Insulin receptor and insulin-like growth factor 1 (IGF-1) receptor. Insulin binds to these receptors to exert its metabolic and mitogenic effects. [2]
Insulin receptor
Insulin-like growth factor 1 (IGF-1) receptor [3]

The transcribed area of the 5' untranslated region of the mRNA contains one of the two intervening sequences in the human insulin gene, while the other one replaces the C-peptide coding region [1]. Type 2 diabetes is frequently treated using human insulin [2].

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Insulin can be found in human breast cancer tissues. Some breast cancers are responsive to insulin, and administration of an insulin/IGF-1 receptor family kinase inhibitor can inhibit tumor growth of breast cancer cell lines. [2]
Insulin glargine (a long-acting insulin analog) has a 6- to 8-fold higher binding affinity to the IGF-1 receptor than human insulin and may stimulate the proliferation of breast cancer cell lines. [2]
Mammalian target of rapamycin (mTOR) is activated by insulin, and insulin-mediated breast cancer progression may be abrogated by inhibition of mTOR. [2]

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In a nationwide cohort study of 482,033 Taiwanese women with type 2 diabetes followed from 2004 to 2009, human insulin use was associated with a significantly higher risk of breast cancer in patients with prolonged exposure. Compared to never-users, patients in the third tertiles of dose-response parameters showed significantly higher risks: hazard ratios of 1.185 (95% CI: 1.026-1.368) for time since starting insulin ≥67 months, 1.260 (95% CI: 1.096-1.450) for cumulative dose ≥39,000 units, and 1.257 (95% CI: 1.094-1.446) for cumulative duration ≥21.8 months. [2]
Patients treated with human insulin alone without any oral antidiabetic drugs had a significantly higher risk of breast cancer (hazard ratio: 1.413, 95% CI: 1.030-1.940). [2]
Patients treated with oral antidiabetic drugs plus human insulin for <2 years had a significantly lower risk of breast cancer (hazard ratio: 0.728, 95% CI: 0.668-0.793). [2]
Human insulin users who also had been treated with metformin for ≥2 years had a significantly lower risk of breast cancer (hazard ratio: 0.798, 95% CI: 0.741-0.859). [2]
Human insulin users who also had been treated with statin for <2 years or ≥2 years had significantly lower risks of breast cancer (hazard ratios: 0.654 and 0.789, respectively). [2]

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Enzyme-based assays for insulin research typically focus on the insulin receptor (INSR) tyrosine kinase activity. The INSR is a membrane receptor tyrosine kinase that, upon insulin binding, undergoes autophosphorylation and activates downstream signaling cascades. Recombinant human INSR kinase domain can be expressed as a GST-fusion protein and used in in vitro kinase assays. These assays employ biotinylated peptide substrates, such as IRS1-derived peptides, and detect substrate phosphorylation using phospho-tyrosine specific antibodies. The ADP-Glo™ Kinase Assay system provides a luminescent method for measuring ADP produced from kinase reactions, allowing quantification of INSR activity and compound screening.

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In vitro cell-based assays are commonly used to assess the biological activity of insulin and its analogs. One widely adopted method is the in-cell western (ICW) assay, which measures insulin-induced activation of the insulin receptor by quantifying tyrosine phosphorylation of downstream signaling proteins. This cell-based approach has been shown to correlate well with traditional in vivo methods, such as the rabbit blood sugar test, and has been validated for assessing the potency of insulin lispro and insulin glargine formulations. Additionally, engineered cell lines overexpressing the human insulin receptor (INSR) are used in bioassays where ligand-induced receptor activation triggers chemiluminescent detection, providing a quantitative measure of insulin activity.

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Historically, the rabbit blood sugar test (USPRats are commonly used in insulin research. One approach involves intravenous glucose tolerance tests in conscious rats to study glucose-stimulated insulin secretion, with mathematical models applied to characterize the glucose-insulin relationship. Allometric scaling from human data has been successfully applied to describe this system in rats, enabling investigation of anti-diabetic drug effects. In vivo biodistribution studies using radioiodinated insulin (¹²⁵I-rh-Insulin) in diabetic mice demonstrate homogeneous organ distribution and confirm the glucose-lowering activity of recombinant insulin analogs. Additionally, rat pancreatic islets can be isolated and cultured ex vivo to study insulin secretion and proinsulin conversion under various glucose concentrations or in response to inflammatory cytokines such as interleukin-1β, providing insights into β-cell function under diabetic conditions.

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Absorption
When injected subcutaneously, the glucose-lowering effect of human insulin begins approximately 30 minutes post-dose. After a single subcutaneous administration of 0.1 unit/kg of human insulin to healthy subjects, peak insulin concentrations occurred between 1.5 to 2.5 hours post-dose. When administered in an inhaled form (as the product Afrezza), the time to maximum serum insulin concentration ranges from 10-20 minutes after oral inhalation of 4 to 48 units of human insulin. Serum insulin concentrations declined to baseline by approximately 60-240 minutes for these dose levels. Intrapatient variability in insulin exposure measured by AUC and Cmax is approximately 16% (95% CI 12-23%) and 21% (95% CI 16-30%), respectively.

Route of Elimination
Following oral inhalation of human insulin, a mean of 39% of the inhaled dose of carrier particles was distributed to the lungs and a mean of 7% of the dose was swallowed. The swallowed fraction was not absorbed from the GI tract and was eliminated unchanged in the feces.

Metabolism / Metabolites
The metabolism and elimination of orally inhaled human insulin are comparable to regular human insulin.

A fraction of exogenous insulin in plasma may be associated with certain proteins, chiefly alpha- and beta-globulins. These associations are of importance for the transport of insulin, which appears to circulate in the blood and the lymph. It is proposed that two systems are involved in the degradation of insulin by liver.(1) The glutathione-insulin transhydrogenase, which utilizes reduced glutathione to reduce disulfide bridges.(2) Proteolic enzymes that cleaves reduced and separated chains to peptides and amino acids. While Insulin is partly excreted in the urine, the kidney filters and reabsorbs the hormone and renal excretion is not the major route of elimination. Liver and kidney are of primary importance in degrading the hormone and each is capable of destroying a large part of the insulin produced daily. (T167).

Biological Half-Life
Systemic insulin disposition (apparent terminal half-life) following oral inhalation of 4 to 48 units of human insulin was 120-206 minutes.

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Effects During Pregnancy and Lactation
◉ Overview of Medication Use During Lactation
Diabetic mothers using insulin can breastfeed. Exogenous insulin is secreted into breast milk, including newer biosynthetic insulins (e.g., insulin aspart, insulin degludec, insulin detemir, insulin glargine, insulin lispro). Even direct oral administration of recombinant insulin to premature infants is safe. Insulin is a normal component of breast milk and can reduce the risk of type 1 diabetes in breastfed infants. Women with type 2 diabetes who receive insulin therapy have higher insulin levels in their breast milk than women who control their diabetes through diet alone.
Postpartum insulin requirements are reduced in women with type 1 diabetes, but there is no significant difference in postpartum insulin requirements between breastfeeding and non-breastfeeding women. Generally, postpartum insulin requirements are 30% to 50% lower than pre-pregnancy doses. On average, insulin requirements during lactation are 21% lower than pre-pregnancy doses, but individual differences are significant. One study found that insulin requirements were lower than pre-pregnancy levels in the first week postpartum: 54% of pre-pregnancy levels on day 2 and 73% on day 3. By day 7 postpartum, insulin levels returned to pre-pregnancy levels. Another study found that some mothers' insulin requirements did not return to normal for up to 6 weeks. A third study found that at 4 months postpartum, type 1 diabetes patients who exclusively breastfed had an average insulin requirement 13% lower than pre-pregnancy levels (range -52% to +40%). A retrospective case-control study found that postpartum insulin requirements were 34% lower than pre-pregnancy levels. Exclusive breastfeeding mothers tended to have lower insulin requirements compared to mothers who partially or exclusively formula-fed, but the difference was not statistically significant. A small study found that mothers using insulin pumps had an average basal insulin infusion rate 14% lower than pre-pregnancy levels, while the carbohydrate-to-insulin ratio increased by 10%. Breastfeeding appears to improve postpartum glucose tolerance in mothers with gestational diabetes and in women without gestational diabetes. A small, well-controlled study of women with type 1 diabetes using continuous subcutaneous insulin therapy found that breastfeeding women with type 1 diabetes had an average basal insulin requirement of 0.21 IU/kg/day and a total insulin requirement of 0.56 IU/kg/day. In contrast, the same group of women who did not breastfeed had a basal insulin requirement of 0.33 IU/kg/day and a total insulin requirement of 0.75 IU/kg/day. The 36% reduction in basal insulin requirement was attributed to glucose being used for milk production. Lactation onset was later in women with type 1 diabetes than in non-diabetic women, with a more pronounced delay in onset in mothers with poor glycemic control. A higher percentage of mothers with type 1 diabetes also stopped breastfeeding in the first week postpartum. Women who developed any type of diabetes during pregnancy were more likely to experience insufficient milk production than non-diabetic women. Once lactation was established, the duration of lactation in diabetic mothers was as long as in non-diabetic mothers. However, as with non-diabetic women, smoking had a significant negative impact on lactation in mothers with type 1 diabetes. Other identified factors contributing to shorter breastfeeding duration in women with type 1 diabetes include higher cesarean section rates and earlier delivery. In women with gestational diabetes, those receiving insulin therapy experienced delayed initiation of lactation stage II compared to those not receiving insulin therapy.
◉ Impact on Breastfed Infants
As of the revision date, no relevant published information was found. Insulin in breast milk is considered crucial for infant gut development and may help reduce the risk of type 1 diabetes in breastfed infants.
◉ Impact on Lactation and Breast Milk
Adequate insulin levels are essential for lactation. Good glycemic control can increase prolactin concentrations in maternal serum and breast milk and reduce potential delays in lactation in mothers with type 1 diabetes.
In a Danish hospital, researchers followed 102 of 107 consecutively delivered mothers with type 1 diabetes. The mothers received information about breastfeeding prenatally and were counseled by nurses postpartum regarding the benefits of breastfeeding. All infants were admitted to the neonatal intensive care unit approximately two hours after birth and received 24-hour monitoring. During this period, mothers breastfed or used breast pumps to express milk for their infants whenever possible. Researchers contacted mothers at 5 days and 4 months postpartum to determine their breastfeeding status. The initiation rates of exclusive breastfeeding, part-breastfeeding, and formula-only feeding, as well as the feeding rate at 4 months postpartum, were not significantly different from the Danish population. Researchers interviewed 883 women with gestational diabetes between 6 and 9 weeks postpartum. Women receiving insulin treatment were more likely to report delayed lactation stage II (>72 hours) than those not receiving insulin treatment, and this outcome was independent of other maternal risk factors. Mothers receiving insulin treatment had a 3.1 times higher risk of delayed lactation stage II than gestational diabetes mothers not receiving insulin treatment.\n

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\nHuman insulin is a polypeptide hormone composed of two chains (A and B) joined by disulfide linkages. It is produced from a precursor, preproinsulin, which contains a signal peptide at the NH₂-terminus. Preproinsulin is processed to proinsulin (NH₂-B-C-A-COOH), and then to mature insulin by removal of the C-peptide. [1]
The human insulin gene is located on a 12.5-kilobase EcoRI fragment and contains two intervening sequences (introns): one (179 base pairs) in the DNA segment encoding the 5′-untranslated region of insulin mRNA, and another (786 base pairs) in the DNA region encoding the C-peptide of proinsulin. The gene has a high GC content (64.8%). [1]
Unlike rats, which have two non-allelic insulin genes (insulin I and II), the human haploid genome contains a single insulin gene. Allelic variation exists, as demonstrated by a PstI site polymorphism in the 3′-untranslated region. [1]
The insulin gene contains a \"Hogness sequence\" (TATAAAG) 24 base pairs before the start of transcription, which is thought to facilitate initiation of transcription. A large imperfect palindrome (positions 155-213) may be a binding site for an insulin-specific regulatory protein. [1]\n

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\nToxicity Summary
\nInsulin overdose can cause toxicity by causing hypoglycemia and many additional effects, including arrhythmias, coma, seizures, hypotension, amongst other symptoms. Long-term insulin use may lead to dermal toxicity by causing lipodystrophy. The patient can mitigate this adverse effect by rotating subcutaneous injection sites. Insulin can also cause hypokalemia and related complications, as mentioned earlier in this article.\nStatPearls\nInsulin has a direct inhibitory effect on the lipase concerned with the mobilization of fattty acids. Insulin binds to a receptor on the surface of the target cell and probably also enters the cell in this state (L1007, T167).

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[1]. Sequence of the human insulin gene. Nature. 1980 Mar 6;284(5751):26-32.
[2]. Prolonged use of human insulin increases breast cancer risk in Taiwanese women with type 2 diabetes. BMC Cancer. 2015 Nov 4;15:846.

Human insulin is produced by the pancreas and is involved in regulating the metabolism of carbohydrates (especially glucose) and fats. It is generally considered a protein composed of two polypeptide chains, one containing 21 amino acid residues and the other containing 30 amino acid residues; these two chains are linked by two disulfide bonds. Recombinant insulin is identical to human insulin, but it is synthesized by inserting the human insulin gene into E. coli, which then produces insulin for human use. It is used to treat type 1 and type 2 diabetes and has a blood sugar-lowering effect.
See also: Human Insulin (note moved to).

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Human insulin is a polypeptide hormone composed of two chains (A and B) joined by disulfide linkages. It is produced from a precursor, preproinsulin, which contains a signal peptide at the NH₂-terminus. Preproinsulin is processed to proinsulin (NH₂-B-C-A-COOH), and then to mature insulin by removal of the C-peptide. [1]
The human insulin gene is located on a 12.5-kilobase EcoRI fragment and contains two intervening sequences (introns): one (179 base pairs) in the DNA segment encoding the 5′-untranslated region of insulin mRNA, and another (786 base pairs) in the DNA region encoding the C-peptide of proinsulin. The gene has a high GC content (64.8%). [1]
Unlike rats, which have two non-allelic insulin genes (insulin I and II), the human haploid genome contains a single insulin gene. Allelic variation exists, as demonstrated by a PstI site polymorphism in the 3′-untranslated region. [1]
The insulin gene contains a "Hogness sequence" (TATAAAG) 24 base pairs before the start of transcription, which is thought to facilitate initiation of transcription. A large imperfect palindrome (positions 155-213) may be a binding site for an insulin-specific regulatory protein. [1]

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The human insulin gene contains two intervening sequences: one within the region transcribed into the 5'-untranslated segment of the mRNA, and the other interrupting the C-peptide encoding region. The human insulin gene is 1,789 base pairs in length with a high GC content (64.8%). An allelic variation (PstI site polymorphism) exists in the 3'-untranslated region. [2]
In a nationwide cohort study of Taiwanese women with type 2 diabetes (n=482,033), ever-users of Insulin (human) (n=59,798) had an overall adjusted hazard ratio for breast cancer of 1.033 (95% CI 0.936-1.139) compared to never-users. However, patients in the highest tertile of exposure parameters showed significantly higher risk: for cumulative duration ≥21.8 months, HR=1.257 (1.094-1.446); for cumulative dose ≥39,000 units, HR=1.260 (1.096-1.450); for time since starting insulin ≥67 months, HR=1.185 (1.026-1.368). [3]
Insulin (human) may increase breast cancer risk through activation of insulin receptor or IGF-1 receptor, and through activation of the mammalian target of rapamycin (mTOR) pathway. Exogenous insulin administration is associated with increased body weight, insulin resistance, hyperinsulinemia, hyperglycemia, oxidative stress, and proinflammation. [3]
Concomitant use of metformin (≥2 years) or statin (any duration) significantly reduced breast cancer risk in Insulin (human) users. ACEI/ARB use for <2 years also reduced risk, but the effect attenuated with longer use. [3]

C257H383N65O77S6

5807.58

5805.644

11061-68-0

118984375

H-Phe-Val-Asn-Gln-His-Leu-Cys(1)-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val-Cys(2)-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Thr-OH.H-Gly-Ile-Val-Glu-Gln-Cys(3)-Cys(1)-Thr-Ser-Ile-Cys(3)-Ser-Leu-Tyr-Gln-Leu-Glu-Asn-Tyr-Cys(2)-Asn-OH
L-phenylalanyl-L-valyl-L-asparagyl-L-glutaminyl-L-histidyl-L-leucyl-L-cysteinyl-glycyl-L-seryl-L-histidyl-L-leucyl-L-valyl-L-alpha-glutamyl-L-alanyl-L-leucyl-L-tyrosyl-L-leucyl-L-valyl-L-cysteinyl-glycyl-L-alpha-glutamyl-L-arginyl-glycyl-L-phenylalanyl-L-phenylalanyl-L-tyrosyl-L-threonyl-L-prolyl-L-lysyl-L-threonine (7->7'),(19->20')-bis(disulfide) compound with glycyl-L-isoleucyl-L-valyl-L-alpha-glutamyl-L-glutaminyl-L-cysteinyl-L-cysteinyl-L-threonyl-L-seryl-L-isoleucyl-L-cysteinyl-L-seryl-L-leucyl-L-tyrosyl-L-glutaminyl-L-leucyl-L-alpha-glutamyl-L-asparagyl-L-tyrosyl-L-cysteinyl-L-asparagine (6'->11')-disulfide

H-FVNQHLC(1)GSHLVEALYLVC(2)GERGFFYTPKT-OH.H-GIVEQC(3)C(1)TSIC(3)SLYQLENYC(2)N-OH

White to off-white solid powder

Biosynthesis

-13.1

78

89

179

405

14600

52

[H]/N=C(/NCCC[C@@H](C(NCC(N[C@H](C(N[C@H](C(N[C@H](C(N[C@H](C(N1[C@H](C(N[C@H](C(N[C@H](C(=O)O)[C@@H](O)C)=O)CCCCN)=O)CCC1)=O)[C@@H](O)C)=O)CC1=CC=C(O)C=C1)=O)CC1=CC=CC=C1)=O)CC1=CC=CC=C1)=O)=O)NC([C@@H](NC(CNC([C@H]1NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC2=CC=C(O)C=C2)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC2N=CNC=2)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@@H](NC([C@@H](NC([C@@H](NC([C@@H](NC([C@H](C(=O)N)NC([C@H](C(C)C)NC([C@H](CC2=CC=CC=C2)N)=O)=O)=O)CCC(=O)N)=O)CC2N=CNC=2)=O)CC(C)C)=O)CSSC[C@@H]2C(N[C@H](C(N[C@H](C(N[C@H](C(N[C@@H](CSSC[C@@H](C(N2)=O)NC([C@@H](NC([C@@H](NC([C@H](C(C)C)NC([C@H]([C@@H](CC)C)NC(CN)=O)=O)=O)CCC(=O)O)=O)CCC(=O)N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC2=CC=C(O)C=C2)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CC2=CC=C(O)C=C2)C(=O)N[C@H](C(N[C@H](C(=O)O)CC(=O)N)=O)CSSC1)=O)[C@@H](CC)C)=O)CO)=O)[C@@H](O)C)=O)=O)=O)CCC(=O)O)=O)\N

PBGKTOXHQIOBKM-FHFVDXKLSA-N

InChI=1S/C257H383N65O77S6/c1-29-131(23)205(313-193(339)104-259)252(393)317-204(130(21)22)248(389)288-159(75-82-200(349)350)217(358)282-156(71-78-189(263)335)221(362)308-183-116-403-404-117-184-243(384)305-178(111-324)240(381)294-162(88-123(7)8)225(366)295-168(95-140-53-61-146(329)62-54-140)228(369)283-154(69-76-187(261)333)218(359)290-161(87-122(5)6)223(364)285-158(74-81-199(347)348)220(361)302-174(101-190(264)336)235(376)298-170(97-142-57-65-148(331)66-58-142)231(372)309-182(242(383)304-176(255(396)397)103-192(266)338)115-402-401-114-181(214(355)273-107-194(340)278-153(72-79-197(343)344)216(357)281-151(51-42-84-271-257(267)268)212(353)272-108-195(341)279-166(93-138-46-36-32-37-47-138)227(368)297-167(94-139-48-38-33-39-49-139)230(371)299-171(98-143-59-67-149(332)68-60-143)238(379)320-208(135(27)327)254(395)322-85-43-52-186(322)246(387)286-152(50-40-41-83-258)222(363)321-209(136(28)328)256(398)399)311-250(391)203(129(19)20)316-236(377)164(90-125(11)12)292-229(370)169(96-141-55-63-147(330)64-56-141)296-224(365)160(86-121(3)4)289-210(351)133(25)277-215(356)157(73-80-198(345)346)287-247(388)202(128(17)18)315-237(378)165(91-126(13)14)293-233(374)173(100-145-106-270-120-276-145)301-239(380)177(110-323)280-196(342)109-274-213(354)180(113-400-405-118-185(310-244(183)385)245(386)319-207(134(26)326)253(394)306-179(112-325)241(382)318-206(132(24)30-2)251(392)312-184)307-226(367)163(89-124(9)10)291-232(373)172(99-144-105-269-119-275-144)300-219(360)155(70-77-188(262)334)284-234(375)175(102-191(265)337)303-249(390)201(127(15)16)314-211(352)150(260)92-137-44-34-31-35-45-137/h31-39,44-49,53-68,105-106,119-136,150-186,201-209,323-332H,29-30,40-43,50-52,69-104,107-118,258-260H2,1-28H3,(H2,261,333)(H2,262,334)(H2,263,335)(H2,264,336)(H2,265,337)(H2,266,338)(H,269,275)(H,270,276)(H,272,353)(H,273,355)(H,274,354)(H,277,356)(H,278,340)(H,279,341)(H,280,342)(H,281,357)(H,282,358)(H,283,369)(H,284,375)(H,285,364)(H,286,387)(H,287,388)(H,288,389)(H,289,351)(H,290,359)(H,291,373)(H,292,370)(H,293,374)(H,294,381)(H,295,366)(H,296,365)(H,297,368)(H,298,376)(H,299,371)(H,300,360)(H,301,380)(H,302,361)(H,303,390)(H,304,383)(H,305,384)(H,306,394)(H,307,367)(H,308,362)(H,309,372)(H,310,385)(H,311,391)(H,312,392)(H,313,339)(H,314,352)(H,315,378)(H,316,377)(H,317,393)(H,318,382)(H,319,386)(H,320,379)(H,321,363)(H,343,344)(H,345,346)(H,347,348)(H,349,350)(H,396,397)(H,398,399)(H4,267,268,271)/t131-,132-,133-,134+,135+,136+,150-,151-,152-,153-,154-,155-,156-,157-,158-,159-,160-,161-,162-,163-,164-,165-,166-,167-,168-,169-,170-,171-,172-,173-,174-,175-,176-,177-,178-,179-,180-,181-,182-,183-,184-,185-,186-,201-,202-,203-,204-,205-,206-,207-,208-,209-/m0/s1

(4S)-4-[[2-[[(1R,6R,12S,15S,18S,21S,24S,27S,30S,33S,36S,39S,42R,47R,50S,53S,56S,59S,62S,65S,68S,71S,74R,77S,80S,83S,88R)-88-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[(2-aminoacetyl)amino]-3-methylpentanoyl]amino]-3-methylbutanoyl]amino]-4-carboxybutanoyl]amino]-5-oxopentanoyl]amino]-6-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-methylbutanoyl]amino]-4-oxobutanoyl]amino]-5-oxopentanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-4-methylpentanoyl]amino]-47-[[(1S)-3-amino-1-carboxy-3-oxopropyl]carbamoyl]-53-(2-amino-2-oxoethyl)-62-(3-amino-3-oxopropyl)-77-[(2S)-butan-2-yl]-24,56-bis(2-carboxyethyl)-83-[(1R)-1-hydroxyethyl]-12,71,80-tris(hydroxymethyl)-33,50,65-tris[(4-hydroxyphenyl)methyl]-15-(1H-imidazol-4-ylmethyl)-27-methyl-18,30,36,59,68-pentakis(2-methylpropyl)-7,10,13,16,19,22,25,28,31,34,37,40,49,52,55,58,61,64,67,70,73,76,79,82,85,87-hexacosaoxo-21,39-di(propan-2-yl)-3,4,44,45,90,91-hexathia-8,11,14,17,20,23,26,29,32,35,38,41,48,51,54,57,60,63,66,69,72,75,78,81,84,86-hexacosazabicyclo[72.11.7]dononacontane-42-carbonyl]amino]acetyl]amino]-5-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3R)-1-[(2S)-2-[[(2S)-6-amino-1-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-1-oxohexan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-hydroxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-2-oxoethyl]amino]-5-carbamimidamido-1-oxopentan-2-yl]amino]-5-oxopentanoic acid

Insulin human; Insulin (human); Exubera; Insulina humana

2934.99.9001

Powder      -20°C    3 years

                     4°C     2 years

In solvent   -80°C    6 months

                  -20°C    1 month

Note: Please store this product in a sealed and protected environment (e.g. under nitrogen), avoid exposure to moisture and light.

Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)

H2O : ~10 mg/mL (~1.72 mM)

Note: Listed below are some common formulations that may be used to formulate products with low water solubility (e.g. < 1 mg/mL), you may test these formulations using a minute amount of products to avoid loss of samples.

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Injection Formulation 1: DMSO : Tween 80： Saline = 10 : 5 : 85 (i.e. 100 μL DMSO stock solution → 50 μL Tween 80 → 850 μL Saline)
*Preparation of saline: Dissolve 0.9 g of sodium chloride in 100 mL ddH ₂ O to obtain a clear solution.
Injection Formulation 2: DMSO : PEG300 ：Tween 80 : Saline = 10 : 40 : 5 : 45 (i.e. 100 μL DMSO → 400 μLPEG300 → 50 μL Tween 80 → 450 μL Saline)
Injection Formulation 3: DMSO : Corn oil = 10 : 90 (i.e. 100 μL DMSO → 900 μL Corn oil)
Example: Take the Injection Formulation 3 (DMSO : Corn oil = 10 : 90) as an example, if 1 mL of 2.5 mg/mL working solution is to be prepared, you can take 100 μL 25 mg/mL DMSO stock solution and add to 900 μL corn oil, mix well to obtain a clear or suspension solution (2.5 mg/mL, ready for use in animals).

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Injection Formulation 4: DMSO : 20% SBE-β-CD in saline = 10 : 90 [i.e. 100 μL DMSO → 900 μL (20% SBE-β-CD in saline)]
*Preparation of 20% SBE-β-CD in Saline (4°C，1 week): Dissolve 2 g SBE-β-CD in 10 mL saline to obtain a clear solution.
Injection Formulation 5: 2-Hydroxypropyl-β-cyclodextrin : Saline = 50 : 50 (i.e. 500 μL 2-Hydroxypropyl-β-cyclodextrin → 500 μL Saline)
Injection Formulation 6: DMSO : PEG300 : castor oil : Saline = 5 : 10 : 20 : 65 (i.e. 50 μL DMSO → 100 μLPEG300 → 200 μL castor oil → 650 μL Saline)
Injection Formulation 7: Ethanol : Cremophor : Saline = 10： 10 : 80 (i.e. 100 μL Ethanol → 100 μL Cremophor → 800 μL Saline)
Injection Formulation 8: Dissolve in Cremophor/Ethanol (50 : 50), then diluted by Saline
Injection Formulation 9: EtOH : Corn oil = 10 : 90 (i.e. 100 μL EtOH → 900 μL Corn oil)
Injection Formulation 10: EtOH : PEG300：Tween 80 : Saline = 10 : 40 : 5 : 45 (i.e. 100 μL EtOH → 400 μLPEG300 → 50 μL Tween 80 → 450 μL Saline)

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Oral Formulation 1: Suspend in 0.5% CMC Na (carboxymethylcellulose sodium)
Oral Formulation 2: Suspend in 0.5% Carboxymethyl cellulose
Example: Take the Oral Formulation 1 (Suspend in 0.5% CMC Na) as an example, if 100 mL of 2.5 mg/mL working solution is to be prepared, you can first prepare 0.5% CMC Na solution by measuring 0.5 g CMC Na and dissolve it in 100 mL ddH2O to obtain a clear solution; then add 250 mg of the product to 100 mL 0.5% CMC Na solution, to make the suspension solution (2.5 mg/mL, ready for use in animals).

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Oral Formulation 3: Dissolved in PEG400
Oral Formulation 4: Suspend in 0.2% Carboxymethyl cellulose
Oral Formulation 5: Dissolve in 0.25% Tween 80 and 0.5% Carboxymethyl cellulose
Oral Formulation 6: Mixing with food powders

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Note: Please be aware that the above formulations are for reference only. InvivoChem strongly recommends customers to read literature methods/protocols carefully before determining which formulation you should use for in vivo studies, as different compounds have different solubility properties and have to be formulated differently.

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 (Please use freshly prepared in vivo formulations for optimal results.)