Catalog No.	BP006254
Product Name	Recombinant Human Insulin | CAS 11061-68-0
Supplier Name	Syd Labs, Inc.
Brand Name	Syd Labs
Synonyms	rDNA human insulin, biosynthetic human insulin (BHI)
CAS No.	11061-68-0
Molecular Weight	5807.57
Molecular Formula	C257H383N65O77S6
Appearance	White or almost white crystalline powder
Biological Activity	Approx. 20 units/mg
Purity	95%-105%
Endotoxin Level	≤10 EU/mg
Typical Zinc content	≤1.0%
Loss on Drying	≤10.0%
Isoelectric Point	Approx. 5.30
Solubility	The recombinant human insulin is soluble in 0.01M HCl (20 mg/mL), yielding a clear colorless solution
Applications	Recombinant human insulin is frequently employed as a culture supplement in cell cultivation systems. Historically recognized as a critical factor for regulating growth and differentiation in most cell types in vitro, its working concentration typically ranges from 1–10 µg/mL (dynamically optimized for specific cell types). In serum-free culture protocols, insulin is often immobilized onto polystyrene culture dish surfaces.
Shipping	Recombinant Human Insulin is shipped with ice packs. Upon receipt, store it immediately at the temperature recommended below
Stability & Storage	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 24 months from date of receipt if stored at -20°C to -70°C as supplied.
Note	The cheapest recombinant human insulin (cell culture grade) in the market.
Order Offline	Phone: 1-617-401-8149 Fax: 1-617-606-5022 Email: message@sydlabs.com Or leave a message with a formal purchase order (PO) Or credit card.

Description

BP006254: CAS No.: 11061-68-0 | Recombinant Human Insulin (Cell Culture Grade)

Insulin is the sole hormone in the human body that lowers blood glucose levels, while simultaneously promoting the synthesis of glycogen, fats, and proteins. Recombinant human insulin is produced through genetic engineering by constructing an E. coli expression system, followed by bioreactor fermentation and purification processes. Its amino acid sequence is identical to endogenously expressed human insulin, making it a high-purity, animal component-free bioactive protein.

Currently, industrial-grade recombinant human insulin is predominantly used as a cell culture medium additive for animal cell cultivation. Cell culture media supplemented with recombinant human insulin can mimic in vivo growth conditions more authentically, thereby enhancing cellular proliferation and stabilizing expression of target proteins.

References for Recombinant Human Insulin (CAS No.11061-68-0)

1、Making, Cloning, and the Expression of Human Insulin Genes in Bacteria: The Path to Humulin
Arthur D Riggs,et al.Endocr Rev. 2021.PMCID: 33340315
“In the mid- to late 1970s, recombinant deoxyribonucleic acid methods for cloning and expressing genes in E. coli were under intense development. The important question had become: Can humans design and chemically synthesize novel genes that function in bacteria? This question was answered in 1978 and in 1979 with the successful expression in E. coli of 2 mammalian hormones, first somatostatin and then human insulin. The successful production of human insulin in bacteria provided, for the first time, a practical, scalable source of human insulin and resulted in the approval, in 1982, of human insulin for the treatment of diabetics. In this short review, I give my personal view of how the making, cloning, and expressing of human insulin genes was accomplished by a team of scientists led by Keiichi Itakura, Herbert W. Boyer, and myself.
Keywords: biotechnology; chemical DNA synthesis; genentech; recombinant DNA.”

2、Insulin Tregopil: An Ultra-Fast Oral Recombinant Human Insulin Analog: Preclinical and Clinical Development in Diabetes Mellitus
Shashank Joshi,et al.Drugs. 2023.PMCID: 37578592
“Insulin therapy is indispensable for achieving glycemic control in all patients with type 1 diabetes mellitus and many patients with type 2 diabetes mellitus. Insulin injections are associated with negative connotations in patients owing to administration discomfort and adverse effects such as hypoglycemia and weight gain. Insulin administered orally can overcome these limitations by providing a convenient and effective mode of delivery with a potentially lower risk of hypoglycemia. Oral insulin mimics the physiologic process of insulin secretion, absorption into the portal circulation, and subsequent peripheral delivery, unlike the subcutaneous route that results in peripheral hyperinsulinemia. Insulin tregopil (IN-105), a new generation human recombinant insulin, methoxy (polyethylene glycol) hexanoyl human recombinant insulin, is developed by Biocon as an ultra-fast onset short-acting oral insulin analog. This recombinant oral insulin is a single short-chain amphiphilic oligomer modified with the covalent attachment of methoxy-triethylene-glycol-propionyl moiety at Lys-β29-amino group of the B-chain via an amide linkage. Sodium caprate, an excipient in the insulin tregopil formulation, is a permeation enhancer that increases its absorption through the gastrointestinal tract. Also, meal composition has been shown to non-significantly affect its absorption. Several global randomized, controlled clinical trials have been conducted in type 1 and type 2 diabetes patients towards the clinical development of insulin tregopil. The formulation shows post-prandial glucose control that is more effective than placebo throughout the meal period; however, compared with an active comparator insulin aspart, the post-prandial control is more effective mainly in the early post-meal period. It shows a good safety profile with a lower incidence of clinically significant hypoglycemia. This review covers the overall clinical development of insulin tregopil establishing it as an ultra-fast onset, short-acting oral insulin analog for optimizing post-prandial glucose.”

3、Downstream processing of recombinant human insulin and its analogues production from E. coli inclusion bodies
Yin Yin Siew,et al.Bioresour Bioprocess. 2021.PMCID: 34336550
“The Global Diabetes Compact was launched by the World Health Organization in April 2021 with one of its important goals to increase the accessibility and affordability of life-saving medicine-insulin. The rising prevalence of diabetes worldwide is bound to escalate the demand for recombinant insulin therapeutics, and currently, the majority of recombinant insulin therapeutics are produced from E. coli inclusion bodies. Here, a comprehensive review of downstream processing of recombinant human insulin/analogue production from E. coli inclusion bodies is presented. All the critical aspects of downstream processing, starting from proinsulin recovery from inclusion bodies, inclusion body washing, inclusion body solubilization and oxidative sulfitolysis, cyanogen bromide cleavage, buffer exchange, purification by chromatography, pH precipitation and zinc crystallization methods, proinsulin refolding, enzymatic cleavage, and formulation, are explained in this review. Pertinent examples are summarized and the practical aspects of integrating every procedure into a multimodal purification scheme are critically discussed. In the face of increasing global demand for insulin product, there is a pressing need to develop a more efficient and economical production process. The information presented would be insightful to all the manufacturers and stakeholders for the production of human insulins, insulin analogues or biosimilars, as they strive to make further progresses in therapeutic recombinant insulin development and production.
Keywords: Downstream processing; E. coli inclusion bodies; Insulin analogues; Purification; Recombinant human insulin.”

4、Recombinant production of hormonally active human insulin from pre-proinsulin by Tetrahymena thermophila
Ayça Fulya Üstüntanır Dede,et al.Enzyme Microb Technol. 2023.PMCID: 37562115
“Alternative cell factories, such as the unicellular ciliate eukaryotic Tetrahymena thermophila, may be required for the production of protein therapeutics that are challenging to produce in conventional expression systems. T. thermophila (Tt) can secrete proteins with the post-translational modifications necessary for their function in humans. In this study, we tested if T. thermophila could process the human pre-proinsulin to produce hormonally active human insulin (hINS) with correct modifications. Flask and bioreactor culture of T. thermophila were used to produce the recombinant Tt-hINS either with or without an affinity tag from a codon-adapted pre-proinsulin sequence. Our results indicate that T. thermophila can produce a 6 kDa Tt-hINS monomer with the appropriate disulfide bonds after removal of the human insulin signal sequence or endogenous phospholipase A signal sequence, and the C-peptide of the human insulin. Additionally, Tt-hINS can form 12 kDa dimeric, 24 kDa tetrameric, and 36 kDa hexameric complexes. Tt-hINS-sfGFP fusion protein was localized to the vesicles within the cytoplasm and was secreted extracellularly. Assessing the affinity-purified Tt-hINS activity using the in vivo T. thermophila extracellular glucose drop assay, we observed that Tt-hINS induced a significant reduction (approximately 21 %) in extracellular glucose levels, indicative of its functional insulin activity. Our results demonstrate that T. thermophila is a promising candidate for the pharmaceutical and biotechnology industries as a host organism for the production of human protein drugs.
Keywords: Bioreactor; Human insulin; Insulin activity; Pre-proinsulin; Recombinant; Therapeutic.”

5、Lipodystrophies in non-insulin-dependent children: Treatment options and results from recombinant human leptin therapy
Valeria Calcaterra,et al.Pharmacol Res. 2023.PMCID: 36566927
“Lipodystrophy is a general definition containing different pathologies which, except for those observed in insulin-treated subjects falling outside the scope of this paper, are characterized by total or partial lack of body fat, that, according to the amount of missing adipose tissue, are divided in generalized or partial lipodystrophy. These diseases are characterized by leptin deficiency, which often leads to metabolic derangement, causing insulin resistance, dyslipidemia, and increasing cardiovascular risk. In this narrative review, we presentend the clinical presentation of different types of lipodystrophies and metabolic unbalances related to disease in children and adolescents, focusing on the main treatment options and the novel results from recombinant human leptin (metreleptin) therapy. Milestones in the management of lipodystrophy include lifestyle modification as diet and physical activity, paired with hypoglycemic drugs, insulin, hypolipidemic drugs, and other drugs with the aim of treating lipodystrophy complications. Metreleptin has been recently approved for pediatric patients with general lipodystrophy (GL)> 2 years of age and for children with partial lipodystrophy (PL)> 12 years of age not controlled with conventional therapies. New therapeutic strategies are currently being investigated, especially for patients with PL forms, specifically, liver-targeted therapies. Further studies are needed to achieve the most specific and precise treatment possible.
Keywords: Children; Leptin; Lipodystrophy; Metabolic unbalance; Metreleptin; Recombinant.”

6、Periosteum and development of the tissue-engineered periosteum for guided bone regeneration
Wentao Zhang,et al.J Orthop Translat. 2022.PMCID: 35228996
“Background: Periosteum plays a significant role in bone formation and regeneration by storing progenitor cells, and also acts as a source of local growth factors and a scaffold for recruiting cells and other growth factors. Recently, tissue-engineered periosteum has been studied extensively and shown to be important for osteogenesis and chondrogenesis. Using biomimetic methods for artificial periosteum synthesis, membranous tissues with similar function and structure to native periosteum are produced that significantly improve the efficacy of bone grafting and scaffold engineering, and can serve as direct replacements for native periosteum. Many problems involving bone defects can be solved by preparation of idealized periosteum from materials with different properties using various techniques.
Methods: This review summarizes the significance of periosteum for osteogenesis and chondrogenesis from the aspects of periosteum tissue structure, osteogenesis performance, clinical application, and development of periosteum tissue engineering. The advantages and disadvantages of different tissue engineering methods are also summarized.
Results: The fast-developing field of periosteum tissue engineering is aimed toward synthesis of bionic periosteum that can ensure or accelerate the repair of bone defects. Artificial periosteum materials can be similar to natural periosteum in both structure and function, and have good therapeutic potential. Induction of periosteum tissue regeneration and bone regeneration by biomimetic periosteum is the ideal process for bone repair.
Conclusions: Periosteum is essential for bone formation and regeneration, and it is indispensable in bone repair. Achieving personalized structure and composition in the construction of tissue engineering periosteum is in accordance with the design concept of both universality and emphasis on individual differences and ensures the combination of commonness and individuality, which are expected to meet the clinical needs of bone repair more effectively.
The translational potential of this article: To better understand the role of periosteum in bone repair, clarify the present research situation of periosteum and tissue engineering periosteum, and determine the development and optimization direction of tissue engineering periosteum in the future. It is hoped that periosteum tissue engineering will play a greater role in meeting the clinical needs of bone repair in the future, and makes it possible to achieve optimization of bone tissue therapy.
Keywords: AF Antheraea pernyi fibroin, AMSCs adipose mesenchymal stem cells; BMP bone morphogenetic proteins, BMP-2 bone morphogenetic protein-2; BMSCs bone marrow stromal cell, CaPs calcium phosphate nanoparticles, COL I collagen I; Biomaterials; Bone defect healing; Bone repair; DOP dopamine, DSCs dental pulp stem cells; ECM extracellular matrix, GBR guided bone regeneration; GelMA methacrylate gelatin, HA hydroxyapatite; HAM human amniotic membrane, HCP human cultured periosteum; ICA Icariin, IGF-1 insulin-like growth factor-1; MBGNs mesoporous bioglass nanoparticles, MOX moxifloxacin hydrochloride; MSCs mesenchymal stem cells, n-HA nano-hydroxyapatite; OCN osteocalcin, OSX osterix; Osteogenesis; PCL polycaprolactone, PDCs periosteum derived cells; PDGF-BB platelet-derived growth factor-BB, PDO periosteal distraction osteogenesis; PEEK polyetheretherketone, PLA polylactic acid; PLLA l-lactic acid, PRP platelet-rich plasma; PU degradable polyurethane fibers without nano-hydroxyapatite, PUHA degradable polyurethane fibers with nano-hydroxyapatite; PVA polyvinyl alcohol, rhBMP-2 recombinant human bone morphogenetic protein-2; Periosteum; SEM scanning electron microscope, SF silk fibroin; SSP synthetic scaffold periosteum, TCP tricalcium phosphate; SiNPs Silica nanoparticles, SIS small intestinal submucosa; TGF-β transforming growth factor-β, VEGF vascular endothelial growth factors; Tissue-engineered periosteum; co-PUPCL a mixed fiber formed by PCL and polyurethane, DEX dexamethasone; rMSCs rat mesenchymal stem cells, Runx2 Runt-related transcription factor 2; s-PEEK sulfonated PEEK, SSCs skeletal stem cells.”

7、Production of recombinant human insulin from a promising Pseudomonas fluorescens cell factory and its kinetic modeling
Ansuman Sahoo,et al.Int J Biol Macromol. 2024.PMCID: 39293616
“Insulin intake is recommended for diabetics in addition to a proper diet and lifestyle to maintain adequate blood glucose level. Currently, there is a need for an alternative expression system for insulin production as the current expression systems may not meet the growing demand due to various constraints. Here, we demonstrate the synthesis of human insulin in an unconventional expression system based on Pseudomonas fluorescens, a BSL 1 bacterium. Human insulin was produced in the form of proinsulin fused with fusion protein. Then, the proinsulin fusion protein was purified using Ni-NTA chromatography and converted into human insulin. The physicochemical parameters for producing proinsulin fusion protein are optimized. Glucose and ammonium chloride are determined to be suitable carbon and nitrogen sources, respectively. The validity of insulin and proinsulin fusion protein is assessed using western blot and quantified using ELISA techniques. Up to 145.35 mg/l of the proinsulin fusion protein is achieved at the shake flask level. Further, MALDI-TOF and RP-HPLC analysis of the purified human insulin were observed to be close to the theoretical value and insulin standard, respectively. The expression of the recombinant fusion protein was found to be 214.7 mg/l in a batch bioreactor, a ∼48% enhancement over the shake flask level. Further, kinetic modeling was performed to understand the system regarding growth, substrate utilization and product formation, and to estimate the various kinetic parameters. This study establishes the potential of the P. fluorescens expression system for producing human insulin.
Keywords: Fusion protein; Kanamycin; Kinetic modeling; One-factor-at-a-time; Proinsulin form; Pseudomonas fluorescens; Recombinant human insulin.”

8、Efficacy and Safety of Enteral Recombinant Human Insulin in Preterm Infants: A Randomized Clinical Trial
Elise Mank,et al.JAMA Pediatr. 2022.PMCID: 35226099
“Importance: Feeding intolerance is a common condition among preterm infants owing to immaturity of the gastrointestinal tract. Enteral insulin appears to promote intestinal maturation. The insulin concentration in human milk declines rapidly post partum and insulin is absent in formula; therefore, recombinant human (rh) insulin for enteral administration as a supplement to human milk and formula may reduce feeding intolerance in preterm infants.
Objective: To assess the efficacy and safety of 2 different dosages of rh insulin as a supplement to both human milk and preterm formula.
Design, setting, and participants: The FIT-04 multicenter, double-blind, placebo-controlled randomized clinical trial was conducted at 46 neonatal intensive care units throughout Europe, Israel, and the US. Preterm infants with a gestational age (GA) of 26 to 32 weeks and a birth weight of 500 g or more were enrolled between October 9, 2016, and April 25, 2018. Data were analyzed in January 2020.
Interventions: Preterm infants were randomly assigned to receive low-dose rh insulin (400-μIU/mL milk), high-dose rh insulin (2000-μIU/mL milk), or placebo for 28 days.
Main outcomes and measures: The primary outcome was time to achieve full enteral feeding (FEF) defined as an enteral intake of 150 mL/kg per day or more for 3 consecutive days.
Results: The final intention-to-treat analysis included 303 preterm infants (low-dose group: median [IQR] GA, 29.1 [28.1-30.4] weeks; 65 boys [59%]; median [IQR] birth weight, 1200 [976-1425] g; high-dose group: median [IQR] GA, 29.0 [27.7-30.5] weeks; 52 boys [55%]; median [IQR] birth weight, 1250 [1020-1445] g; placebo group: median [IQR] GA, 28.8 [27.6-30.4] weeks; 54 boys [55%]; median [IQR] birth weight, 1208 [1021-1430] g). The data safety monitoring board advised to discontinue the study early based on interim futility analysis (including the first 225 randomized infants), as the conditional power did not reach the prespecified threshold of 35% for both rh-insulin dosages. The study continued while the data safety monitoring board analyzed and discussed the data. In the final intention-to-treat analysis, the median (IQR) time to achieve FEF was significantly reduced in 94 infants receiving low-dose rh insulin (10.0 [7.0-21.8] days; P = .03) and in 82 infants receiving high-dose rh insulin (10.0 [6.0-15.0] days; P = .001) compared with 85 infants receiving placebo (14.0 [8.0-28.0] days). Compared with placebo, the difference in median (95% CI) time to FEF was 4.0 (1.0-8.0) days for the low-dose group and 4.0 (1.0-7.0) days for the high-dose group. Weight gain rates did not differ significantly between groups. Necrotizing enterocolitis (Bell stage 2 or 3) occurred in 7 of 108 infants (6%) in the low-dose group, 4 of 88 infants (5%) in the high-dose group, and 10 of 97 infants (10%) in the placebo group. None of the infants developed serum insulin antibodies.
Conclusions and relevance: Results of this randomized clinical trial revealed that enteral administration of 2 different rh-insulin dosages was safe and compared with placebo, significantly reduced time to FEF in preterm infants with a GA of 26 to 32 weeks. These findings support the use of rh insulin as a supplement to human milk and preterm formula.”

9、Five-Year Therapy with Recombinant Human Insulin-Like Growth Factor-1 in a Patient with PAPP-A2 Deficiency
Gajanthan Muthuvel,et al.Horm Res Paediatr. 2023.PMCID: 36646053
“Introduction: The metalloproteinase pregnancy-associated plasma protein A2 (PAPP-A2) cleaves insulin-like growth factor (IGF)-binding proteins 3 and 5 to release bioactive IGF-I from its ternary complex. Patients with mutations in PAPP-A2 have growth failure and low free IGF-I despite elevated total IGF-I. We describe 5-year treatment response to recombinant human IGF-1 (rhIGF-1) in a patient with PAPP-A2 deficiency, and the phenotype of PAPP-A2 deficiency in three siblings.
Methods: Two siblings (P2, P3) with PAPP-A2 deficiency were recruited for rhIGF-1 therapy at 120 μg/kg subcutaneous twice daily, along with a third sibling (P1) for phenotyping. We evaluated efficacy and safety of rhIGF-1 therapy, including effect on metabolic measures and bone mineral density (BMD).
Results: Treatment with rhIGF-1 was started in 10.4-year- (P3) and 14.5-year (P2)-old brothers. P2 discontinued therapy due to pseudotumor cerebri. P3 continued rhIGF-1 for 5 years; height velocity increased (3.0 cm/year at baseline; 5.0-7.6 cm/year thereafter) as did height SDS (+0.6). P3’s pubertal onset was at 12.4 year. BMD height-adjusted Z-score modestly improved for lumbar spine (+0.4), and decreased in forearm (-0.2) and hip (-0.3). All siblings had hyperinsulinemia. Impaired glucose tolerance (IGT) resolved in P1. P2 showed worsening glucose tolerance (2-h glucose: 225 mg/dL). Impaired fasting glucose and hyperinsulinemia initially resolved for P3, but IGT (2-h glucose: 152 mg/dL) developed during puberty.
Conclusion: Therapy with rhIGF-1 modestly improved linear growth in one patient with PAPP-A2 deficiency, but without true catch-up. Therapy was associated with pseudotumor cerebri in a sibling. Initial improvement in BMD and glycemic pattern on rhIGF-1 was not sustained during puberty.
Keywords: Growth failure; PAPP-A2 deficiency; Recombinant human IGF-1.”

10、Exogenous recombinant human insulin-induced severe hypersensitivity reaction precipitating hyperglycemic crisis: A clinical conundrum
K U Lijesh,et al.J Family Med Prim Care. 2020.PMCID: 33110889
“Hypersensitivity reactions against exogenous insulin are a rare clinical entity after the advent of recombinant human insulin; however, there are still case reports wherein patients develop hypersensitivity reactions against insulin. We present the case of a type 1 diabetes mellitus patient who developed type 1 hypersensitivity reaction against subcutaneous insulin. He had recurrent episodes of diabetic ketoacidosis after developing hypersensitivity reactions against insulin, requiring multiple hospital admissions. When he presented to us, he was on both insulin infusion and subcutaneous insulin, requiring a daily insulin dose of about 800 units and having severe insulin hypersensitivity reactions and hyperglycemia. He had multiple subcutaneous erythematous nodules at the insulin injection sites, however, had no evidence of systemic allergy. Investigations revealed eosinophilic leukocytosis, and high IgE levels and skin biopsy showing evidence of insulin hypersensitivity. He was desensitized to insulin according to Heinzerling et al. insulin desensitization protocol and subsequently with immunomodulation therapy using steroids (pulse methylprednisolone) and mycophenolate mofetil as well as by installation of insulin pump.
Keywords:Desensitization protocol; immunomodulation; insulin hypersensitivity; insulin pump.”

Preparation Instructions of Recombinant Human Insulin
To dissolve insulin, use either dilute acetic acid (1%) or hydrochloric acid (pH 2-3) at a concentration of 1-10 mg/mL. Insulin stock solutions should be aliquoted into single-use volumes, stored frozen at -20°C, and repeated freeze-thaw cycles must be avoided. Alternatively, after sterile filtration through a low protein-binding membrane, solutions may be stored refrigerated at 2-8°C for up to 6 months. Note: Though insulin can also be dissolved in 125 mM sodium bicarbonate solution, alkaline stock solutions are not recommended due to accelerated rates of deamidation and aggregation at high pH. Autoclaving of insulin solutions is strictly prohibited.

Precautions and Disclaimer for Recombinant Human Insulin (Cell Culture Grade)
Recombinant human insulin is intended for laboratory use only. It is strictly prohibited for pharmaceutical, household, or any other applications.

Structure of Recombinant Human Insulin(CAS No.: 11061-68-0)

No more offers for this product!