RHCE Protein, Human (Cell-Free, His)

The RHCE protein is an important component of the ankyrin-1 complex and is essential for the stability and shape of the red blood cell membrane. RHCE Protein, Human (Cell-Free, His) is the recombinant human-derived RHCE protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of RHCE Protein, Human (Cell-Free, His) is 417 a.a., with molecular weight of 47.1 kDa.

RHCE, an integral component of the ankyrin-1 complex, plays a crucial role in preserving the stability and shape of the erythrocyte membrane. Within this multiprotein assembly, RHCE functions as the primary membrane attachment site for ANK1 when associated with RHAG, contributing to the structural integrity of erythrocytes. Additionally, RHCE is implicated in potential roles related to ammonium and carbon dioxide transport through its heterotrimeric form. The heterotrimeric configuration involves interaction between a RHCE monomer and a RHAG homodimer. As part of the larger ankyrin-1 complex in the erythrocyte membrane, which also includes ANK1, RHAG, SLC4A1, EPB42, GYPA, GYPB, and AQP1, RHCE collaborates to maintain the overall stability and shape of these vital blood cells. The interaction between RHCE and ANK1, facilitated via the N- and C-terminal domains, serves as the primary membrane attachment site for ANK1, underscoring the coordinated efforts within the ankyrin-1 complex in sustaining erythrocyte membrane architecture.

Human

E. coli Cell-free

N-10*His

P18577 (M1-F417)

6006

MSSKYPRSVRRCLPLWALTLEAALILLFYFFTHYDASLEDQKGLVASYQVGQDLTVMAALGLGFLTSNFRRHSWSSVAFNLFMLALGVQWAILLDGFLSQFPPGKVVITLFSIRLATMSAMSVLISAGAVLGKVNLAQLVVMVLVEVTALGTLRMVISNIFNTDYHMNLRHFYVFAAYFGLTVAWCLPKPLPKGTEDNDQRATIPSLSAMLGALFLWMFWPSVNSPLLRSPIQRKNAMFNTYYALAVSVVTAISGSSLAHPQRKISMTYVHSAVLAGGVAVGTSCHLIPSPWLAMVLGLVAGLISIGGAKCLPVCCNRVLGIHHISVMHSIFSLLGLLGEITYIVLLVLHTVWNGNGMIGFQVLLSIGELSLAIVIALTSGLLTGLLLNLKIWKAPHVAKYFDDQVFWKFPHLAVGF

47.1 kDa

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

<1 EU/μg, determined by LAL method.