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 >  Protein>IGF-II >IG2-H82F9

Biotinylated Human IGF-II Protein, Avitag™,Fc Tag

分子别名(Synonym)

IGF2,C11orf43,FLJ22066,FLJ44734,IGF-II,PP9974

表达区间及表达系统(Source)

Biotinylated Human IGF-II, Avitag,Fc Tag (IG2-H82F9) is expressed from human 293 cells (HEK293). It contains AA Ala 25 - Glu 91 (Accession # P01344-1).

Predicted N-terminus: Gly

Request for sequence

蛋白结构(Molecular Characterization)

IGF-II Structure

This protein carries an Avi tag (Avitag™) at the N-terminus, followed by a human IgG1 Fc tag.

The protein has a calculated MW of 35.3 kDa. The protein migrates as 38-42kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

标记(Labeling)

Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.

蛋白标记度(Protein Ratio)

Passed as determined by the HABA assay / binding ELISA.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>95% as determined by SDS-PAGE.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in Tris with Glycine, Arginine and NaCl, pH7.5 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

电泳(SDS-PAGE)

IGF-II SDS-PAGE

Biotinylated Human IGF-II, Avitag,Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

 

活性(Bioactivity)-ELISA

IGF-II ELISA

Immobilized Human IGFBP-3, His Tag (Cat. No. IG3-H52H9) at 5 μg/mL (100 μL/well) can bind Biotinylated Human IGF-II, Avitag,Fc Tag (Cat. No. IG2-H82F9) with a linear range of 1.2-39 ng/mL (QC tested).

Protocol

 
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背景(Background)

Insulin-like growth factor 2 (IGF-2) is also known as Somatomedin-A, IGF-II, PP9974, and is one of three protein hormones that share structural similarity to insulin. IGF-2 exerts its effects by binding to the IGF-1 receptor. IGF2 may also bind to the IGF-2 receptor (also called the cation-independent mannose 6-phosphate receptor), which acts as a signalling antagonist; that is, to prevent IGF2 responses. The major role of IGF2 is as a growth promoting hormone during gestation. In the process of Folliculogenesis, IGF2 is created by Theca cells to act in an autocrine manner on the theca cells themselves, and in a paracrine manner on Granulosa cells in the ovary. IGF2 promotes granulosa cell proliferation during the follicular phase of the menstrual cycle, acting alongside Follicle Stimulating Hormone (FSH). After ovulation has occurred, IGF-2 promotes progesterone secretion during the luteal phase of the menstrual cycle together with Luteinizing Hormone (LH). Thus, IGF2 acts as a Co-hormone together with both FSH and LH. IGF-2 may play a key role in memory and could potentially be used to treat Alzheimer's Disease. It is sometimes produced in excess in islet cell tumours, causing hypoglycemia. Doege-Potter syndrome is a paraneoplastic syndrome in which hypoglycemia is associated with the presence of one or more non-islet fibrous tumors in the pleural cavity. has been shown to interact with IGFBP3 and Transferrin.

 

前沿进展

Targeted proteomics of serum IGF-I, -II, IGFBP-2, -3, -4, -5, -6 and ALS
Albrethsen, Drici, Slot Vilmann et al
Clin Chem Lab Med (2025)
Abstract: The insulin-like growth factors (IGFs) regulate growth in humans. IGF-I and IGF binding protein (IGFBP)-3 are biomarkers in children with growth disorders. We investigate a targeted proteomics method for absolute quantitation of eight IGF protein family members in human serum, including the peptide hormones IGF-I and -II, and the six binding proteins IGFBP-2, -3, -4, -5, -6 and acid labile subunit (ALS).Serum preparation was optimized for targeted proteomics of IGF related proteins on a clinical LC-MS/MS platform (UHPLC coupled with Triple-Q MS). We created quality controls, standards and internal standards and 289 serum samples from healthy children and adolescents were measured in ten batches over two months. The method was compared to WHO reference standards, clinical and research immunoassays, and relative proteomics profiling.The sensitivity and reproducibility were sufficient for most but not all IGF protein family members. Targeted proteomics correlated well with clinical immunoassays for IGF-I (R2=0.88) and for IGFBP-3 (R2=0.46), (p<0.001). The correlation between targeted proteomics and non-clinical immunoassays for IGF-II, IGFBP-2, -4, -5, -6 and ALS varied between proteins.We present a method for parallel quantification of IGF-I, IGFBP-3, 5 and ALS for clinical verification studies, whereas targeted proteomics of the five remaining IGF related proteins (IGF-II, IGFBP-2, -4, and -6) require further examination. The sensitivity of our new IGF-I method suggests a possible diagnostic role for targeted proteomics of IGF-I in the management of children with extremely low levels of circulating IGF-I.© 2025 Walter de Gruyter GmbH, Berlin/Boston.
Insulin‑like growth factor 2 in spermatogenesis dysfunction (Review)
Tang, Wang, Tang et al
Mol Med Rep (2025) 31 (5)
Abstract: Spermatogenesis dysfunction is characterized by abnormal morphology, destruction, atrophy of seminiferous tubules, blocked differentiation of spermatogenic cells, decreased sperm count and increased sperm abnormalities. Inflammation, oxidative stress, endoplasmic reticulum stress and obesity are important factors leading to spermatogenesis dysfunction. It has been demonstrated that insulin‑like growth factor 2 (IGF2) is closely related to the aforementioned factors. In the present review, the relationship between IGF2 and inflammation, oxidative stress, ER stress and obesity was investigated, providing theoretical and experimental evidence on the role of IGF2 in the prevention and treatment of spermatogenesis dysfunction of male infertility.
Mutation of an insulin-sensitive Drosophila insulin-like receptor mutant requires methionine metabolism reprogramming to extend lifespan
Tatar, Zheng, Yadav et al
bioRxiv (2025)
Abstract: Insulin/insulin growth factor signaling is a conserved pathway that regulates lifespan across many species. Multiple mechanisms are proposed for how this altered signaling slows aging. To elaborate these causes, we recently developed a series of Drosophila insulin-like receptor (dInr) mutants with single amino acid substitutions that extend lifespan but differentially affect insulin sensitivity, growth and reproduction. Transheterozygotes of canonical dInr mutants (Type I) extend longevity and are insulin-resistant, small and weakly fecund. In contrast, a dominant mutation (dInr 353, Type II) within the Kinase Insert Domain (KID) robustly extends longevity but is insulin-sensitive, full-sized, and highly fecund. We applied transcriptome and metabolome analyses to explore how dInr 353 slows aging without insulin resistance. Type I and II mutants overlap in many pathways but also produce distinct transcriptomic profiles that include differences in innate immune and reproductive functions. In metabolomic analyses, the KID mutant dInr 353 reprograms methionine metabolism in a way that phenocopies dietary methionine restriction, in contrast to canonical mutants which are characterized by upregulation of the transsulfuration pathway. Because abrogation of S-adenosylhomocysteine hydrolase blocks the longevity benefit conferred by dInr 353, we conclude the methionine cycle reprogramming of Type II is sufficient to slow aging. Metabolomic analysis further revealed the Type II mutant is metabolically flexible: unlike aged wildtype, aged dInr 353 adults can reroute methionine toward the transsulfuration pathway, while Type I mutant flies upregulate the trassulfuration pathway continuously from young age. Altered insulin/insulin growth factor signaling has the potential to slow aging without the complications of insulin resistance by modulating methionine cycle dynamics.
IGF2BP3 promotes the proliferation and cisplatin resistance of bladder cancer by enhancing the mRNA stability of CDK6 in an m6A dependent manner
Song, Wang, Yu et al
Int J Biol Sci (2025) 21 (5), 2048-2066
Abstract: Cisplatin-based chemotherapy is a primary treatment for bladder cancer, yet the development of chemoresistance poses a significant therapeutic challenge. Insulin-like growth factor II mRNA binding protein 3 (IGF2BP3) is an RNA-binding protein and a key m6A reader that regulates various cancers through m6A-dependent mechanisms. However, its role in chemotherapy resistance in bladder cancer remains unclear. Our in vivo and in vitro experiments identified IGF2BP3 as a key regulator of cisplatin resistance in bladder cancer. We demonstrated that IGF2BP3 enhances the stability of CDK6 mRNA in an m6A-dependent manner, leading to increased CDK6 expression. This, in turn, promoted tumor cell proliferation and resistance to cisplatin chemotherapy. Moreover, we showed that the CDK6 inhibitor palbociclib effectively suppresses the pro-growth and chemoresistant effects induced by IGF2BP3 overexpression. These results suggested that the IGF2BP3/m6A/CDK6 axis plays a pivotal role in bladder cancer progression and chemoresistance, and that targeting this pathway with CDK6 inhibitors such as palbociclib may offer a promising therapeutic strategy for overcoming cisplatin resistance in bladder cancer.© The author(s).
Showing 1-4 of 15007 papers.
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IGF-II靶点信息
英文全称:Insulin-like growth factor II
中文全称:胰岛素样生长因子Ⅱ
种类:Homo sapiens
上市药物数量:0详情
临床药物数量:1详情
最高研发阶段:临床二期
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