Insulin Protein, Human, Recombinant

Catalog No. TMPY-00395 Copy Product Info

INS (Insulin) is a Protein Coding gene. This gene encodes insulin, a peptide hormone that plays a vital role in the regulation of carbohydrate and lipid metabolism. 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. The binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Diseases associated with INS include Hyperproinsulinemia and Maturity-Onset Diabetes Of The Young, Type 10. A multitude of mutant alleles with phenotypic effects has been identified, including insulin-dependent diabetes mellitus, permanent neonatal diabetes mellitus, maturity-onset diabetes of the young type 10, and hyperproinsulinemia.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

Insulin Protein, Human, Recombinant

Catalog No. TMPY-00395

Copy Product Info

Pack Size	Price	USA Stock	Global Stock
5 μg	$48	-	In Stock
10 μg	$75	-	In Stock
20 μg	$118	-	In Stock
50 μg	$229	7-10 days	7-10 days
100 μg	$386	-	In Stock
200 μg	$660	7-10 days	7-10 days
500 μg	$1,330	7-10 days	7-10 days

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For In stock only · Estimated delivery:USA Stock (1-2 days) Global Stock (5-7 days)

For research use only—not for human use. No sales to individuals. Use as intended only.

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COA User Guide of Recombinant Proteins

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Biological Activity	Measured in a serum-free cell proliferation assay using MCF‑7 human breast cancer cells. The ED50 for this effect is typically 0.2-1 µg/mL.
Description	INS (Insulin) is a Protein Coding gene. This gene encodes insulin, a peptide hormone that plays a vital role in the regulation of carbohydrate and lipid metabolism. 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. The binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Diseases associated with INS include Hyperproinsulinemia and Maturity-Onset Diabetes Of The Young, Type 10. A multitude of mutant alleles with phenotypic effects has been identified, including insulin-dependent diabetes mellitus, permanent neonatal diabetes mellitus, maturity-onset diabetes of the young type 10, and hyperproinsulinemia.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
Species	Human
Expression System	P. pastoris (Yeast)
Tag	Tag Free
Accession Number	P01308
Synonyms	MODY10,IRDN,insulin,INS,ILPR,IDDM2,IDDM1,IDDM
Construction	A DNA sequence encoding human insulin B chain (P01308)(Phe25-Lys53) and human insulin A chain (P01308)(Gly90-Asn110) was expressed with a linker AAK. Predicted N terminal: Phe
Protein Purity	> 95% as determined by SDS-PAGE
Molecular Weight	7.1 kDa (predicted); 6 kDa (reducing conditions)
Endotoxin	Please contact us for more information.
Formulation	Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 7.4. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
Reconstitution	Reconstituted with sterile deionized water to 0.13 mg/mL. Reconstitution conditions may vary depending on the lot.
Stability & Storage	It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, lyophilized powders are shipped with blue ice, while solutions are shipped with dry ice.
Research Background	INS (Insulin) is a Protein Coding gene. This gene encodes insulin, a peptide hormone that plays a vital role in the regulation of carbohydrate and lipid metabolism. 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. The binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Diseases associated with INS include Hyperproinsulinemia and Maturity-Onset Diabetes Of The Young, Type 10. A multitude of mutant alleles with phenotypic effects has been identified, including insulin-dependent diabetes mellitus, permanent neonatal diabetes mellitus, maturity-onset diabetes of the young type 10, and hyperproinsulinemia.