Human Endocan Recombinant Protein C-6 His Tag Lyophilized from Innovative Research has been recombinantly produced in Human Cells. This is a Lyophilized protein buffered in Lyophilized from a 0.2 um filtered solution of 20mM PB, 150mM NaCl, pH 7.2. It is not recommended to reconstitute to a concentration less than 100UG/ml. Dissolve the lyophilized protein in ddH2O. with a purity of Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test..More Details: Species: Human Target: ESM1 Purity: Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. Source: Human Cells Storage Conditions: Lyophilized protein should be stored at -20░C, though stable at room temperature for 3 weeks.Reconstituted protein solution can be stored at 4-7░C for 2-7 days.Aliquots of reconstituted samples are stable at -20░C for 3 months.

Additional Information:

ESM-1, short from Endothelial cell-specific molecule 1, is expressed in lung, on the vascular capillary network within alveolar walls, and also at lower level in kidney. It is a secretory protein, and can be inducted by TNF and IL1B/interleukin-1beta, but not IL4/interleukin-4. This protein plays great roles in angiogenesis, sprouting, and may have potent implications in lung endothelial cell-leukocyte interactions.This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

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This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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