protein

IAPP Protein, Human (GST)

HY-P72240

5 μg;10 μg;50 μg

47;80;224 USD

IAPP Protein, Human (GST)

proteins

E. coli

5 μg;10 μg;50 μg

47;80;224 USD

The IAPP protein selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, affecting glucose metabolism without affecting adipocytes. IAPP interacts with IDE (insulin-degrading enzyme) and insulin (INS) to form homodimers, affecting their fibril formation. IAPP Protein, Human (GST) is the recombinant human-derived IAPP protein, expressed by E. coli , with N-GST labeled tag. The total length of IAPP Protein, Human (GST) is 37 a.a., with molecular weight of ~31.4 kDa.

Human

IAPP protein demonstrates selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, exhibiting a specific impact on muscle glucose metabolism without affecting adipocytes. This protein is known to interact with IDE (insulin-degrading enzyme) and insulin (INS), forming homodimers as part of its functional mechanisms. Notably, the interaction with insulin not only influences the homodimerization of IAPP but also inhibits fibril formation, suggesting a regulatory role in modulating the assembly of fibrillar structures associated with IAPP. These interactions highlight the intricate interplay of IAPP in the regulation of glucose metabolism and its dynamic relationship with key molecular partners.

Amylin; DAP; Diabetes associated peptide; Diabetes-associated peptide; IAP; IAPP; IAPP_HUMAN; Insulinoma amyloid peptide; Islet amyloid polypeptide diabetes associated peptide, amylin; ; Islet amyloid polypeptide

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm solution of PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US;may vary elsewhere.