Human Leptin pegylated super antagonist (mutant D23L/L39A/D40A/F41A)

Slide this table

Cat-Nr.500-045
Size100 µg
Price390 €
SourceE. coli
LabelPEG
Formulationlyophilized
Purity Confirmation> 98.0% as determined by Gel filtration and SDS-PAGE gel.
Length [aa]146
Molecular Weight35.6 kDa
N Terminal SequenceAVPIQ
Endotoxin Levels< 0.1 ng/µg of protein (<1EU/µg)
Biological ActivityRecombinantr human pegylated leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
Species ReactivityHuman
ReconstitutionIt is recommended to reconstitute the lyophilized human pegylated leptin antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
SynonymsLep; ob; obese
DescriptionMono-pegylated (with 20 kDa PEG) recombinant super human leptin antagonist is one polypeptide chain containing 146 amino, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus, having an expected molecular mass of ~ 35.6 kDa as determined by MS. However due to enlarged hydrodymanic volume human pegylated leptin antagonist runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Super human leptin antagonist (SHLA) was initially mutated, resulting in D23L/L39A/D40A/F41A mutant that was purified by proprietary chromatographic techniques. Pegylation of human leptin antagonist similar to that described in Elinav et al. Endocrinology 150:3083-91 (2009) for PEG-MLA. More details can be found in Shpilman at al., J. Biol. Chem. 286:4439-42 (2011).
Protein SequenceAVPIQKVQDDTKTLIKTIVTRINLISHTQSVSSKQKVTGAAAAPGLHPILTLSKMDQTLAVYQQILTSMPSRNVIQISNDLENLRDLLHVLAFSKSCHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLSPGC
Uniprot IDP41159
Protein RefSeqNP_000221.1
mRNA RefSeqNM_000230

All prices plus VAT + possible delivery charges