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Mouse Anti-LPA Recombinant Antibody (CBYCL-434) (CBMAB-L0335-YC)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYCL-434
Antibody Isotype
IgG1
Application
ELISA, IHC-P, WB

Basic Information

Immunogen
Purified recombinant fragment of LPA(4330-4521) expressed in E. coli
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
0.03% sodium azide
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 4330-4521

Target

Full Name
S. aureus MAGI2
Introduction
LPA 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.
Entrez Gene ID
4018
UniProt ID
P08519
Alternative Names
AK38; APOA; LP
Function
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.
Biological Process
Blood circulationManual Assertion Based On ExperimentTAS:ProtInc
Lipid metabolic process1 PublicationNAS:ProtInc
Lipid transportIEA:UniProtKB-KW
ProteolysisManual Assertion Based On ExperimentIBA:GO_Central
Cellular Location
Extracellular region
Extracellular space
Extrinsic component of plasma membrane
Plasma lipoprotein particle
PTM
N- and O-glycosylated. The N-glycans are complex biantennary structures present in either a mono- or disialylated state. The O-glycans are mostly (80%) represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated and non-sialylated O-glycans also detected.
More Infomation

Lau, F. D., & Giugliano, R. P. (2022). Lipoprotein (a) and its significance in cardiovascular disease: a review. Jama Cardiology.

Coassin, S., & Kronenberg, F. (2022). Lipoprotein (a) beyond the kringle IV repeat polymorphism: the complexity of genetic variation in the LPA gene. Atherosclerosis, 349, 17-35.

Gu, J. X., Huang, J., Li, S. S., Zhou, L. H., Yang, M., Li, Y., ... & Su, M. (2022). Elevated lipoprotein (a) and genetic polymorphisms in the LPA gene may predict cardiovascular events. Scientific Reports, 12(1), 3588.

Kamstrup, P. R. (2021). Lipoprotein (a) and cardiovascular disease. Clinical chemistry, 67(1), 154-166.

Trinder, M., Uddin, M. M., Finneran, P., Aragam, K. G., & Natarajan, P. (2021). Clinical utility of lipoprotein (a) and LPA genetic risk score in risk prediction of incident atherosclerotic cardiovascular disease. JAMA cardiology, 6(3), 287-295.

Ruscica, M., Sirtori, C. R., Corsini, A., Watts, G. F., & Sahebkar, A. (2021). Lipoprotein (a): Knowns, unknowns and uncertainties. Pharmacological research, 173, 105812.

Miksenas, H., Januzzi, J. L., & Natarajan, P. (2021). Lipoprotein (a) and cardiovascular diseases. JAMA, 326(4), 352-353.

Schachtl-Riess, J. F., Kheirkhah, A., Grüneis, R., Di Maio, S., Schoenherr, S., Streiter, G., ... & Coassin, S. (2021). Frequent LPA KIV-2 variants lower lipoprotein (a) concentrations and protect against coronary artery disease. Journal of the American College of Cardiology, 78(5), 437-449.

Langsted, A., Kamstrup, P. R., & Nordestgaard, B. G. (2019). High lipoprotein (a) and high risk of mortality. European heart journal, 40(33), 2760-2770.

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For research use only. Not intended for any clinical use.

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