GYPA/CD235a Protein, Mouse (HEK293, Fc)

The GYPA/CD235a protein is an important component of the ankyrin 1 complex, which maintains the stability and shape of the red blood cell membrane. As a major intrinsic membrane protein, GYPA ensures the structural integrity and function of these blood cells. GYPA/CD235a Protein, Mouse (HEK293, Fc) is the recombinant mouse-derived GYPA/CD235a protein, expressed by HEK293 , with C-hFc labeled tag. The total length of GYPA/CD235a Protein, Mouse (HEK293, Fc) is 108 a.a., with molecular weight of 68-75 kDa.

GYPA, a crucial component of the ankyrin-1 complex, intricately participates in maintaining the stability and shape of the erythrocyte membrane. Serving as the major intrinsic membrane protein of erythrocytes, GYPA plays a vital role in the structural integrity and functionality of these blood cells. The N-terminal glycosylated segment, projecting outside the erythrocyte membrane, hosts MN blood group receptors, underscoring its involvement in blood group determinants. Additionally, GYPA is integral for the proper function of SLC4A1, and its presence is essential for the high activity of SLC4A1. Furthermore, GYPA serves as a receptor for influenza virus, Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175), and Hepatitis A virus (HAV). Notably, it forms homodimers and is a key constituent of the ankyrin-1 complex, working in concert with other proteins such as ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPB, and AQP1 to maintain erythrocyte membrane architecture. The interaction with SLC4A1 results in the formation of a heterotetramer, highlighting the collaborative role of GYPA in the molecular organization of erythrocyte structures.

Mouse

HEK293

C-hFc

P14220 (M1-V108)

14934  [NCBI]

68-75 kDa

Greater than 95% as determined by Tris-Bis PAGE.

<1 EU/μg, determined by LAL method.