Anti-Lipoprotein a monoclonal antibody (DCABH-1722)

Rabbit Anti-Human Lipoprotein a monoclonal antibody for WB, IHC-P, FC Datasheet

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Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Clone
FQS7585
Species Reactivity
Human
Immunogen
A synthetic peptide, corresponding to residues in Human Lipoprotein a.
Conjugate
Unconjugated

Applications


Application Notes
WB: 1/10000 - 1/50000; IHC-P: 1/100 - 1/250; Flow Cyt: 1/100
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
LPA; lipoprotein, Lp(a); LP; apolipoprotein(a); lp(a); apo(a)
Entrez Gene ID

Product Background


Gene summary
LPA (Lipoprotein(A)) is a Protein Coding gene. Diseases associated with LPA include pontocerebellar hypoplasia type 2d and atherosclerosis. Among its related pathways are Lipoprotein metabolism and Metabolism. GO annotations related to this gene include serine-type endopeptidase activity and endopeptidase inhibitor activity. An important paralog of this gene is PLAT. The protein encoded by this gene is a serine proteinase that inhibits the activity of tissue-type plasminogen activator I. The encoded protein constitutes a substantial portion of lipoprotein(a) and is proteolytically cleaved, resulting in fragments that attach to atherosclerotic lesions and promote thrombogenesis. Elevated plasma levels of this protein are linked to atherosclerosis. Depending on the individual, the encoded protein contains 2-43 copies of kringle-type domains. The allele represented here contains 15 copies of the kringle-type repeats and corresponds to that found in the reference genome sequence.
Antigen Description
Lipoprotein(a) (Lp(a)) is a lipoprotein subclass assembled in the blood from low density lipoprotein (LDL) molecules and apolipoprotein-a (apo-a). Lp(a) recruits inflammatory cells through interaction with Mac-1 integrin. High Lp(a) in blood is a risk factor for coronary heart disease, cerebrovascular disease, atherosclerosis, thrombosis, and stroke. Lp(a) concentrations may be affected by disease states, but are only moderately affected by diet, exercise and other environmental factors. Lipid-reducing drugs have no effect on Lp(a) concentration. High Lp(a) predicts risk of early atherosclerosis similar to high LDL, but in advanced atherosclerosis, Lp(a) is a risk factor independent of LDL, indicating a coagulant risk of plaque thrombosis. Apo(a) contains domains that are very similar to plasminogen (PLG). Lp(a) accumulates in the vessel wall and inhibits binding of PLG to the cell surface, reducing plasmin generation which increases clotting. This inhibition also promotes proliferation of smooth muscle cells. These unique features of Lp(a) suggest a role in the generation of clots and atherosclerosis. Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330. Lipoprotein(a) (also called Lp(a) or LPA) is a lipoprotein subclass. Genetic studies and numerous epidemiologic studies have identified Lp(a) as a risk factor for atherosclerotic diseases such as coronary heart disease and stroke. The physiological function of Lp(a)/apo(a) is still unknown. A function within the coagulation system seems plausible, given the aspect of the high homology between apo(a) and plasminogen. In fact, the LPA gene derives from a duplication of the plasminogen gene.
Pathway
LDL-mediated lipid transport, organism-specific biosystem; Lipid digestion, mobilization, and transport, organism-specific biosystem; Lipoprotein metabolism, organism-specific biosystem; Metabolism, organism-specific biosystem; Metabolism of lipids and lipoproteins, organism-specific biosystem; amb2 Integrin signaling, organism-specific biosystem.

Citations


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References


Jeong, KJ; Park, SY; et al. Lysophosphatidic acid receptor 2 and Gi/Src pathway mediate cell motility through cyclooxygenase 2 expression in CAOV-3 ovarian cancer cells. EXPERIMENTAL AND MOLECULAR MEDICINE 40:607-616(2008).
RADER, DJ; CASTRO, G; et al. INVIVO METABOLISM OF APOLIPOPROTEIN A-I ON HIGH-DENSITY-LIPOPROTEIN PARTICLES LPA-I AND LPA-I,A-II. JOURNAL OF LIPID RESEARCH 32:1849-1859(1991).

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