Recombinant Mouse Insulin-2 (INS2) Protein (His&Myc)

Name: Recombinant Mouse Insulin-2 (INS2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-11183P
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Ins2.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Mouse Insulin-2 (INS2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P01326
Target Symbol	INS2
Synonyms	Ins2; Ins-2; Insulin-2 [Cleaved into: Insulin-2 B chain; Insulin-2 A chain]
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	FVKQHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQLELGGGPGAGDLQTLALEVAQQKRGIVDQCCTSICSLYQLENYCN
Expression Range	25-110aa
Protein Length	Full Length of Mature Protein
Mol. Weight	16.9 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Subcellular Location	Secreted.
Protein Families	Insulin family
Database References	KEGG: mmu:16334 STRING: 10090.ENSMUSP00000000220 UniGene: Mm.4946

Gene Functions References

High INS2 expression is associated with weight gain and obesity. PMID: 29122848
Data (including data from studies in knockout mice) suggest that Ins2 is involved in impaired nociception/diabetic neuropathy; here, mice heterozygous for mutant Ins2 exhibit (a) significant loss of intra-epidermal nerve fibers, (b) markedly reduced responsiveness to heat in dorsal root ganglion neurons, and (c) mostly unchanged function of cold-sensitive neurons; such mice become diabetic soon after weaning. PMID: 29875100
These results suggest that PABP interacts with HuD in basal glucose conditions making translation inhibitory complex, however upon glucose stimulation this association is affected and PABP is acted upon by PDI resulting in stimulation of insulin translation. PMID: 29590218
cTAGE5 deletion in pancreatic beta cells impairs proinsulin trafficking and insulin biogenesis in mice. PMID: 29133483
report that EndMTs occur in the diabetic endothelium of Ins2Akita/wt mouse, and show that induction of sex determining region Y-box 2 (Sox2) is a mediator of excess BMP signaling that results in activation of EndMTs and increased vascular calcification PMID: 27936229
Transplantation of transduced hematopoietic stem cells (HSCs) expressing proinsulin II prevents diabetes development. PMID: 26784909
Wnt3a increased the expression of NeuroD1 and Ins2 in the hypothalamus. PMID: 26956881
have characterized the distinctive sex-specific phenotypes exhibited by the ApoE(-/-):Ins2(+/Akita) mouse model and present evidence for the action of sex hormones on pancreatic beta-cell function PMID: 26597883
Data indicate that insulin/incomplete Freund's adjuvant (IFA) does not prevent but induces diabetes in RIP-CD80GP transgenic mice. PMID: 24387268
RORalpha is a transcriptional activator of insulin. PMID: 24583012
Mice deficient in coinhibitory PD-L1 or PD-1 molecules (PD-L1(-/-) and PD-1(-/-) mice), were used to study induction of preproinsulin (ppins)-specific CD8 T-cell responses and experimental autoimmune diabetes. PMID: 23977133
Akita mouse has a mutation in Ins2 and is a model of the effects of maternal and paternal hyperglycemia in wildtype offspring PMID: 23209676
Cortical bone was affected in STZ but not Ins2(+/-) mice. PMID: 22886636
proSAAS as a novel down-regulated target of Pax6 PMID: 23056534
Leptin administration improves dyslipidemia and reduces atherosclerosis in type 1 diabetic Ins2(+/Akita):apoE(-/-) mice. PMID: 23099119
Ins2(Akita) mouse is a good model for later-onset DR, modeling both early and some late disease signs. PMID: 23221078
The Akita(ins2) type 1 diabetic model is protected against systolic failure due to increased NCX1 expression via a CXCR4/NF-kappaB pathway. PMID: 22610174
Integrin alpha1KOAkitaKO Balb/c mouse represents a promising model presenting with most features of human diabetic nephropathy. PMID: 22297672
these results indicate that CaMKIIdelta2 downregulates insulin gene expression by Ser142 phosphorylation of CREB and reducing binding of CREB to CBP. PMID: 22554507
HuD controls insulin II translation PMID: 22387028
Data show that TMED6 mRNA is highly and selectively expressed in pancreas,and knockdown of TMED6 gene expression in Min6 beta cells decreased insulin secretion. PMID: 22129529
The results indicated that intraislet ghrelin does not play a major role in the regulation of insulin secretion in vivo. PMID: 22114024
Data suggest that high glucose mediates the recruitment of p300, CBP, PCAF, and GCN5 to the insulin promoter and that all four histone acetyltransferase (HATs) are important for insulin gene expression. PMID: 21774670
Raf-1 specifically and acutely regulates insulin 2 mRNA via negative action on Foxo1 PMID: 21817126
The findings demonstrate that the perturbation of proinsulin homeostasis results in defects in the subsequent conversion process of proinsulin and is a contributor to the occurrence of disproportionate hyperproinsulinemia in diabetes. PMID: 21723250
Exaggerated hypercholesterolemia and atherosclerosis in spontaneously diabetic Ins2(+/Akita):apoE(-/-) mice may be attributable to impaired lipoprotein clearance in the setting of diminished expression of LSR. PMID: 21447785
The transcriptional programs in both endoneurial and neuronal compartments of the peripheral nerve are relatively resistant to the onset of hyperglycemia and hypoinsulinemia in Ins2 mice. PMID: 20520806
Alternative splicing of insulin mRNA in mice could result in an additional level of regulation in insulin biosynthesis. PMID: 20153322
These studies identify strong effects of genetic background to modify the renal phenotype associated with the Ins2(C96Y) mutation. PMID: 20042456
Type 1 diabetic cardiomyopathy in the Akita (Ins2WT/C96Y) mouse model is characterized by lipotoxicity and diastolic dysfunction with preserved systolic function. PMID: 19801494
The interval between Ins2 and Ascl2 is dispensable for imprinting centre function in the mouse model of Beckwith-Wiedemann Syndrome. PMID: 19684026
mutated in iddm in mice PMID: 11981430
findings suggest that the organelle dysfunction resulting from the intracellular accumulation of misfolded proinsulin 2 is primarily responsible for the defect of coexisting wild-type insulin secretion in Akita beta-cells PMID: 12540615
Transcriptional up-regulation of the remaining functional insulin gene in Ins2-/- mice could potentially contribute to beta-cell adaptation. PMID: 12745665
Wild-type preproinsulin-2-expressing pancreatic islets transplanted in preproinsulin-2-deficient mice elicit a mononuclear cell infiltration and insulin antibodies; graft infiltration is further increased by immunization with preproinsulin-2 peptides. PMID: 14688305
A missense mutation of the insulin 2 gene (Cys96Tyr) disrupts 1 of the 2 interchain disulfide bonds resulting in accumulation of misfolded protein in pre-Golgi intermediates. PMID: 15033933
platelet-derived growth factor-induced cell proliferation is inhibited by insulin PMID: 15525682
Pancreatic beta-cells that glucose stimulates the recruitment of ribosome-associated proinsulin mRNA, located in the cytoplasm, to the ER, the site of proinsulin synthesis; this plays an important role in glucose-stimulated proinsulin synthesis. PMID: 15972000
Proinsulin-2 gene expression by radioresistant thymic epithelial cells is involved in the induction of self-tolerance, and additional factors are required to induce islet abnormalities. PMID: 16785498
Munich Ins2 mutant mice are a valuable model to study the mechanisms of beta-cell dysfunction and death during development of diabetes. PMID: 17303807
diabetes causes fusion between Proins-P bone marrow-derived cells and hepatocytes PMID: 17360472
Cre recombinase is controlled by a short fragment of the rat insulin II gene promoter PMID: 17533574
The data underline a direct role for Aire in tissue-restricted antigens expression and suggest that modulation of Aire has a potential to control central tolerance and autoimmunity. PMID: 17599412
misfolded proinsulin causes enlargement of pre-Golgi intermediates which indicates their involvement in protein quality control. PMID: 17647009
Nonobese, insulin-deficient Ins2(Akita) mice develop type 2 diabetes phenotypes including peripheral and hepatic insulin resistance and cardiac remodeling. PMID: 17911348
Insulin II is a direct target of RHOX5. PMID: 18184911
Arterial superoxide generated from diverse sources may potentiate the contractions of carotid arteries in Ins2(Akita) diabetic mice. PMID: 18788099
Mutant huntingtin disrupts intracellular transport and insulin secretion by interacting with tubulin beta 5. PMID: 19628478
Ins2 expression by NOD bone marrow-derived cells did not delay diabetes development in NOD-Ins2-/- mice. PMID: 19874548

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.