protein

S100A3 Protein, Human (His-MBP)

HY-P76585

5 μg;10 μg;50 μg

55;95;260 USD

S100A3 Protein, Human (His-MBP)

proteins

E. coli

5 μg;10 μg;50 μg

55;95;260 USD

S100A3 Protein, functioning as a monomer, displays a robust binding affinity for calcium and zinc. It is implicated in calcium-dependent cuticle cell differentiation and contributes to the formation of the hair shaft and hair cuticular barrier. In its citrullinated state, S100A3 can exist as both a homodimer and a homotetramer, indicating potential involvement in various cellular processes associated with these forms. S100A3 Protein, Human (His-MBP) is the recombinant human-derived S100A3 protein, expressed by E. coli , with N-His, N-MBP labeled tag. The total length of S100A3 Protein, Human (His-MBP) is 101 a.a., with molecular weight of ~50 kDa.

Human

S100A3, a protein with the ability to bind both calcium and zinc, emerges as a potential player in calcium-dependent cuticle cell differentiation and the formation of hair shafts and cuticular barriers. Its binding affinity for calcium and zinc suggests a regulatory role in cellular processes dependent on these ions. The protein is known to exist in homodimer and homotetramer forms, particularly in its citrullinated state, indicating a potential structural significance in its functional activity. The implication of S100A3 in processes related to hair development and barrier formation underscores its importance in the molecular mechanisms governing tissue differentiation and integrity.

Protein S100-A3; Protein S-100E; S100 calcium-binding protein A3; S100E

Greater than 95% as determined by reducing SDS-PAGE

Supplied as a 0.2 μm filtered solution of PBS, 20% glycerol, pH 7.4.

Shipping with dry ice.