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Key Documents

HPA004189

Sigma-Aldrich

Anti-HDLBP antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-HDL-binding protein antibody produced in rabbit, Anti-High density lipoprotein-binding protein antibody produced in rabbit, Anti-Vigilin antibody produced in rabbit

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.43

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human

technique(s)

immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

immunogen sequence

DMNQFGEGEQAKICLEIMQRTGAHLELSLAKDQGLSIMVSGKLDAVMKARKDIVARLQTQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQDKRAVE

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HDLBP(3069)

General description

HDLBP is a novel HDL receptor candidate gene with molecular mass of 95kDa. It is expressed almost in all endothelial cells. It is also found in human atherosclerosis.

Immunogen

Vigilin recombinant protein epitope signature tag (PrEST)

Application

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biochem/physiol Actions

HDLBP is mainly involved in the HDL metabolism although it lacks a transmembrane domain. It removes excess intracellular cholesterol. During cholesterol loading of cells, it binds to the high density lipoprotein (HDL) apolipoproteins for facilitating the removal of excess cholesterol from cells. The complex HDLBP protein possesses a 14 repeated KH domains similar to nucleic acid-binding proteins. The KH domains are responsible for direct polynucleotide interaction. It has another primary functional area in RNA metabolism, in addition to HDL metabolism. It helps in tRNA protection, mRNA stabilization and RNA transportation between the nucleus and cytoplasm. It has been reported that HDLBP has ability for adhering to the cytoplasmic t-RNA-protein complexes in human liver cells.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST86822

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A V Bocharov et al.
Biochemistry, 40(14), 4407-4416 (2001-04-04)
A new human 95 kDa high density lipoprotein (HDL)-binding protein (HBP) corresponding to a high affinity HDL-binding site with K(d) = 1.67 microg/mL and a capacity of 13.4 ng/mg was identified in human fetal hepatocytes. The HDL binding with the
H Kurata et al.
Nihon rinsho. Japanese journal of clinical medicine, 57(12), 2704-2710 (2000-01-19)
Several HDL binding proteins have recently cloned and their roles in HDL metabolism have been gradually elucidated. HBP (vigilin), which lacks a transmembrane domain, is responsive to cell cholesterol levels, however, its physiological roles remain unknown. SR-B1, a member of
G L McKnight et al.
The Journal of biological chemistry, 267(17), 12131-12141 (1992-06-15)
Plasma membranes of cultured cells contain high affinity receptors for high density lipoprotein (HDL) that appear to mediate removal of excess intracellular cholesterol. Recent studies using ligand blot analysis have identified a 110-kDa membrane protein which has features predicted for
D S Chiu et al.
Arteriosclerosis, thrombosis, and vascular biology, 17(11), 2350-2358 (1997-12-31)
Accumulation of cholesteryl esters within cells of the arterial intima is a hallmark of atherosclerosis. A small number of proteins have been shown in vitro to be upregulated by cellular cholesterol loading, including apolipoprotein E (apoE) and the recently cloned

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