RBP7 Human

Retinol Binding Protein-7 Human Recombinant
Cat. No.
BT1830
Source
Escherichia Coli.
Synonyms
Retinoid-binding protein 7, Cellular retinoic acid-binding protein 4, CRABP4, CRBP4, Cellular retinoic acid-binding protein IV, CRABP-IV, RBP7, MGC70641.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
RBP7, a member of a superfamily of small cytoplasmic proteins, interacts with hydrophobic ligands. This cytoplasmic protein, similar to CRBP I and CRBP II, forms β-barrel structures and plays a role in the intracellular transport of retinol. RBP7, a recently identified cellular retinol carrier, is found in the kidney, heart, and transverse colon in humans.
Description
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.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The RBP7 solution is provided at a concentration of 0.5 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.2M NaCl, 2mM DTT, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure long-term stability during frozen storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90.0% using SDS-PAGE analysis.
Synonyms
Retinoid-binding protein 7, Cellular retinoic acid-binding protein 4, CRABP4, CRBP4, Cellular retinoic acid-binding protein IV, CRABP-IV, RBP7, MGC70641.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPADLSGTWT LLSSDNFEGY MLALGIDFAT RKIAKLLKPQ KVIEQNGDSF TIHTNSSLRN YFVKFKVGEE FDEDNRGLDN RKCKSLVIWD NDRLTCIQKG EKKNRGWTHW IEGDKLHLEM FCEGQVCKQT FQRA.

Product Science Overview

Gene and Protein Structure

The RBP7 gene is located on human chromosome 1p36.22 and encodes a protein consisting of 134 amino acids . The protein binds all-trans-retinol, although it has a lower binding affinity compared to other CRBPs . This binding is vital for the intracellular transport of retinol, ensuring its availability for metabolic processes .

Function and Importance

RBP7 plays a significant role in several biological processes, including:

  • Vitamin A Metabolism: It helps in the transport and stability of retinol, which is essential for vision, immune function, and cellular growth .
  • Adipogenesis: RBP7 is involved in the formation of adipose (fat) tissue .
  • Response to Cold Exposure: It plays a role in the body’s response to cold environments .
  • Nutritional Treatment: RBP7 is important in the body’s adaptation to different nutritional states .
Clinical Relevance

RBP7 has been studied for its potential role in various health conditions:

  • Hypertension: It has been implicated in the regulation of blood pressure .
  • Cancer: RBP7 functions as a tumor suppressor in hormone receptor-positive breast cancer .
  • Endothelial Function: It is an endothelium-specific gene regulated by PPARγ, a nuclear receptor involved in fat metabolism and inflammation .
Research and Applications

Human recombinant RBP7 is used in research to study its function and potential therapeutic applications. By understanding how RBP7 interacts with retinol and other molecules, scientists can develop new treatments for diseases related to vitamin A deficiency, metabolic disorders, and certain types of cancer .

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