Resistin Mouse

Resistin Mouse Recombinant

Recombinant Mouse Resistin, produced in E. coli, is a non-glycosylated, homodimeric polypeptide chain composed of two chains of 95 amino acids, resulting in a total molecular mass of 20.6 kDa.

Purification of Resistin is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT21353
Source

Escherichia Coli.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Resistin Mouse, Flag

Resistin Mouse Recombinant, Flag Tag

The Resistin Mouse protein is engineered with a phage fd signal sequence (21 amino acids) and a C-terminal flagTag (10 amino acids). This results in a 13.7 kDa recombinant fusion protein comprising 93 amino acids of the Resistin Mouse sequence and 31 additional amino acids from the phage fd signal sequence and the flagTag (underlined).
Shipped with Ice Packs
Cat. No.
BT21419
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder that has been filtered.

Resistin Mutant Human

Resistin Mutant Human Recombinant

This product consists of a 9.9 kDa protein containing 93 amino acid residues and is produced in E.coli. The mutant form of Resistin has undergone a Cysteine residue mutation to prevent dimerization, potentially leading to antagonist activity.
Shipped with Ice Packs
Cat. No.
BT21500
Source
Escherichia Coli.

Resistin Rat

Resistin Rat Recombinant

Recombinant Rat Resistin, produced in E. coli, is a disulfide-linked homodimer. It comprises two polypeptide chains, each containing 95 amino acids, resulting in a molecular weight of approximately 20.2 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21596
Source

Escherichia Coli.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Resistin Rat, His

Resistin Rat Recombinant, His Tag

Recombinant Rat Resistin is produced with an N-terminal His tag. This His-tagged fusion protein is 11.9 kDa in size and comprises 94 amino acids from the Rat Resistin sequence plus an additional 16 amino acids forming the His tag (underlined).
Shipped with Ice Packs
Cat. No.
BT21687
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder following filtration.
Definition and Classification

Resistin, also known as adipose tissue-specific secretory factor (ADSF) or C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein (XCP1), is a cysteine-rich peptide hormone derived from adipose tissue. In humans, it is encoded by the RETN gene located on chromosome 19 . Resistin belongs to the family of resistin-like molecules (RELMs), which also includes RELMα, RELMβ, and RELMγ .

Biological Properties

Key Biological Properties: Resistin is a cysteine-rich protein with a molecular weight of approximately 12.5 kDa. It consists of 108 amino acids in humans and 114 amino acids in mice .

Expression Patterns and Tissue Distribution: In humans, resistin is predominantly expressed in immune cells such as monocytes and macrophages, while in rodents, it is primarily secreted by adipocytes . Resistin is found in various tissues, including bone marrow, spleen, and blood .

Biological Functions

Primary Biological Functions: Resistin plays a significant role in regulating glucose metabolism, lipid metabolism, and insulin resistance . It is also involved in inflammatory processes and has been linked to chronic inflammatory diseases, metabolic diseases, infectious diseases, and cancers .

Role in Immune Responses and Pathogen Recognition: Resistin functions as a host defense peptide of innate immunity, exhibiting wide-spectrum antimicrobial activity and modulating immune responses . It limits microbial product-induced inflammation and plays a regulatory role in chronic inflammatory diseases .

Modes of Action

Mechanisms with Other Molecules and Cells: Resistin interacts with various molecules and cells, including endothelial cells, smooth muscle cells, and immune cells . It influences several biological processes such as inflammation, endothelial dysfunction, thrombosis, and angiogenesis .

Binding Partners and Downstream Signaling Cascades: Resistin binds to receptors on target cells, activating signaling pathways such as the NF-κB pathway, which leads to the expression of pro-inflammatory cytokines like interleukin-1 (IL-1), interleukin-6 (IL-6), and tumor necrosis factor-α (TNF-α) . It also affects the phosphorylation state of enzymes like AMPK, influencing glucose metabolism .

Regulatory Mechanisms

Transcriptional Regulation: Resistin expression is regulated by various transcription factors, including PPARγ and C/EBP . These factors influence the transcriptional events leading to the production of resistin in different tissues.

Post-Translational Modifications: Resistin undergoes post-translational modifications that affect its stability and activity. These modifications include disulfide bond formation, which is crucial for its structural integrity and function .

Applications

Biomedical Research: Resistin is extensively studied for its role in metabolic diseases, particularly type 2 diabetes mellitus (T2DM) and obesity . It serves as a biomarker for these conditions and is used to understand the underlying mechanisms of insulin resistance .

Diagnostic Tools: Resistin levels are measured in clinical settings to diagnose and monitor inflammatory diseases and metabolic disorders . It is also explored as a potential diagnostic biomarker for sepsis .

Therapeutic Strategies: Targeting resistin and its signaling pathways is considered a therapeutic strategy for treating metabolic and inflammatory diseases. Inhibitors of resistin activity are being developed to improve insulin sensitivity and reduce inflammation .

Role in the Life Cycle

Development to Aging and Disease: Resistin plays a role throughout the life cycle, from development to aging. It is involved in energy homeostasis, glucose and lipid metabolism, and immune responses . Elevated resistin levels are associated with aging-related diseases such as T2DM, cardiovascular diseases, and chronic inflammatory conditions .

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