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Recombinant Exendin-4

Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
HOR-269

Background:

Recombinant Exendin-4 is a glucagon like peptide-1 receptor agonist. The native hormone is produced in the gut of Gila monster Heloderma suspectrum (a type of reptile found in the desert) that stimulates insulin production without causing threateningly low blood sugar, which can occur after using insulin and some anti-diabetes products. Recently, researchers used extracted saliva from gila monsters to create an unprecedented breakthrough in Diabetes Type 2 treatment. Exedin-4 enhances glucose-dependant insulin secretion, suppresses inappropriately elevated glucagon secretion and slows gastric emptying in vivo. It also promotes B-cell proliferation and neogenesis in vitro and in animal models. Exedin-4 stimulates an increase in acinar cAMP, without stimulating the release of amylase.

Description:

Recombinant Exendin-4 is a novel 39-amino acids peptide having a molecular mass of 4186.7 dalton, which shares 53%, sequence homology with GLP-17-36 amide and interacts with the same membrane receptor.

Physical Appearance:

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation:

The protein (1mg/ml) was lyophilized after extensive dialyses against 20mM PBS and contains 4% mannitol.

Solubility:

It is recommended to reconstitute the lyophilized recombinant Exendin-4 in sterile 18MΩ-cm H2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.

Stability:

Lyophilized Recombinant Exendin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -180 C. Upon reconstitution Recombinant Exendin-4 should be stored at 40 C between 2-7 days and for future use below -180 C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

Purity:

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

Amino acid sequence:

The sequence determined and was found to be His-Gly-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Leu-Ser-Lys-Gln-Met-Glu-Glu-Glu-Ala-Val-Arg-Leu-Phe-Ile-Glu-Trp-Leu-Lys-Asn-Gly-Gly-Pro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser.

Dimers and aggregates:

Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

Endotoxin:

Less than 0.1 ng/ug (IEU/ug) of Recombinant Exendin-4.

Protein content:

Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280 nm.
2. Analysis by RP-HPLC, using a calibrated solution of Exendin-4 as a Reference Standard.

Usage:

Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.


Protein synonyms/aliases:

Exendin-4 precursor.

Protein Family:

Belongs to the glucagon family.

Protein Domains:


Domains:
IPR000532   Glucagon/GIP/secretin/VIP

Related proteins:

Recombinant Human Glucagon Like Peptide-1 (7-36)
Human Growth Hormone Releasing Hormone

Protein links:

Recombinant Exendin-4 protein domain

Recombinant Exendin-4 protein family


Precursor- Protein structure and amino acid sequence:


Latest Publications:

1. Exendin-4, but not glucagon-like peptide-1, is cleared exclusively by glomerular filtration in anaesthetised pigs.
Diabetologia 2006 Jan 31;:1-7
2. Exenatide (Exendin-4)-Induced Pancreatitis: A case report.
Diabetes Care 2006 Feb;29(2):471
3. Identification of transcriptional targets during pancreatic growth after partial pancreatectomy and exendin-4 treatment.
Physiol Genomics 2006 Jan 12;24(2):133-43
4. Exendin-4, a glucagon-like protein-1 (GLP-1) receptor agonist, reverses hepatic steatosis in ob/ob mice.
Hepatology 2006 Jan;4 3(1):173-81
5. Growth restriction and exendin 4 promote endocrine expression in cultured islet cells derived from patients with persistent hyperinsulinemic hypoglycemia of infancy (PHHI).
Endocr Res 2005;31(2):99-109
6. Release of exendin-4 is controlled by mechanical action in Gila Monsters, Heloderma suspectum.
Comp Biochem Physiol A Mol Integr Physiol 2006 Jan;143(1):85-8

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中華民國95年06月06日更新