Recombinant Human Proinsulin protein INS-315H

Recombinant Human Proinsulin protein

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Recombinant Human Proinsulin protein

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Cat.No. : INS-315H
Product Overview : Recombinant Human Proinsulin(Phe25 -Asn110) was expressed in E. coli.
Description : After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5' region and with the IGF2 gene at the 3' region. Alternative splicing results in multiple transcript variants.
Source : E. coli
Species : Human
Molecular Mass : 9394.67 Da
AA Sequence : FVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTS ICSLYQLENYCN
Purity : >99%
Storage : Lyophilized peptide is shipped at ambient temperature.12 months from date of receipt, -20°C to -70 °C as supplied.3 months, -20°C to -70 °C under sterile conditions after reconstitution.1 month, 2 to 8 °C under sterile conditions after reconstitution.Avoid multiple freeze-thaw cycles.
Reconstitution : Reconstitute to 1.0mg/mL in sterile phosphate buffered saline.
Gene Name : INS insulin [ Homo sapiens ]
Official Symbol : INS
Synonyms : INS; insulin; proinsulin; ILPR; IRDN; IDDM2; MODY10;
Gene ID : 3630
mRNA Refseq : NM_000207
Protein Refseq : NP_000198
MIM : 176730
UniProt ID : P01308
Chromosome Location : 11p15.5
Pathway : ATF-2 transcription factor network, organism-specific biosystem; Adipogenesis, organism-specific biosystem; Aldosterone-regulated sodium reabsorption, organism-specific biosystem; Aldosterone-regulated sodium reabsorption, conserved biosystem; Amyloids, organism-specific biosystem; Arf6 trafficking events, organism-specific biosystem; Developmental Biology, organism-specific biosystem;
Function : hormone activity; hormone activity; hormone activity; insulin receptor binding; insulin receptor binding; insulin-like growth factor receptor binding; protein binding;

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