Analytical Data
-
Gene name
LOX
- Application
-
Alternative Names
LOX；LOG15；Polyunsaturated fatty acid lipoxygenase ALOX15
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P28300
-
Expression Region
174-417aa
-
AA Sequence
PYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY
-
Molecular Weight
35.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Lox (Lysyl oxidase) is a crucial enzyme involved in the cross-linking of collagen and elastin, which are fundamental components of the extracellular matrix. This enzyme plays a significant role in various biological processes, including tissue development, wound healing, and the maintenance of structural integrity in connective tissues. Dysregulation of Lox has been linked to several pathological conditions, such as fibrosis, cancer progression, and cardiovascular diseases. As a result, the study of Lox recombinant proteins has garnered substantial interest in both basic and clinical research. Researchers aim to understand the molecular mechanisms governing Lox activity, its role in fibrotic diseases, and its potential as a therapeutic target. Recombinant Lox proteins provide a valuable tool for elucidating these functions, enabling scientists to explore the biochemical properties and regulatory pathways associated with Lox. Furthermore, the development of Lox inhibitors or modulators through recombinant technologies holds promise for the treatment of diseases characterized by excessive collagen deposition or impaired matrix remodeling. This research is vital for advancing therapeutic strategies and improving our understanding of the extracellular matrix's role in health and disease.
