Filtered White lyophilized (freeze-dried) powder.
Greater than 95% as determined by SDS-PAGE.
Resistin Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 93 amino acids and having a total molecular weight of 19.7kDa.
The Resistin Human Recombinant protein is purified by standard chromatographic techniques.
Resistin, encoded by the RSTN gene, is a peptide hormone classified as a cysteine-rich secreted protein within the RELM family. It is also known as ADSF (Adipose Tissue-Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin, initially a 108-amino acid prepeptide, undergoes signal peptide cleavage before secretion, resulting in a circulating dimeric protein. This dimer comprises two 92-amino acid polypeptides linked by a disulfide bond at Cys26.
Primarily produced and secreted by adipocytes in mice, resistin interacts with skeletal muscle myocytes, hepatocytes, and adipocytes, reducing their sensitivity to insulin. Studies by Steppan et al. suggest that resistin can suppress glucose uptake stimulation and is found at elevated levels in the blood of obese mice. Conversely, fasting and antidiabetic drugs seem to downregulate its presence. However, contrasting findings by Way et al. indicate that resistin expression is significantly reduced in obesity and upregulated by certain antidiabetic medications.
Further research reveals that while mouse resistin levels increase during adipocyte differentiation, it might also hinder adipogenesis. In contrast, human adipogenic differentiation appears to correlate with a downregulation of resistin gene expression.
Recombinant Human Resistin, produced in E. coli, is a non-glycosylated, homodimeric polypeptide chain. It consists of two chains, each containing 93 amino acids, resulting in a total molecular weight of 19.7 kDa.
The purification of Recombinant Human Resistin is achieved using standardized chromatographic techniques.
Filtered White lyophilized (freeze-dried) powder.
Greater than 95% purity as determined by SDS-PAGE analysis.
Sterile filtered and lyophilized from a solution containing 0.1% Trifluoroacetic Acid (TFA).
For reconstitution, it is recommended to dissolve the lyophilized Resistin in sterile 18 MΩ-cm H2O at a concentration of 100 µg/ml. This solution can be further diluted into other aqueous solutions as needed.
MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP
Resistin was first discovered in mice, where it was proposed as a link between obesity and diabetes. In these early studies, resistin was found to be secreted by adipocytes and was associated with insulin resistance . However, subsequent research revealed significant differences between resistin’s role in rodents and humans.
In humans, resistin is predominantly expressed in immune cells, such as peripheral-blood mononuclear cells (PBMCs), rather than adipocytes . Human resistin is considered a pro-inflammatory molecule that plays a regulatory role in various chronic inflammatory diseases, metabolic diseases, infectious diseases, and cancers .
Resistin is an 11 kDa or 12.5 kDa protein consisting of 94 and 108 amino acids in mice and humans, respectively . Its structure comprises a carboxy-terminal disulfide-rich β-sandwich “head” domain with positive electrostatic surfaces and an amino-terminal α-helical “tail” segment with negative electrostatic potential .
Human resistin has been implicated in several diseases:
Recombinant resistin refers to the protein produced through recombinant DNA technology, which allows for the expression of human resistin in various host systems. This technology enables researchers to study the protein’s structure, function, and role in disease more effectively.