IL 16 Human, (121 a.a.)

Interleukin-16 Human Recombinant, (121 a.a.)
Cat. No.
BT30873
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 97.0% 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 121 amino acids and having a molecular mass of 12.4 kDa.
The IL-16 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Interleukin-16 (IL-16) is a multifunctional cytokine with a critical role in immune response regulation. Acting as a chemoattractant, it guides the movement of immune cells expressing the CD4 receptor, including T cells, monocytes, and eosinophils, to the site of inflammation. IL-16 also modulates T cell activation, influencing their proliferation and cytokine production. Notably, it has been identified as an inhibitor of HIV replication, highlighting its potential antiviral properties. The biological activities of IL-16 are mediated by its interaction with the CD4 receptor. This cytokine is synthesized as a precursor protein that undergoes proteolytic cleavage to generate mature, active IL-16. This process involves the enzyme caspase 3, which cleaves the precursor molecule into two fragments. While the C-terminal fragment embodies the chemoattractant and immune-modulatory functions of IL-16, the N-terminal fragment is suggested to participate in cell cycle regulation. Two distinct mRNA transcripts encoding IL-16 have been identified, resulting in the production of two isoforms of this cytokine. Overall, IL-16 exerts its effects by stimulating the migration of CD4+ immune cells, inducing the expression of the interleukin-2 receptor on T lymphocytes, and interacting with the CD4 receptor.
Description
Recombinant Human Interleukin-16, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 121 amino acids. This protein, with a molecular weight of 12.4 kDa, is purified to a high degree using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The lyophilized Interleukin-16 was prepared in a 0.2µm filtered concentrated solution of phosphate-buffered saline (PBS) at pH 7.4.
Solubility
To reconstitute the lyophilized Interleukin-16, it is recommended to dissolve it in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Interleukin-16 remains stable at room temperature for up to 3 weeks; however, it is advisable to store it desiccated at a temperature below -18°C for prolonged storage. After reconstitution, IL-16 should be stored at 4°C for 2-7 days. For long-term storage, it is recommended to add a carrier protein, such as 0.1% HSA or BSA, to the solution. Avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 97.0% as determined by:
(a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis.
(b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
This product demonstrates full biological activity comparable to the standard. Its activity is assessed based on its ability to chemoattract human CD4+ T lymphocytes at concentrations ranging from 50.0 to 100.0 ng/ml.
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Source
Escherichia Coli.
Amino Acid Sequence
SAASASAASD VSVESTAEAT VCTVTLEKMS AGLGFSLEGG KGSLHGDKPL TINRIFKGAA SEQSETVQPG DEILQLGGTA MQGLTRFEAW NIIKALPDGP VTIVIRRKSL QSKETTAAGD S

Product Science Overview

Structure and Composition

Recombinant human IL-16 (121 a.a.) is a non-glycosylated polypeptide chain consisting of 121 amino acids. The molecular weight of this protein is approximately 12.4 kDa . The amino acid sequence of IL-16 is as follows:

SAASASAASD VSVESTAEAT VCTVTLEKMS AGLGFSLEGG KGSLHGDKPL TINRIFKGAA SEQSETVQPG DEILQLGGTA MQGLTRFEAW NIIKALPDGP VTIVIRRKSL QSKETTAAGD S
Biological Function

IL-16 functions primarily as a chemoattractant for CD4+ T cells, monocytes, and eosinophils. It signals through the CD4 receptor, which is also the primary receptor for HIV . This cytokine undergoes proteolytic processing, resulting in two functional proteins. The secreted C-terminal peptide is responsible for the cytokine activity, while the N-terminal product may play a role in cell cycle control .

Production and Purification

Recombinant human IL-16 (121 a.a.) is typically produced in Escherichia coli (E. coli) expression systems. The protein is purified using high-performance liquid chromatography (HPLC) and SDS-PAGE gel analyses to ensure a purity of ≥ 98% . The endotoxin concentration is maintained at <1 EU/µg to ensure its safety and efficacy in research applications .

Applications

IL-16 is widely used in research to study its role in immune responses and its potential therapeutic applications. It is particularly valuable in investigating T cell activation, chemoattraction, and HIV inhibition mechanisms .

Storage and Handling

Recombinant human IL-16 (121 a.a.) is typically lyophilized and should be stored at -20°C for long-term stability. Upon reconstitution, it is recommended to store the protein at 2-8°C for short-term use and at -20°C to -70°C for long-term storage . Avoid repeated freeze-thaw cycles to maintain its stability and activity .

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