Validation Data Gallery
|Positive WB detected in||MCF7 cells, HEK-293 cells, HepG2 cells, L02 cells, MCF-7 cells, mouse liver tissue, PC-3 cells|
|Positive IP detected in||mouse liver tissue|
|Positive IHC detected in||human liver tissue, human brain tissue|
Note: suggested antigen retrieval with TE buffer pH 9.0; (*) Alternatively, antigen retrieval may be performed with citrate buffer pH 6.0
|Western Blot (WB)||WB : 1:1000-1:4000|
|Immunoprecipitation (IP)||IP : 0.5-4.0 ug for IP and 1:1000-1:4000 for WB|
|Immunohistochemistry (IHC)||IHC : 1:20-1:200|
|Sample-dependent, check data in validation data gallery|
16209-1-AP targets GGCX in WB, IP, IHC,ELISA applications and shows reactivity with human, mouse, rat samples.
|Tested Reactivity||human, mouse, rat|
|Cited Reactivity||human, mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||GGCX fusion protein Ag9185|
|Full Name||gamma-glutamyl carboxylase|
|Calculated molecular weight||758 aa, 88 kDa|
|Observed molecular weight||88 kDa|
|GenBank accession number||BC013979|
|Gene ID (NCBI)||2677|
|Purification Method||Antigen affinity purification|
|Storage Buffer||PBS with 0.02% sodium azide and 50% glycerol pH 7.3.|
|Storage Conditions||Store at -20°C. Stable for one year after shipment. Aliquoting is unnecessary for -20oC storage.|
GGCX(Gamma-glutamyl carboxylase) is also named as GC and belongs to the vitamin K-dependent gamma-carboxylase family. This 94 kDa (including all modifications, such as the five N-linked glycosylations), is a 5-pass transmembrane protein and a key regulator of blood coagulation(PMID:20518534). It mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. Defects in GGCX are a cause of combined deficiency of vitamin K-dependent clotting factors type 1 (VKCFD1) and pseudoxanthoma elasticum-like disorder with multiple coagulation factor deficiency (PXEL-MCFD)(PMID:9845520;17110937).
Divergent effects of vitamins K1 and K2 on triple negative breast cancer cells.
Functional Study of the Vitamin K Cycle Enzymes in Live Cells.
VKOR paralog VKORC1L1 supports vitamin K-dependent protein carboxylation in vivo.
Characterization of vitamin K-dependent carboxylase mutations that cause bleeding and nonbleeding disorders.
J Cell Biol
GGCX and VKORC1 inhibit osteocalcin endocrine functions.