Rantes Human

Rantes Human Recombinant (CCL5)
Cat. No.
BT22732
Source
Escherichia Coli.
Synonyms
Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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

Rantes Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 68 amino acids and having a molecular mass of 7809.2 Dalton.
The Rantes is purified by proprietary chromatographic techniques.

Product Specs

Introduction
RANTES, also known as CCL5, is an 8 kDa chemokine that plays a crucial role in immune responses. It attracts and activates leukocytes, including T cells, eosinophils, and basophils, to inflammatory sites. RANTES also contributes to the activation of natural killer (NK) cells, leading to the formation of CC-Chemokine-activated killer (CHAK) cells. Additionally, RANTES exhibits HIV-suppressive properties. The gene encoding RANTES is located on chromosome 17 in humans.
Description
Recombinant human RANTES is produced in E. coli and purified to a single, non-glycosylated polypeptide chain. This protein consists of 68 amino acids and has a molecular weight of 7809.2 Daltons. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Sterile white lyophilized (freeze-dried) powder.
Formulation
Lyophilized from a 0.2 µm filtered solution containing 50 mM sodium acetate (pH 5.0) and 100 mM sodium chloride.
Solubility
To reconstitute lyophilized RANTES, dissolve in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. Further dilutions can be made using other aqueous solutions.
Stability
Lyophilized RANTES remains stable at room temperature for up to 3 weeks. For long-term storage, store desiccated below -18°C. After reconstitution, RANTES can be stored at 4°C for 2-7 days. For extended storage, add a carrier protein (0.1% HSA or BSA) and store below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 97.0%, as determined by RP-HPLC and SDS-PAGE analyses.
Biological Activity
The biological activity of RANTES is assessed by its ability to chemoattract human blood monocytes. A concentration range of 1-10 ng/ml corresponds to a specific activity of 100,000-1,000,000 IU/mg.
Synonyms
Small inducible cytokine A5, CCL5, T-cell-specific RANTES protein, SIS-delta, T cell- specific protein P228, TCP228, chemokine (C-C motif) ligand 5, SISd, SCYA5, RANTES, D17S136E, MGC17164.
Source
Escherichia Coli.
Amino Acid Sequence
SPYSSDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS.

Product Science Overview

Discovery and Nomenclature

RANTES was initially identified as a protein expressed and secreted by T cells upon activation. The name RANTES stands for Regulated upon Activation, Normal T-cell Expressed and Secreted. It has since been renamed to CCL5 to align with the standardized nomenclature for chemokines .

Structure and Function

CCL5 is a member of the C-C chemokine family, characterized by two adjacent cysteine residues near their amino terminus. The protein is produced by various cell types, including T cells, macrophages, and platelets. It is known for its ability to attract T cells, eosinophils, and basophils to inflammatory sites, thereby playing a significant role in the immune response .

Mechanism of Action

CCL5 exerts its effects by binding to specific receptors on the surface of target cells. The primary receptors for CCL5 are CCR1, CCR3, and CCR5. Upon binding to these receptors, CCL5 activates intracellular signaling pathways that lead to the migration of leukocytes to the site of inflammation .

Clinical Significance

Due to its role in recruiting immune cells, CCL5 is implicated in various inflammatory diseases, including asthma, rheumatoid arthritis, and multiple sclerosis. Elevated levels of CCL5 have been observed in these conditions, making it a potential target for therapeutic intervention .

Recombinant CCL5

Recombinant human CCL5 is produced using E. coli expression systems. The recombinant protein is typically purified to high levels of purity (>97%) and is used in various research applications, including studies on chemotaxis, inflammation, and immune response .

Applications in Research

Recombinant CCL5 is widely used in research to study its role in immune cell migration and its potential as a therapeutic target. It is also used in assays to measure the chemotactic activity of immune cells and to investigate the signaling pathways activated by CCL5 .

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