GYPB Protein, Human (Cell-Free, His)

GYPB Protein is an integral part of the ankyrin-1 complex, crucial for erythrocyte membrane stability and shape. Within the erythrocyte complex, including ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB, and AQP1, GYPB interacts with RHAG via its N-terminal, bridging the heterotrimer (RHAG)2(RHCE) with the SLC4A1 Band 3 I dimer complexed with GYPA. GYPB Protein, Human (Cell-Free, His) is the recombinant human-derived GYPB protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of GYPB Protein, Human (Cell-Free, His) is 72 a.a., with molecular weight of 10.5 kDa.

GYPB is an integral component of the ankyrin-1 complex, a multiprotein assembly crucial for maintaining the stability and shape of the erythrocyte membrane. Within the erythrocyte-specific ankyrin-1 complex, which includes ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB, and AQP1, GYPB contributes to the overall structural integrity of these essential blood cells. Specifically, GYPB interacts via its N-terminal domain with RHAG, facilitating a connection between the (RHAG)2(RHCE) heterotrimer and the SLC4A1 Band 3 I dimer complexed with GYPA. This intricate interaction network highlights the coordinated efforts of the ankyrin-1 complex in ensuring the stability and shape of the erythrocyte membrane, emphasizing the significance of GYPB in this regulatory mechanism.

Human

E. coli Cell-free

N-10*His

P06028 (L20-A91)

2994

LSTTEVAMHTSTSSSVTKSYISSQTNGETGQLVHRFTVPAPVVIILIILCVMAGIIGTILLISYSIRRLIKA

10.5 kDa

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

<1 EU/μg, determined by LAL method.