prospec
RBP4 Human

RBP4 Human

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  • RBP4 Human

  • Retinol Binding Protein-4 Human Recombinant
  • CYT-535
  • Shipped with Ice Packs

Catalogue number

CYT-535

Synonyms

Retinol Binding Protein 4, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.

Introduction

Retinol binding protein 4(RBP4) belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. This protein was found to be expressed and secreted by adipose tissue, and was strongly associated with insulin resistance. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli.
RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the rbp-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

Description

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.

Source

Escherichia Coli.

Physical Appearance

Sterile Filtered colorless solution.

Formulation

1 mg/ml in PBS pH-7.4.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Amino acid sequence

MERDCRVSSF RVKENFDKAR FSGTWYAMAK KDPEGLFLQD NIVAEFSVDE TGQMSATAKGRVRLLNNWDV CADMVGTFTD TEDPAKFKMK YWGVASFLQK GNDDHWIVDT DYDTYAVQYS CRLLNLDGTC ADSYSFVFSR DPNGLPPEAQ KIVRQRQEEL CLARQYRLIV HNGYCDGRSE RNLL.

Safety Data Sheet

Usage

ProSpec'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.
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