Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 0.8-4 μg/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse Resistin protein Ser21-Ser114 |
Accession # | |
N-terminal Sequence | Ser21 |
Structure / Form | Homohexamer |
Protein/Peptide Type | Recombinant Proteins |
Gene | Retn |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 10.2 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE | 10 kDa, under reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 500 μg/mL in sterile PBS. |
Resistin (resistance-to-insulin), also known as adipocyte-specific secretory factor (ADSF) and found in inflammatory zone 3 (FIZZ3), is a 10 kDa member of a small family of secreted cysteine-rich peptide hormones. These molecules purportedly play some role in inflammation, glucose metabolism, and angiogenesis (1, 2, 3, 4). Mouse Resistin precursor is 114 amino acids (aa) in length. It contains a 20 aa signal sequence plus a 94 aa mature region. The mature region shows an N-terminal alpha -helical tail (aa 27 - 48) and a C-terminal beta -sheet globular head (aa 51 - 112) (5, 6). The Resistin molecule circulates as either a noncovalent trimer (minor form), or a disulfide-linked homohexamer (major form). Noncovalent trimers are generated when the alpha -helical segments self-associate to form a three-stranded coiled-coil structure. Covalent hexamers subsequently appear when the free Cys at position #26 is engaged by adjacent trimers. It is hypothesized that the hexamer is a less active form of the molecule, and bioactivity is achieved at the target site by disulfide bond reduction (5). Although Resistin family molecules can noncovalently interact to form heterotrimers in vitro, there is no evidence to suggest this occurs in vivo with Resistin (7, 8). Mature mouse Resistin shares 72% and 56% aa identity with rat and human Resistin, respectively. Rat Resistin possesses an alternate start site at Met48; this Met is not found in the mouse molecule, however (9). Rodent Resistin is expressed by white adipocytes, splenocytes, astrocytes, and anterior pituitary epithelium (6, 10, 11). Although the function of Resistin is unclear, it would seem to block insulin-stimulated uptake of glucose by adipocytes, and promote glucose release by hepatocytes (6, 12, 13). As such, it has been proposed to participate in diet-induced insulin-sensitivity. Diets high in fat promote an increase in overall adipocyte size. Hypertrophic adipocytes are known to secrete TNF-alpha , which acts locally to block ACRP30 production. Since ACRP30 is an insulin-sensitizer, a drop in ACRP30 availability leads to insulin-insensitivity, which drives increased insulin production (a compensatory mechanism). High insulin induces Resistin secretion, which now antagonizes insulin action, prompting more insulin production, and more Resistin secretion (14).
"Get the skinny" on Adiponectin & Leptin Antibodies We at Novus Biologicals have an extensive antibody catalog covering lipid and metabolism research, including Adiponectin and leptin antibody products.Excess body fat is linked to many human diseases, including IRS (insulin resistance syndrome), type... Read full blog post. |
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