VCAM 1 Recombinant Protein His Tag Lyophilized

VCAM 1 Recombinant Protein His Tag Lyophilized from Innovative Research has been recombinantly produced in HEK293 cells. This is a Lyophilized protein buffered in PBS, pH7.4 with a purity of >92% as determined by SDS-PAGE..

More Details:

• Species: Human
• Target: VCAM1
• Purity: >92% as determined by SDS-PAGE.
• Source: HEK293 cells
• Storage Conditions: Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles.

Additional Information:

Vascular cell adhesion protein 1 (VCAM1) is also known as CD106, INCAM-100 and L1CAM, is a cell surface sialoglycoprotein belonging to the immunoglobulin superfamily. VCAM1 / CD106 contains 7 Ig-like C2-type (immunoglobulin-like) domains. CD106 / VCAM-1 is expressed on inflammed vascular endothelium, as well as on macrophage-like and dendritic cell types in both normal and inflammed tissue. L1CAM / VCAM-1 is Important in cell-cell recognition and appears to function in leukocyte-endothelial cell adhesion. CD106 / VCAM1 interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1 / VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation. INCAM-100 / VCAM1 binds to ECMV-D capsid proteins and acts as a receptor for this virus.

This recombinant protein can be used for WB. 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 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 herein are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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