Human Leptin qA Recombinant Protein (RPPB0724)
- SKU:
- RPPB0724
- Product Type:
- Recombinant Protein
- Species:
- Human
- Research Area:
- Growth Factors & Cytokines
Frequently bought together:
Description
Product Name: | Human Leptin qA Recombinant Protein |
Product Code: | RPPB0724 |
Size: | 50µg |
Species: | Human |
Target: | Leptin qA |
Source: | Escherichia Coli |
Physical Appearance: | White lyophilized (freeze-dried) powder. |
Formulation: | The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3. |
Solubility: | It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100�g/ml, which can then be further diluted to other aqueous solutions. |
Stability: | Lyophilized Leptin Antagonist Quadruple Mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles. |
Purity: | Greater than 98.0% as determined by:(a) Gel filtration analysis.(b) Analysis by SDS-PAGE. |
Amino Acid Sequence: | The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln |
Biological Activity: | ProSpec�s Leptin Quadruple Antagonist Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays. |
Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.Leptin Antagonist Quadruple Mutant was purified by proprietary chromatographic techniques.