|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive ,Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A myc tag is a polypeptide protein tag derived from the c-myc gene product that can be added to a protein using recombinant DNA technology. It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild type protein expressed by the host organism. It can also be used in the isolation of protein complexes with multiple subunits.
A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.
The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.
|Human Leptin ORF mammalian expression plasmid, C-GFPSpark tag||HG10221-ACG|
|Human Leptin ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10221-ACR|
|Human Leptin ORF mammalian expression plasmid, C-Flag tag||HG10221-CF|
|Human Leptin ORF mammalian expression plasmid, C-His tag||HG10221-CH|
|Human Leptin ORF mammalian expression plasmid, C-Myc tag||HG10221-CM|
|Human Leptin ORF mammalian expression plasmid, C-HA tag||HG10221-CY|
|Human Leptin Gene cDNA clone plasmid||HG10221-M|
|Human Leptin natural ORF mammalian expression plasmid||HG10221-M-N|
|Human Leptin ORF mammalian expression plasmid, N-Flag tag||HG10221-NF|
|Human Leptin ORF mammalian expression plasmid, N-His tag||HG10221-NH|
|Human Leptin ORF mammalian expression plasmid, N-Myc tag||HG10221-NM|
|Human Leptin ORF mammalian expression plasmid, N-HA tag||HG10221-NY|
|Human Leptin natural ORF mammalian expression plasmid||HG10221-UT|
|Learn more about expression Vectors|
Leptin is one of the most important hormones secreted by adipocytes, as an adipokine that modulates multiple functions including energy homeostasis, thermoregulation, bone metabolism, endocrine and pro-inflammatory immune responses. The circulating leptin levels serve as a gauge of energy stores, thereby directing the regulation of energy homeostasis, neuroendocrine function, and metabolism. Recent studies suggest that leptin is physiologically more important as an indicator of energy deficiency, rather than energy excess, and may mediate adaptation by driving increased food intake and directing neuroendocrine function to converse energy, such as inducing hypothalamic hypogonadism to prevent fertilization. One of these functions is the connection between nutritional status and immune competence. The adipocyte-derived hormone Leptin has been shown to regulate the immune response, innate and adaptive response, both in normal and pathological conditions. Thus, Leptin is a mediator of the inflammatory response. Leptin has a dual effect on bone, acting by two independent mechanisms. As a signal molecule with growth factor characteristics, leptin is able to stimulate osteoblastic cells and to inhibit osteoclast formation and activity, thus promoting osteogenesis. However, as a molecule which stimulates sympathetic neurons in the hypothalamus, leptin indirectly inhibits bone formation. This inhibitory effect of leptin mediated by activation of sympathetic nervous system can be abrogated by application of blood pressure-reducing beta-blockers, which also inhibit receptors of hypothalamic adrenergic neurons. Leptin appears to regulate a number of features defining Alzheimer's disease (AD) at the molecular and physiological level. Leptin can stimulate mitogenic and angiogenic processes in peripheral organs. Because leptin levels are elevated in obese individuals and excess body weight has been shown to increase breast cancer risk in postmenopausal women. Furthermore, a recent report clearly shows that targeting leptin signaling may reduce mammary carcinogenesis.