defects

Expression system: E. coli
Length: 38-208, Full Length of Mature Protein
Activity: Organoid Coculture、Cells

Expression system: E. coli
Length: 1-712, Partial
Activity: Not Tested

Expression system: E. coli
Length: 17-86, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 22-68, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 19-201, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 19-267, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 20-220, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 303-414, Partial
Activity: Cell Activity

Expression system: HEK293 Cells
Length: 303-414, Partial
Activity: ELISA

Expression system: E. coli
Length: 2-505, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 24-152, Partial
Activity: Not Tested

CD19 is a single-pass type I membrane protein containing 2 Ig-like C2-type (immunoglobulin-like) domains. CD19 is expressed on follicular dendritic cells and B cells. In fact, it is present on B cells from earliest recognizable B-lineage cells during development to B-cell blasts but is lost on maturation to plasma cells. CD19 primarily acts as a B cell co-receptor in conjunction with CD21 and CD81. Upon activation, the cytoplasmic tail of CD19 becomes phosphorylated, which leads to binding by Src-family kinases and recruitment of PI-3 kinase. CD19 Assembles with the antigen receptor of B lymphocytes in order to decrease the threshold for antigen receptor-dependent stimulation. Defects in CD19 are the cause of immunodeficiency common variable type 3 (CVID3) which is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen.

Expression system: HEK293 Cells
Length: 20-356, Partial
Activity: Not Tested

Expression system: E. coli
Length: 26-176 (mutation), Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 22-788, Partial
Activity: BLI

Ketohexokinase, also known as Hepatic fructokinase, is a member of the carbohydrate kinase PfkB family. It exits as a homodimer and most abundant in liver, kidney, gut, spleen and pancreas. Low levels also found in adrenal, muscle, brain and eye.This enzyme catalyzes conversion of fructose to fructose-1-phosphate. It is the first enzyme with a specialized pathway that catabolizes dietary fructose. Defects in KHK are the cause of fructosuria.

Angiotensinogen is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. Genetic variations in Angiotensinogen are associated with susceptibility to essential hypertension, and can cause renal tubular dysgenesis, a severe disorder of renal tubular development. Defects in the encoding gene have also been associated with non-familial structural atrial fibrillation, and inflammatory bowel disease.

Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is composed of just 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion.

PEPD belongs to the peptidase M24B family of Eukaryotic-type prolidase subfamily. PEPD is a cytosolic dipeptidase that hydrolyzes dipeptides with proline or hydroxyproline at the carboxy terminus. It is important in collagen metabolism because of the high levels of imino acids. Defects in PEPD are a cause of prolidase deficiency which is an autosomal recessive disorder associated with iminodipeptiduria.

APOC2 activates the lipoprotein lipase in capillaries, which hydrolyzes triglycerides and thus provides free fatty acids for cells. APOC2 is component of the very low density lipoprotein (VLDL) fraction in plasma. It is also an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly. Defects in APOC2 are the cause of hyperlipoproteinemia type 1B (HLPP1B) which characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis.

Expression system: E. coli
Length: 132-301, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-134, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 24-79, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 24-100, Full Length of Mature Protein
Activity: Not Tested