IL 16 Human, (130 a.a.)

Interleukin-16 Human Recombinant, (130 a.a.)
Cat. No.
BT30890
Source
Escherichia Coli.
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 13.5 kDa.
The IL-16 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-16 (IL-16) is a multifunctional cytokine that plays roles in chemotaxis, T cell activation modulation, and HIV replication inhibition. It exerts its effects by binding to the CD4 receptor. IL-16 undergoes proteolytic processing, resulting in two functional proteins. The C-terminal peptide, generated through this processing, is responsible for the cytokine's biological activities, while the N-terminal fragment might be involved in cell cycle regulation. Caspase 3 has been implicated in the proteolytic cleavage of IL-16. This gene exhibits two transcript variants that encode distinct protein isoforms. IL-16 exhibits chemoattractant properties towards CD4+ lymphocytes, monocytes, and eosinophils, inducing their migration. Furthermore, it stimulates the expression of the interleukin-2 receptor, the ligand for CD4, on T lymphocytes.
Description
Recombinant Human Interleukin-16, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 130 amino acids with a molecular weight of 13.5 kDa. The purification of IL-16 is achieved using proprietary chromatographic methods.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The lyophilization of IL-16 was carried out at a concentration of 1 mg/ml in 10mM NaP buffer with a pH of 7.5.
Solubility
For reconstitution of the lyophilized Interleukin-16, sterile 18MΩ-cm H2O is recommended at a concentration of not less than 100 µg/ml. This reconstituted solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Interleukin-16, while stable at room temperature for a duration of 3 weeks, is best stored in a desiccated state at a temperature below -18°C. After reconstitution, it is advisable to store IL16 at 4°C for a period of 2-7 days. For long-term storage, freezing at -18°C is recommended. To enhance stability during long-term storage, the addition of a carrier protein, such as HSA or BSA, at a concentration of 0.1% is suggested. It is important to avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 90.0% as determined by the following methods: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50, determined by the cytokine's ability to induce chemotaxis in human CD4+ T lymphocytes, falls within the range of 10-100 ng/ml. This corresponds to a specific activity of 10,000-100,000 units/mg.
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Asp-Leu-Asn.

Product Science Overview

Structure and Isoforms

IL-16 exists in multiple isoforms, which are cleaved from a precursor protein known as pre-Interleukin-16 . The biologically active form of IL-16 is a homotetramer composed of 14 kDa chains, each containing 130 amino acid residues . The recombinant form of IL-16, specifically the 130 amino acid variant, is a single non-glycosylated polypeptide chain expressed in E. coli .

Biological Activity

IL-16 plays a crucial role in the immune system by acting as a chemoattractant for CD4+ T lymphocytes. It is fully biologically active and its activity can be measured using a chemotaxis bioassay with human CD4+ T lymphocytes . The concentration range for its biological activity is typically between 1.0-100 ng/ml .

Applications and Storage

Recombinant IL-16 is used in various research applications, including studies on immune responses and cell signaling. It is typically purified using high-performance liquid chromatography (HPLC) and validated for bioactivity on appropriate cell lines . For storage, the lyophilized preparation is stable at 2-8°C but should be kept at -20°C for long-term storage. Upon reconstitution, it is most stable at -20 to -80°C .

Purity and Endotoxin Levels

The recombinant IL-16 protein is highly purified, with a purity greater than 95% as determined by SDS-PAGE and HPLC . The endotoxin level is less than 1 EU/μg, as determined by the Limulus Amebocyte Lysate (LAL) method .

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