286 products were found matching "GeneID 2993"!

Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of...

Granulomatosis with polyangiitis (GPA) presents a wide spectrum of manifestations from the common respiratory symptoms to infrequent neurological and cardiac complications. The challenge in diagnosis and management makes the rapidly progressive disorder one of the most challenging dilemmas in clinical medicine.The...

Human CD235a (Glycophorin A) is a sialoglycoprotein expressed early on the cell surface during erythropoiesis as pluripotent stem cells are recruited to differentiate into erythrocytes. CD235a is a useful marker to study the developmental biology of hematopoietic progenitor cells.

Human CD235a (Glycophorin A) is a sialoglycoprotein expressed early on the cell surface during erythropoiesis as pluripotent stem cells are recruited to differentiate into erythrocytes. CD235a is a useful marker to study the developmental biology of hematopoietic progenitor cells.

Human CD235a (Glycophorin A) is a sialoglycoprotein expressed early on the cell surface during erythropoiesis as pluripotent stem cells are recruited to differentiate into erythrocytes. CD235a is a useful marker to study the developmental biology of hematopoietic progenitor cells.

Human CD235a (Glycophorin A) is a sialoglycoprotein expressed early on the cell surface during erythropoiesis as pluripotent stem cells are recruited to differentiate into erythrocytes. CD235a is a useful marker to study the developmental biology of hematopoietic progenitor cells.

Protein function: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved...

Protein function: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved...

Protein function: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved...

Protein function: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved...

Protein function: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved...

Protein function: Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved...