RBP Human, Native

Retinol Binding Protein Native Human

Human Retinol Binding Protein Native produced in urine from the patients with renal tubular proteinuria having a molecular mass of approximately 21kD.

Shipped with Ice Packs
Cat. No.
BT1224
Source

Urine from the patients with renal tubular proteinuria.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

RBP1 Human

Retinol Binding Protein-1 Human Recombinant

RBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a.) and having a molecular mass of 24.7kDa.
RBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1298
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

RBP2 Human

Retinol Binding Protein-2 Human Recombinant

RBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (1-134 a.a.) and having a molecular mass of 18kDa. RBP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1402
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

RBP3 Human

Retinol Binding Protein-3 Human Recombinant

RBP3 Human Recombinant (321-630a.a) produced in E.Coli is a single, non-glycosylated Polypeptide chain. RBP3 is fused to a 6 a.a His tag at N-terminal and is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT1475
Source

Escherichia Coli.

Appearance
Filtered White lyophilized (freeze-dried) powder.

RBP4 Human

Retinol Binding Protein-4 Human Recombinant

RBP-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (19-201 a.a.) containing 184 amino acids and having a molecular mass of 21 kDa.
The Retinol Binding Protein-4 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1547
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

RBP4 Human, His

Retinol Binding Protein-4 Human Recombinant, His tag

RBP-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 183 amino acids fragment (19-201) corresponding to the mature Retinol Binding Protein, having a total molecular mass of 25.57kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The RBP4 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT1628
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

RBP4 Mouse

Retinol Binding Protein-4 Mouse Recombinant, BioActive

RBP4 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 191 amino acids (19-201 a.a) and having a molecular mass of 22.4kDa. RBP4 is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT1717
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

RBP5 Human

Retinol Binding Protein-5 Human Recombinant

RBP5 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids (1-135 a.a.) and having a molecular mass of 18.1kDa. The RBP5 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1770
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

RBP7 Human

Retinol Binding Protein-7 Human Recombinant

RBP7 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids (1-134 a.a.) and having a molecular mass of 17.6kDa. The RBP7 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT1830
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless 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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