Retinol Binding Protein / RBP Mouse Monoclonal Antibody [Clone ID: SPM442]

Specifications

Product Data
Clone Name	SPM442
Applications	IF, IHC, IP, WB
Recommend Dilution	ELISA: Use BSA free Antibody for coating. Immunofluorescence: 1-2 μg/ml. Western Blotting: 0.5-1 μg/ml. Immunoprecipitation: 1-2 μg/500 μg protein lysate. Immunohistochemistry on Frozen Sections: 1.-2 μg/ml for 30 minutes at RT. Positive Control: Liver or placenta.
Reactivity	Goat, Human, Monkey, Mouse, Rabbit, Rat
Host	Mouse
Clonality	Monoclonal
Immunogen	Human Retinol Binding Protein (RBP) purified from plasma.
Specificity	Recognizes a protein of 21kDa-25kDa, identified as retinol binding protein (RBP). Its epitope localizes between aa 74-182 of Human RBP. This Monoclonal Antibody recognizes reduced and carboxy-methylated RBP (RCM-RBP) as well as the circulatory RBP but not the native RBP, thereby suggesting that its epitope becomes accessible either on unfolding or upon binding of RBP to transthyretin (prealbumin). RBP is responsible for distributing retinol from the retinoid stores in the liver to the various target tissues. Once secreted into the blood with bound retinol, the vitamin carrier circulates complexed with transthyretin prior to vitamin delivery at the plasma membrane through a receptor-mediated mechanism. Cellular Localization: Cytoplasmic.
Formulation	10mM PBS State: Purified State: Liquid purified IgG fraction from Bioreactor Concentrate Stabilizer: 0.05% BSA Preservative: 0.05% Sodium Azide
Concentration	lot specific
Purification	Protein A/G Chromatography
Conjugation	Unconjugated
Storage Condition	Store undiluted at 2-8°C.
Predicted Protein Size	21-25 kDa
Background	Retinol Binding Protein is a single-chain glycoprotein belonging to the superfamily of hydrophobic molecule transporter proteins, which is responsible for the transport of Retinol (vitamin A1) from the liver to peripheral target tissues. RBP is synthesised by hepatic parenchymal cells where it becomes bound to its ligand retinol and is then released into the circulation, where it binds further to the protein transthyretin, to form a transporting complex. An increasing number of studies suggest that the subsequent release of retinol from RBP at the plasma membrane occurs through interaction of RBP with specific membrane receptors.
Reference Data

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