Biotinylated Human IGFBP-5 Protein (C-6His-Avi)

Name: Biotinylated Human IGFBP-5 Protein (C-6His-Avi)
Brand: Beta LifeScience
SKU: BL-2638NP
Availability: InStock

BL-2638NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: Avi-tagged proteins, Biotinylated proteins, Cytokines and growth factors, Featured biotinylated protein molecules, Growth factors and receptors, Recombinant proteins

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Product Overview

Description	Biotinylated Recombinant Human Insulin-Like Growth Factor-Binding Protein 5 is produced by our Mammalian expression system and the target gene encoding Leu21-Glu272 is expressed with a 6His, Avi tag at the C-terminus.
Accession	P24593
Synonym	Insulin-Like Growth Factor-Binding Protein 5; IBP-5; IGF-Binding Protein 5; IGFBP-5; IGFBP5; IBP5
Gene Background	Insulin-Like Growth Factor-Binding Protein 5 (IGFBP-5) is a secreted protein that belongs to the insulin-like growth factor (IGF) binding proteins superfamily. Members of this family prolong the half-life of the IGFs. They have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. IGFBP-5 contains one IGFBP N-terminal domain and one thyroglobulin type-1 domain. IGFBP-5 is expressed by fibroblasts, myoblasts and Osteosarcoma. It is also present at lower levels in liver, kidney, and brain.
Molecular Mass	31.4 KDa
Apmol Mass	32-45 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 300mM NaCl, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular Location	Secreted.
Database References	HGNC: 5474 OMIM: 146734 KEGG: hsa:3488 STRING: 9606.ENSP00000233813 UniGene: Hs.607212
Tissue Specificity	Osteosarcoma, and at lower levels in liver, kidney and brain.

Gene Functions References

Data suggest that IGFBP5 nuclear import is mediated by KPNA5/KPNB1 complex; nuclear localization sequence of IGFBP5 is critical domain in this nuclear translocation. (IGFBP5 = insulin-like growth factor binding protein-5; KPNA5 = karyopherin subunit alpha-5; KPNB1 = karyopherin subunit beta-1/importin-beta) PMID: 28835592
These results suggest that the C-terminus of IGFBP-5 exerts anti-cancer activity by inhibiting angiogenesis via regulation of the Akt/ERK and NF-kB-VEGF/MMP-9 signaling pathway. PMID: 28008951
AMP-IBP5 markedly enhanced keratinocyte migration and proliferation. AMP-IBP5-induced keratinocyte activation was mediated by Mrg X1-X4 receptors with MAPK and NF-kappaB pathways. PMID: 28554590
Factor Xa induced endothelial cell senescence through IGFBP-5. PMID: 27752126
The findings suggest that miR-140 suppresses colorectal cancer progression and metastasis, possibly through downregulating ADAMTS5 and IGFBP5. PMID: 27906093
MiR-137 inhibited cell proliferation and migration of vascular smooth muscle cells via targeting IGFBP-5 and modulating the mTOR/STAT3 signaling. PMID: 29016699
dysregulation of DNMT3A and IGFBP5 is relevant to preeclampsia. Thus, we propose that DNMT3A and IGFBP5 can serve as potential markers and targets for the clinical diagnosis and therapy of preeclampsia. PMID: 28049695
IGFBP5 promoter and exon-I methylation did not have any differences between tumor and adjacent tissues so that IGFBP5 methylation did not change IGFBP5 gene regulation in breast cancer. PMID: 27612043
IGFBP5 promoted osteogenic differentiation potentials of periodontal ligament stem cells and Wharton's jelly umbilical cord stem cells via the JNK and MEK/Erk signalling pathways. PMID: 27484838
Data demonstrate that dysregulation of miR-143-3p:Igfbp5 interactions in satellite cells with age may be responsible for age-related changes in satellite cell function. PMID: 26762731
Results shed light on the mechanism of IGFBP5 as a potential tumor-suppressor in melanoma progression. PMID: 26010068
data provide further insights into the role of cellular compartmentalization in IGFBP-5-induced fibrosis PMID: 26103640
Demethylation of IGFBP5 by Histone Demethylase KDM6B Promotes Mesenchymal Stem Cell-Mediated Periodontal Tissue Regeneration by Enhancing Osteogenic Differentiation and Anti-Inflammation Potentials. PMID: 25827480
rs4442975 at 2q35 flanks a transcriptional enhancer that physically interacts with the promoter of IGFBP5. Evidence suggests that the g-allele confers increased breast cancer susceptibility through relative downregulation of IGFBP5. PMID: 25248036
IGFBP5 mRNA expression is a good indicator in clinical outcome of breast cancer patients. PMID: 25422220
miR-204-5p suppresses IGFBP5 expression by direct binding to the 3' untranslated region. PMID: 25603050
IGFBP-5 may be a negative modulator of RASSF1C/ PIWIL1 growth-promoting activities. PMID: 25007054
IGFBP-5 induces its pro-fibrotic effects, at least in part, via DOK5. IGFBP-5 and DOK5 are both increased in systemic sclerosis fibroblasts and tissues and may thus be acting in concert to promote fibrosis. PMID: 24551065
IGFBP-5 is important in maintaining epithelial-mesenchymal boundaries and thus may limit metastasis and fibrosis by inducing an orderly repair mechanism, very distinct from the fibrotic disruption induced by TGFbeta1. PMID: 24120850
Serum IGFBP-5 concentrations were lower in Crohn's disease patients compared to healthy controls regardless of disease activity or the presence of stricture formation. PMID: 24379630
IGFBP-5 modulates the efficiency of estrogen-triggered activation of the Akt/PKB signaling pathway which has been associated with growth factor/ ERalpha cross-talks. PMID: 23499909
IGFBP-5 overexpression is a poor prognostic factor in patients with urothelial carcinomas of upper urinary tracts and urinary bladder. PMID: 23539739
IGFBP5 domains modulate tumorigenicity and metastasis of human osteosarcoma in different ways PMID: 23665505
Data suggest that insulin-like growth factor-binding protein 5 (IGFBP5) regulation by calcium-dependent chloride channel DOG1. PMID: 23576565
The IGFBP5 enhanced adhesion, it inhibited cell migration, although this was not evident using the truncated C-terminal mutant, suggesting that effects of IGFBP5 on adhesion and migration involve different mechanisms. PMID: 22328518
c-Src and IL-6 inhibit osteoblast differentiation and integrate IGFBP5 signalling PMID: 22252554
This study demonistrated that IGFBP5 was significantly decreased in skeletal muscel in patient with amyotrophic lateral sclerosis. PMID: 22246875
Data revealed a strong induction of several genes encoding components of the extracellular matrix, such as collagens, COMP, IGFBP5 and biglycan. PMID: 21029365
Insulin-like growth factor binding protein 5 is a novel marker that has an important role in the pathogenesis of osteosarcoma. The loss of insulin-like growth factor binding protein 5 function may contribute to metastasis in osteosarcoma. PMID: 21460855
The IGFBP5 polymorphism is functional and may potentially be a biomarker for susceptibility to late-stage risk of squamous cell carcinoma of the head and neck. PMID: 20949447
results suggest that PGE(2) may play an important role in controlling cellular senescence of HDFs through the regulation of IGFBP5 and therefore may contribute to inflammatory disorders associated with aging PMID: 21191810
Decreased Cav-1 expression in fibrotic diseases likely leads to increased deposition of IGFBP-5 in the extracellular matrix. PMID: 20345844
the L-domain of IGFBP-5 is a novel TNFR1 ligand that functions as a competitive TNF-alpha inhibitor. PMID: 21256825
IGFBP-5 has an effect on human hair shape. PMID: 20944648
Data indicate that retinal astrocytes enhance the proliferation of cone-like retinoblastoma cells by deploying IGFBP5, a factor that also provides trophic support to the tumor cells' non-neoplastic counterparts. PMID: 20508032
Data show that IGFBP5 expression is down-regulated during 4HPR-induced neuronal differentiation of human RPE cells through a MAPK signal transduction pathway involving C/EBPbeta. PMID: 20583135
insulin-like growth factor binding protein 5 is a modulator of tamoxifen resistance in breast cancer PMID: 20354179
Regulation of the IGFBP-5 and MMP-13 genes by the microRNAs miR-140 and miR-27a in human osteoarthritic chondrocytes. PMID: 19948051
Insulin-like growth factor-binding protein 5 (IGFBP-5) interacts with a four and a half LIM protein 2 (FHL2). PMID: 11821401
role in stimulating growth and IGF-I secretion in intestinal smooth muscle by ras-dependent activation of MAP kinase signaling pathways PMID: 11923300
c-Myb and B-Myb transactivate the IGFBP-5 promoter through binding-dependent and -independent mechanisms. PMID: 11973331
cDNA probes were used to analyze the gene expression of IGFBP-5 in luteinized granulosa cells from different-sized follicles after ovarian hyperstimulation. Transcript levels increased with increasing follicular fluid (FF) volume PMID: 12005306
IGFBP-5 is a potent growth inhibitor and proapoptotic agent in human breast cancer cells via modulation of cell cycle regulation and apoptotic mediators PMID: 12777377
Fibronectin and IGFBP-5 bind to each other, and this binding negatively regulates the ligand-dependent action of IGFBP-5 by triggering IGFBP-5 proteolysis. PMID: 14645245
The IGFBP-5 C-domain is necessary and sufficient for its nuclear localization, and residues K206, K208, K217, and K218 are particularly critical. The IGFBP-5 N-domain contains a putative transactivation domain. PMID: 15001525
exogenous IGFBP-5 increases apoptosis by binding to and inhibiting the activities of insulin-like growth factors PMID: 15155755
Understanding the mechanism of how cleavage of IGFBP-5 by this protease (IGFBPase) alters its activity will help to further our understanding of the biologic actions of the IGFs PMID: 15534875
Inhibition of expression of IGFBP-5 by micro and small interfering RNA has marked effect on neuroblastoma cell proliferation, apoptosis, and differentiation PMID: 15618969
IGFBP-5 has a role in growth and differentiation of neuroblastoma cells PMID: 15650232
Activation by C/EBP alpha and beta did not depend on their binding to the C/EBP site, since they still activated IGFBP-5 promoter. PMID: 15777798

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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.