVQRAHL YSLRCAAEEK CLASTAYAPE ATDYDVRVLL RFPQRVKNQG TADFLPNRPR HTWEWHSCHQ HYHSMDEFSH YDLLDAATGK KVAEGHKASF CLEDSTCDFG NLKRYACTSH TQGLSPGCYD TYNADIDCQW IDITDVQPGN YILKVHVNPK YIVLESDFTN NVVRCNIHYT GRYVSATNCK IVQS
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Molecular Weight
32 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
Lysyl oxidase-like 1 (LOXL1) is an enzyme that plays a crucial role in the extracellular matrix remodeling and is involved in the cross-linking of collagen and elastin fibers, which are essential for maintaining tissue integrity and elasticity. Research has highlighted the association of LOXL1 with various pathological conditions, including glaucoma, where it has been identified as a potential biomarker for the disease, as well as in fibrotic disorders and cardiovascular diseases. The interest in LOXL1 has escalated due to its function in cell adhesion and migration, suggesting a significant role in tumor progression and metastasis. Understanding the biochemical properties and regulatory mechanisms of LOXL1 is vital for exploring its therapeutic potential. Recent studies have focused on the recombinant expression of LOXL1 to facilitate functional analyses and structural studies that could reveal insights into its enzymatic activity and molecular interactions. By producing LOXL1 as a recombinant protein, researchers aim to unravel its role in physiological and pathological conditions, contributing to the development of targeted therapies that modulate its activity in various diseases.
