Human HMGB1 Recombinant Protein Mouse IgG Fc Tag Lyophilized from Innovative Research has been recombinantly produced in HEK293 cells. This is a Lyophilized protein buffered in Tris with Glycine, Arginine and NaCl, pH7.5 with a purity of >95% as determined by SDS-PAGE..

More Details:

• Species: Human
• Target: HMGB1
• Purity: >95% 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:

High-mobility group protein B1 (HMGB1) is also known as high-mobility group protein 1 (HMG-1) and amphoterin, is a member of the HMGB family consisting of three members, HMGB1, HMGB2 and HMGB3. HMGB1 is a non-histone architectural chromosomal protein ubiquitously present in all vertebrate nuclei and binds double-stranded DNA without sequence specificity. The mechanism of inflammation and damage is binding to TLR4, which mediates HMGB1-dependent activation of macrophage cytokine release. This positions HMGB1 at the intersection of sterile and infectious inflammatory responses. HMGB1 has been studied as a DNA vaccine adjuvant and a target for cancer therapy.

This protein carries a mouse IgG2a Fc Tag at the N-terminal. The protein has a calculated MW of 51.6 kDa. The protein migrates as 60 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.. 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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