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 >  Protein>IGFBP-5 >IG5-H82D3

Biotinylated Human IGFBP-5 Protein, Avitag™,Flag&His Tag (MALS verified)

分子别名(Synonym)

IBP5,IGFBP5

表达区间及表达系统(Source)

Biotinylated Human IGFBP-5 Protein, Avitag,Flag&His Tag (IG5-H82D3) is expressed from human 293 cells (HEK293). It contains AA Leu 21 - Glu 272 (Accession # P24593).

Predicted N-terminus: Gly

Request for sequence

蛋白结构(Molecular Characterization)

IGFBP-5 Structure

This protein carries an Avi tag (Avitag™) at the N-terminus followed a Flag tag and at the C-terminus by a polyhistidine tag. The protein has a calculated MW of 33.3 kDa. The protein migrates as 38-43 kDa 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)

>90% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 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)

IGFBP-5 SDS-PAGE

Biotinylated Human IGFBP-5 Protein, Avitag,Flag&His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS

IGFBP-5 SEC-MALS

The purity of Biotinylated Human IGFBP-5 Protein, Avitag,Flag&His Tag (Cat. No. IG5-H82D3) is more than 90% and the molecular weight of this protein is around 35-55 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

IGFBP-5 ELISA

Immobilized Human IGF-I Protein, Fc Tag (Cat. No. IG1-H5263) at 5 μg/mL (100 μL/well) can bind Biotinylated Human IGFBP-5 Protein, Avitag,Flag&His Tag (Cat. No. IG5-H82D3) with a linear range of 0.5-16 ng/mL (QC tested).

Protocol

 
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背景(Background)

IGFBP5 stands for Insulin-like Growth Factor Binding Protein 5. It is a protein that belongs to the insulin-like growth factor binding protein (IGFBP) family. IGFBP5 plays a crucial role in regulating the activity and distribution of insulin-like growth factors (IGFs) in the body. Enables insulin-like growth factor I binding activity.

 

前沿进展

IGF1 Signaling Regulates Neuropeptide Expression in Hypothalamic Neurons Under Physiological and Pathological Conditions
He, Loganathan, Belsham
Endocrinology (2025) 166 (5)
Abstract: Insulin-like growth factor 1 (IGF1) plays a critical role in metabolism and aging, but its role in the brain remains unclear. This study examined whether hypothalamic neurons respond to IGF1 and how its actions are modulated. RT-qPCR and single-cell RNA sequencing indicated that Igf1r mRNA is expressed in neuropeptide Y/Agouti-related peptide (NPY/AgRP) neurons but has higher expression in pro-opiomelanocortin (POMC) neurons. IGF1 binding proteins Igfbp3 and Igfbp5 were significantly expressed, whereby Igfbp5 levels were modulated by fasting, nutrient availability, and circadian rhythms, implying that IGF1 signaling can be controlled by multiple mechanisms. In mouse and human models, IGF1 regulated Agrp, Npy, Pomc, Cartpt, Spx, Gal, and Fam237b expression, producing an overall anorexigenic profile. Hyperinsulinemia induced IGF1 resistance, accompanied by reduced IGF1R protein, as well as Igf1r and Irs2 mRNA expression via over-activation of phosphoinositide 3-kinase/forkhead box O1 (PI3K-FOXO1) signaling. Thus, hypothalamic neurons respond to IGF1 under physiological conditions, and hyperinsulinemia is a novel mechanism that drives cellular IGF1 resistance.© The Author(s) 2025. Published by Oxford University Press on behalf of the Endocrine Society.
Targeting insulin-like growth factor 1 receptor restricts development and severity of secondary lymphedema in mice
Yuan, Levy, Yeo et al
iScience (2025) 28 (3), 111948
Abstract: Secondary lymphedema is a debilitating chronic tissue swelling in a limb caused by inadequate interstitial fluid drainage due to dysfunctional lymphatic vessels. Pathological enlargement of small lymphatics contributes to lymphatic dysfunction in secondary lymphedema, but molecular mechanisms driving this remodeling are unclear. Here, using a surgical mouse model of secondary lymphedema and whole-genome microarray, we identified the transcript for insulin-like growth factor binding protein 5 (IGFBP5), a negative regulator of insulin-like growth factor (IGF) signaling, as the most profoundly down-regulated in lymphedematous tissue. Notably, IGF signaling via IGF1 receptor (IGF1R) was previously shown to promote lymphatic remodeling. We therefore targeted IGF1R in the mouse model using the small molecule IGF1R inhibitor linsitinib. Linsitinib restricted enlargement of small lymphatics and tissue swelling during lymphedema development, likely by inhibiting IGF1R-driven vascular endothelial growth factor-C (VEGF-C) synthesis by macrophages. Importantly, linsitinib profoundly reduced tissue swelling in mice with chronic lymphedema suggesting IGF signaling as a therapeutic target for this disease.© 2025 The Authors.
Schwann cells secrete IGFBP5 to facilitate the growth of keloids
Wei, Shi, Wang et al
Life Sci (2025) 369, 123534
Abstract: Keloids (KD) are noncancerous fibroproliferative tumors exhibiting cancer-like traits, encompass aggressive unregulated growth, absence of natural regression, and a significantly high rate of recurrence. The precise molecular mechanisms underlying KD pathology remain poorly understood. In this study, we employed single-cell sequencing to examine the characteristics of cells in KD and normal scar (NS) tissue. We evaluated Schwann cells and their secretory protein IGFBP5 function in KD. Then, the recombinant IGFBP5 protein was employed to elucidate the regulatory roles of IGFBP5 in the proliferation, migration, invasion, angiogenesis, and cell cycle of keloids fibroblasts (KF). The rabbit ear scar model was utilized to ascertain the function of IGFBP5 in vivo. We demonstrated that in KD, the proportion of Schwann cells was 4.13 times that of NS. Besides, the IGFBP5 gene exhibited an expression level that was 8.02 times higher in KD Schwann cells compared to those in NS Schwann cells. High IGFBP5 expression was positively associated with the cell proliferation, migration, invasion, angiogenesis, and cell cycle of KF. Additionally, the p53/p21/Cyclin D1 pathway regulated cell cycle and promoted cell proliferation, which was suppressed after rIGFBP5 administration. These findings suggest that Schwann cells infiltrate in KD and secrete IGFBP5 protein to promote KD growth, and targeting IGFBP5 or Schwann cell infiltration could offer novel therapeutic strategies for KD.Copyright © 2025 The Authors. Published by Elsevier Inc. All rights reserved.
IGFBP5 regulates fibrocartilage differentiation and cartilage injury induced by T-2 toxin via blocking IGF-1/IGF-1R signaling
Wang, Wang, Lei et al
Rheumatology (Oxford) (2025)
Abstract: Kashin-Beck disease (KBD) is a form of osteoarthropathy that affects the skeletal and joint systems of children and adolescents. Insulin-like Growth Factor Binding Protein 5 (IGFBP5) plays an important role in bone growth and development. This study aimed to investigate the role of IGBFP5 in regulating the function and differentiation of chondrocytes in KBD.The mRNA and protein expressions of IGFBP5, IGF-1 and IGF-1R were detected by RT-qPCR and western blot assays. Commercial kits were performed to measure the mitochondrial ROS content, calcium loading and ATP synthesis in chondrocytes. MTT assay was used to detect the cell viability of chondrocytes. Co-IP and pull-down assays were conducted to verify the binding activity of IGFBP5 to IGF-1R. The rat KBD model was constructed by a low selenium diet and T-2 toxin.The expression of IGFBP5 was upregulated in KBD patient and rat tissues. Further studies showed that interfering with IGFBP5 effectively inhibited T-2-induced chondrocyte damage and mitochondrial stress. IGFBP5 depressed the interaction between IGF-1 and IGF-1R, thereby affecting the regulation of IGF-1/IGF-1R signalling in the repair of chondrocytes. In addition, the fibrous differentiation of cartilage progenitor cells (CPCs) and the activity and migration of CPCs induced by T-2 stimulation were suppressed under IGFBP5 silence treatment.IGFBP5 was upregulated during the pathological progression of KBD, and IGFBP5 competitively bound with IGF-1R to impede the interactions between IGF-1 and IGF-1R. Knockdown of IGFBP5 inhibited fibrotic differentiation and ameliorated reduction of CPC function in KBD model.© The Author(s) 2025. Published by Oxford University Press on behalf of the British Society for Rheumatology. All rights reserved. For commercial re-use, please contact reprints@oup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.
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