Human B7-H7 / HHLA2 Recombinant Protein 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 >90% as determined by reduced SDS-PAGE. .

More Details:

• Species: Human
• Target: HHLA2
• Purity: >90% as determined by reduced 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:

B7-H7 (HHLA2) is a newly identified B7 family member that regulates human T-cell functions. B7-H7 was previously known as human endogenous retrovirus-H long terminal repeat associating 2 (HHLA2) with unidentified function. Recently, B7-H7 has been identified as a specific ligand for human CD28H. The B7-H7-CD28H pathway strongly promoted CD4+ T-cell proliferation and cytokine production via an AKT-dependent signaling cascade in the presence of TCR signaling, suggesting B7-H7 comprises a new co-stimulatory pathway. The first IgV domain of B7-H7, which presumably binds to a putative receptor, shows the highest homology to other B7 family members.

This protein carries a human IgG1 Fc Tag at the C-terminal. The protein has a calculated MW of 63.4 kDa. The protein migrates as 80-100 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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