RBP Human, Native

Retinol Binding Protein Native Human

This product consists of naturally-produced Human Retinol Binding Protein, isolated from the urine of patients with renal tubular proteinuria. Its molecular weight is approximately 21 kDa.

Shipped with Ice Packs
Cat. No.
BT1224
Source

Urine from the patients with renal tubular proteinuria.

Appearance

Sterile, white powder, freeze-dried and filtered.

RBP1 Human

Retinol Binding Protein-1 Human Recombinant

Recombinant human RBP1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 220 amino acids (1-197 a.a.). With a molecular weight of 24.7kDa, it includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1298
Source
E.coli.
Appearance
Colorless, sterile filtered solution.

RBP2 Human

Retinol Binding Protein-2 Human Recombinant

Recombinant human RBP2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 158 amino acids (specifically, amino acids 1 to 134). With a molecular weight of 18 kDa, RBP2 is fused to a 24 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1402
Source
E.coli.
Appearance
A sterile, colorless solution that has been filtered.

RBP3 Human

Retinol Binding Protein-3 Human Recombinant

This product is a recombinant human RBP3 protein, specifically the 321-630a.a fragment, produced in E. coli bacteria. It's a single, non-glycosylated polypeptide chain with a 6-amino acid Histidine tag at the N-terminus. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT1475
Source

Escherichia Coli.

Appearance
White powder, freeze-dried and filtered.

RBP4 Human

Retinol Binding Protein-4 Human Recombinant

Recombinant Human RBP-4, produced in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 19-201. This protein consists of 184 amino acids, resulting in a molecular weight of 21 kDa. Purification of the Retinol Binding Protein-4 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT1547
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution.

RBP4 Human, His

Retinol Binding Protein-4 Human Recombinant, His tag

Recombinant Human RBP-4, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 183 amino acids (corresponding to amino acid residues 19-201 of the mature Retinol Binding Protein). This protein has a molecular weight of 25.57 kDa, including a 4.5 kDa N-terminal hexahistidine tag. Purification of RBP4 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT1628
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

RBP4 Mouse

Retinol Binding Protein-4 Mouse Recombinant, BioActive

This product consists of the Mouse Retinol Binding Protein 4 protein, engineered and produced using Sf9 insect cells infected with a baculovirus expression system. The protein is a single chain with a molecular weight of 22.4kDa, encompassing amino acids 19 to 201 of the native protein sequence. For purification and detection purposes, it also includes an 8 amino acid Histidine tag attached to the C-terminus. The protein is glycosylated, meaning it has undergone post-translational modification with sugar molecules, which is a common feature in naturally occurring proteins.
Shipped with Ice Packs
Cat. No.
BT1717
Source

Sf9, Baculovirus cells.

Appearance
A clear, colorless liquid that has been sterilized through filtration.

RBP5 Human

Retinol Binding Protein-5 Human Recombinant

Recombinant human RBP5, engineered with a 20 amino acid His tag at its N-terminus, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain consisting of 155 amino acids (1-135 a.a.) with a molecular weight of 18.1 kDa. Purification of RBP5 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1770
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

RBP7 Human

Retinol Binding Protein-7 Human Recombinant

Recombinant human RBP7, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It contains 154 amino acids (including a 20 amino acid His tag at the N-terminus, spanning residues 1-134) and has a molecular weight of 17.6 kDa. Purification of RBP7 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1830
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.
Definition and Classification

Retinol Binding Proteins (RBPs) are a family of proteins that serve as carriers for retinol (vitamin A) in the blood. They belong to the lipocalin family and are crucial for the transport of retinol from the liver to peripheral tissues . RBPs are classified into several types, including plasma retinol-binding protein (RBP4), cellular retinol-binding proteins (CRBP I/II), and cellular retinoic acid-binding proteins (CRABPs) .

Biological Properties

Key Biological Properties: RBPs are low-molecular-weight proteins (approximately 21 kDa) that bind retinol with high affinity . They form complexes with transthyretin (TTR) to prevent renal filtration .

Expression Patterns: RBP4 is primarily expressed in the liver, where it binds retinol and is secreted into the bloodstream . Other RBPs, such as CRBP I/II and CRABPs, are expressed in various tissues and are involved in intracellular retinoid transport and metabolism .

Tissue Distribution: RBPs are found in the liver, kidneys, and various other tissues. They are also present in the uterus, embryo, and extraembryonic tissues during pregnancy .

Biological Functions

Primary Biological Functions: The main function of RBPs is to transport retinol from the liver to peripheral tissues . Retinol is essential for vision, immune function, reproduction, and cellular differentiation .

Role in Immune Responses and Pathogen Recognition: Retinol and its metabolites play a crucial role in modulating immune responses. They are involved in the regulation of gene expression related to immune cell function .

Modes of Action

Mechanisms with Other Molecules and Cells: RBPs bind retinol and form a complex with TTR in the bloodstream . This complex interacts with specific membrane receptors, such as ‘stimulated by retinoic acid 6’ (STRA6), to deliver retinol to target cells .

Binding Partners and Downstream Signaling Cascades: RBPs interact with various binding partners, including TTR and STRA6, to facilitate retinol transport and signaling . The retinol-RBP complex is crucial for maintaining retinoid homeostasis and regulating downstream signaling pathways .

Regulatory Mechanisms

Transcriptional Regulation: The expression of RBPs is regulated by a multiprotein complex involving high mobility group A1, protein-associated splicing factor, and steroidogenic factor 1 . Cyclic AMP stimulation can also induce RBP expression .

Post-Translational Modifications: RBPs undergo various post-translational modifications that affect their stability and function. These modifications include phosphorylation and glycosylation .

Applications

Biomedical Research: RBPs are used as biomarkers for assessing vitamin A status and diagnosing renal tubular dysfunction . They are also studied for their role in retinoid homeostasis and related diseases .

Diagnostic Tools: Measurement of RBP levels in blood and urine is used to diagnose and monitor kidney diseases and vitamin A deficiency .

Therapeutic Strategies: RBPs are being explored as potential therapeutic targets for diseases related to retinoid metabolism, such as certain cancers and metabolic disorders .

Role in the Life Cycle

Development: RBPs are essential for embryonic development, as retinol is crucial for cell differentiation and growth . Proper retinol transport and metabolism are necessary for successful pregnancy and fetal development .

Aging and Disease: RBPs play a role in maintaining retinoid homeostasis throughout life. Dysregulation of RBP expression or function can lead to various diseases, including vision disorders, immune deficiencies, and metabolic syndromes .

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