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Mouse Anti-GPIHBP1 Recombinant Antibody (1F9) (CBMAB-G4599-LY)

This product is antibody recognizes GPIHBP1. The antibody 1F9 immunoassay techniques such as: ELISA, WB.
See all GPIHBP1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
1F9
Antibody Isotype
IgG
Application
ELISA, WB

Basic Information

Immunogen
Full-length recombinant protein corresponding to aa19184 from human GPIHBP1 with a GST Tag. MW of the GST tag alone is 26kD. (NP_835466.1)
Specificity
Human
Antibody Isotype
IgG
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!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1
Introduction
This gene encodes a capillary endothelial cell protein that facilitates the lipolytic processing of triglyceride-rich lipoproteins. The encoded protein is a glycosylphosphatidylinositol-anchored protein that is a member of the lymphocyte antigen 6 (Ly6) family. This protein plays a major role in transporting lipoprotein lipase (LPL) from the subendothelial spaces to the capillary lumen. Mutations in this gene are the cause of hyperlipoproteinemia, type 1D. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2014]
Entrez Gene ID
338328
UniProt ID
Q8IV16
Alternative Names
Glycosylphosphatidylinositol Anchored High Density Lipoprotein Binding Protein 1; GPI Anchored High Density Lipoprotein Binding Protein 1; GPI-Anchored HDL-Binding Protein 1; Endothelial Cell LPL Transporter; GPI-HBP1; Glycosylphosphatidylinositol-Anchored High Density Lipoprotein-Binding Protein 1; High Density Lipoprotein-Binding Protein 1; HYPL1D; HBP1;
Function
Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries (By similarity).

Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries (By similarity).

Protects LPL against loss of activity, and against ANGPTL4-mediated unfolding (PubMed:27929370, PubMed:29899144).

Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis (PubMed:19304573, PubMed:21314738).

Binds chylomicrons and phospholipid particles that contain APOA5 (PubMed:17997385, PubMed:19304573).

Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL (By similarity).
Biological Process
Cholesterol homeostasis Source: BHF-UCL
Intracellular protein transport Source: BHF-UCL
Positive regulation of chylomicron remnant clearance Source: BHF-UCL
Positive regulation of lipoprotein lipase activity Source: ARUK-UCL
Protein import Source: BHF-UCL
Protein localization to cell surface Source: BHF-UCL
Protein stabilization Source: ARUK-UCL
Response to heparin Source: BHF-UCL
Transcytosis Source: BHF-UCL
Triglyceride homeostasis Source: BHF-UCL
Cellular Location
Apical cell membrane; Basolateral cell membrane; Cell membrane
Involvement in disease
Hyperlipoproteinemia 1D (HLPP1D):
An autosomal recessive disorder characterized by hyperlipoproteinemia, decreased plasma LPL levels in some patients, high plasma triglyceride levels, and refractory fasting chylomicronemia.
PTM
Glycosylation of Asn-78 is critical for cell surface localization.By similarity
Sulfation of a Tyr in the N-terminal acidic region increases the affinity for LPL.

Young, S. G., Song, W., Yang, Y., Birrane, G., Jiang, H., Beigneux, A. P., ... & Fong, L. G. (2022). A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism. Proceedings of the National Academy of Sciences, 119(36), e2211136119.

Kristensen, K. K., Leth-Espensen, K. Z., Kumari, A., Grønnemose, A. L., Lund-Winther, A. M., Young, S. G., & Ploug, M. (2021). GPIHBP1 and ANGPTL4 utilize protein disorder to orchestrate order in plasma triglyceride metabolism and regulate compartmentalization of LPL activity. Frontiers in Cell and Developmental Biology, 9, 702508.

Miyashita, K., Lutz, J., Hudgins, L. C., Toib, D., Ashraf, A. P., Song, W., ... & Beigneux, A. P. (2020). Chylomicronemia from GPIHBP1 autoantibodies. Journal of Lipid Research, 61(11), 1365-1376.

Eguchi, J., Miyashita, K., Fukamachi, I., Nakajima, K., Murakami, M., Kawahara, Y., ... & Beigneux, A. P. (2019). GPIHBP1 autoantibody syndrome during interferon β1a treatment. Journal of clinical lipidology, 13(1), 62-69.

Young, S. G., Fong, L. G., Beigneux, A. P., Allan, C. M., He, C., Jiang, H., ... & Ploug, M. (2019). GPIHBP1 and lipoprotein lipase, partners in plasma triglyceride metabolism. Cell metabolism, 30(1), 51-65.

Arora, R., Nimonkar, A. V., Baird, D., Wang, C., Chiu, C. H., Horton, P. A., ... & Trauger, J. W. (2019). Structure of lipoprotein lipase in complex with GPIHBP1. Proceedings of the National Academy of Sciences, 116(21), 10360-10365.

Birrane, G., Beigneux, A. P., Dwyer, B., Strack-Logue, B., Kristensen, K. K., Francone, O. L., ... & Meiyappan, M. (2019). Structure of the lipoprotein lipase–GPIHBP1 complex that mediates plasma triglyceride hydrolysis. Proceedings of the National Academy of Sciences, 116(5), 1723-1732.

Kristensen, K. K., Midtgaard, S. R., Mysling, S., Kovrov, O., Hansen, L. B., Skar-Gislinge, N., ... & Ploug, M. (2018). A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase. Proceedings of the National Academy of Sciences, 115(26), E6020-E6029.

Miyashita, K., Fukamachi, I., Nagao, M., Ishida, T., Kobayashi, J., Machida, T., ... & Nakajima, K. (2018). An enzyme-linked immunosorbent assay for measuring GPIHBP1 levels in human plasma or serum. Journal of clinical lipidology, 12(1), 203-210.

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

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