IAPP Protein, Human (GST)

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.

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.

Human

E. coli

N-GST

P10997 (K34-Y70)

3375  [NCBI]

KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY

Approximately 31.4 kDa

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

Lyophilized powder.

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

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US;may vary elsewhere.