Abcam, ab108897, Human Retinol binding protein 4 ELISA Kit (RBP4)

Size: 1 x 96Tests
Human Retinol binding protein 4 ELISA Kit (RBP4) is a Sandwich (quantitative) ELISA for the measurement of Human Retinol binding protein 4 (RBP4) in Human in Biofluids, Cell/Tissue Extracts samples.
Key facts
Detection method:Colorimetric,
Sample types:Cerebral Spinal Fluid, Milk, Plasma, Saliva, Serum, Urine, Cell Lysate, Tissue,
Reacts with:Human,
Assay type:Sandwich (quantitative),
Sensitivity:= 8.3 ng/mL,
Range:12.5 - 800 ng/mL,
Assay time:4h,
Assay Platform:Microplate

Product details:
Abcam's Retinol binding protein 4 (RBP4) Human
in vitro
ELISA (Enzyme-Linked Immunosorbent Assay) kit is designed for the quantitative measurement of Retinol binding protein 4 concentrations in plasma, serum, saliva, urine, milk, cerebrospinal fluid and cell culture supernatants.
A Retinol binding protein 4 specific antibody has been precoated onto 96-well plates and blocked. Standards or test samples are added to the wells and subsequently a Retinol binding protein 4specific biotinylated detection antibody is added and then followed by washing with wash buffer. Streptavidin-Peroxidase Conjugate is added and unbound conjugates are washed away with wash buffer. TMB is then used to visualize Streptavidin-Peroxidase enzymatic reaction. TMB is catalyzed by Streptavidin-Peroxidase to produce a blue color product that changes into yellow after adding acidic stop solution. The density of yellow coloration is directly proportional to the amount of Retinol binding protein 4 captured in plate.
Get higher sensitivity in only 90 minutes with Human Retinol Binding Protein 4 ELISA Kit (
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range.
The entire kit may be stored at -20°C for long term storage before reconstitution - Avoid repeated freeze-thaw cycles.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions-Multi, Storage information-Please refer to protocols

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
RBP4 or retinol-binding protein 4 is a carrier protein that is essential for the transport of retinol or vitamin A in the bloodstream. Also known by the names RBP or plasma retinol-binding protein this protein has a molecular weight of approximately 21 kDa. RBP4 is mainly expressed in the liver and secreted into the blood where it binds to retinol and protects it from oxidation. The structure of RBP4 allows it to fit into binding pockets facilitating the transport of retinol to peripheral tissues.
Biological function summary
RBP4 plays a role as a transporter of vitamin A from the liver to tissues where it is needed. It forms complexes with transthyretin in the blood which prevents kidney filtration and subsequent loss of retinol. This function ensures the proper delivery and availability of retinol essential for vision cellular differentiation and immune system function. The stability of the retinol-RBP4 complex is important to maintaining sufficient vitamin A levels in the body.
Pathways
RBP4 is significant in the vitamin A metabolism pathway and affects the retinoid signaling pathways. These pathways are critical for processes such as vision and skin health. RBP4 interacts with proteins like lecithin retinol acyltransferase (LRAT) in these pathways which are responsible for esterifying retinol into retinyl esters a storage form of vitamin A. These interactions ensure the efficient transport and storage of vitamin A and that it is accessible when needed by different tissues.
RBP4 is linked to the development of insulin resistance and type 2 diabetes. Elevated RBP4 levels correlate with these conditions and highlight its role in metabolic processes. Studies also show a connection between altered RBP4 levels and obesity with insulin resistance often occurring in conjunction with obesity. The protein is implicated in these metabolic disorders through its interactions with insulin-regulating proteins which influence glucose homeostasis.