IL 32A Human, His

Interleukin-32 alpha Human Recombinant , His Tag

Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-131 a.a.) and having a molecular mass of 19.1 kDa. The IL-32 is fused to a 37 amino acid His Tag at N-terminus and purified by conventional chromatography.
Shipped with Ice Packs
Cat. No.
BT4518
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

IL 33 Human

Interleukin-33 Human Recombinant

Interleukin33 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 18,125 Dalton.
The IL-33 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4688
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IL 33 Human, His

Interleukin-33 Human Recombinant, His Tag

Interleukin-33 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 159 amino acids C-terminal fragment (112-270) having a molecular weight of 22.49kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The IL-33 His is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4812
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

IL 33 Mouse

Interleukin-33 Mouse Recombinant

Interleukin33 Mouse recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 17.7 kDa.

Shipped with Ice Packs
Cat. No.
BT4910
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IL 33 Rat

Interleukin-33 Rat Recombinant

IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a molecular mass of 17.4kDa.
The IL 33 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4983
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IL 33 Rat, His

Interleukin-33 Rat Recombinant, His Tag

IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (109-264 a.a) and having a molecular mass of 19.8kDa.
IL 33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5059
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

IL 4 Human

Interleukin-4 Human Recombinant

Interleukin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 15kDa.
The IL-4 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5159
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IL 4 Human, HEK

Interleukin-4 Human Recombinant, HEK

IL-4 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 14-19kDa due to glycosylation.
The IL-4 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5210
Source
HEK.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

IL 4 Human, His

Interleukin-4 Human Recombinant, His Tag

Interleukin-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 150 amino acids fragment (25-153) and having a total molecular mass of 17.2kDa.
The IL-4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5289
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

IL 4 Human, Yeast

Interleukin 4 Human Recombinant, Yeast

Interleukin-4 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 129 amino acids.
The IL-4 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5355
Source
Pichia pastoris.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

Interleukins (ILs) are a group of cytokines, which are secreted proteins and signal molecules primarily produced by leukocytes (white blood cells). They play a crucial role in the immune system by mediating communication between cells . The human genome encodes more than 50 interleukins and related proteins . Interleukins are classified based on their structure and function, with common families including IL-1, IL-2, IL-6, and IL-12 .

Biological Properties

Key Biological Properties: Interleukins are biologically active glycoproteins derived primarily from activated lymphocytes and macrophages . They induce T-lymphocyte activation and proliferation, augment neutrophil, macrophage, and T-lymphocyte cytotoxicity, and promote B lymphocyte and multilineage bone marrow stem-cell precursor growth and differentiation .

Expression Patterns and Tissue Distribution: Interleukins are produced by various cell types, including immune cells like macrophages and lymphocytes . They are expressed in different tissues, such as the bone marrow, thymus, and other epithelial cells .

Biological Functions

Primary Biological Functions: Interleukins modulate the growth, differentiation, and activation of immune cells during inflammatory and immune responses . They play a role in both innate and adaptive immune responses .

Role in Immune Responses and Pathogen Recognition: Interleukins are involved in the regulation of immune responses, inflammatory reactions, and hematopoiesis . They help coordinate the body’s response to infections, inflammation, and other immune challenges .

Modes of Action

Mechanisms with Other Molecules and Cells: Interleukins interact with specific cell surface receptors to stimulate target cells . For example, IL-6 controls leucocyte recruitment, determines the activity and maintenance of the inflammatory infiltrate, and drives various innate and adaptive immune responses .

Binding Partners and Downstream Signaling Cascades: Interleukins bind to their respective receptors, triggering downstream signaling pathways such as the Janus kinase (JAK)-signal transducer and activator of transcription (STAT) pathways . These signaling cascades lead to various cellular responses, including proliferation, differentiation, and cytokine production .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of interleukins are regulated by complex molecular mechanisms. For example, IL-10 production is regulated by metabolic pathways and molecular signals downstream of the IL-10 receptor .

Transcriptional Regulation and Post-Translational Modifications: Interleukins undergo transcriptional regulation and post-translational modifications to ensure proper function. These modifications can include phosphorylation, glycosylation, and cleavage .

Applications

Biomedical Research: Interleukins are extensively studied in biomedical research for their roles in immune regulation and disease pathogenesis .

Diagnostic Tools: Interleukins serve as biomarkers for various diseases, aiding in diagnosis and monitoring of disease progression .

Therapeutic Strategies: Interleukins are used in therapeutic strategies, such as cancer immunotherapy and treatment of autoimmune diseases . For example, engineered cytokines from the IL-2 family have shown significant effects in tumor immunotherapy .

Role in the Life Cycle

Role Throughout the Life Cycle: Interleukins play essential roles throughout the life cycle, from development to aging and disease. They regulate hematopoiesis, immune responses, and inflammation . For instance, IL-5 regulates eosinophil proliferation and differentiation, while IL-1 is involved in inflammatory responses .

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