Recombinant Human Insulin-Like Growth Factor Ii (IGF2), Active

Name: Recombinant Human Insulin-Like Growth Factor Ii (IGF2), Active
Brand: Beta LifeScience
SKU: BLC-05942P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Description	Recombinant Human Insulin-Like Growth Factor Ii (IGF2), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined in a serum-free cell proliferation assay using MCF-7 human breast cancer cells is less than 20 ng/ml.
Uniprotkb	P01344
Target Symbol	IGF2
Synonyms	C11orf43; IGF 2; IGF II; IGF-II; IGF2; IGF2_HUMAN; IGFII; INSIGF; insulin like growth factor 2 (somatomedin A) ; Insulin like Growth Factor 2; Insulin like growth factor II; Insulin like growth factor II precursor; Insulin like growth factor type 2; pp9974; Preptin; putative insulin like growth factor II associated protein; Somatomedin A; Somatomedin-A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	AYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSE
Expression Range	25-91aa
Protein Length	Full Length of Mature Protein
Mol. Weight	8.91 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm Filtered 5 mM HAC, PH 3.0
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	The insulin-like growth factors possess growth-promoting activity. Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver (Probable). Acts as a ligand for integrin which is required for IGF2 signaling. Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation. Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate.; Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.
Subcellular Location	Secreted.
Protein Families	Insulin family
Database References	HGNC: 5466 OMIM: 147470 KEGG: hsa:3481 STRING: 9606.ENSP00000391826 UniGene: Hs.272259
Associated Diseases	Silver-Russell syndrome (SRS); Growth restriction, severe, with distinctive facies (GRDF)
Tissue Specificity	Expressed in heart, placenta, lung, liver, muscle, kidney, tongue, limb, eye and pancreas.

Gene Functions References

serum preptin levels in women decrease after menopause and have a positive correlation with estradiol, femoral and total hip bone mineral density. PMID: 29134283
Analysis of patient serum samples showed that concurrent elevation of insulin like growth factor 2 (IGF2) and vascular endothelial growth factor (VEGF) levels may serve as a prognostic biomarker for oesophageal cancer. PMID: 28186102
Our results revealed that IGF-II promotes cell proliferation and EMT in HCC cells. PMID: 29970663
Serum preptin levels were significantly higher in women with polycystic ovary syndrome compared with controls. PMID: 29374985
infants with intrauterine growth restriction had higher serum levels of IGF2 if they had the A/G genotype at the ApaI restriction fragment length polymorphism and higher values of IGF2R if they had the A/A genotype PMID: 28460554
Upregulation of IGF-II expression is associated with ovarian cancer. PMID: 28829218
Data suggest that high IGF2 DMR methylation status would be a phenomenon that is observed with the progression of gastric cancer (GC) toward more aggressive features, supporting their potential utility as a biomarker in GC patients. PMID: 28871451
Data suggest that expression of CDKN1C and IGF2 is significantly up-regulated in placenta after assisted reproductive technology; DNA methylation was significantly down-regulated in DMR of CDKN1C and up-regulated in DMR of IGF2. (CDKN1C = cyclin-dependent kinase inhibitor-1C; IGF2 = insulin like growth factor 2; DMR = differential methylation regions) PMID: 29277274
The expression of miR-3941 was significantly down-regulated in acute pneumonia; IGF2 was confirmed as a direct target gene of miR-3941. PMID: 29328418
Our data reveal that vigilin is essential for maintenance of imprinting of IGF2 gene via functional interaction between KH1-7 domains of vigilin and zinc-finger domains of CTCF. PMID: 29157910
Low IGF-II serum levels were associated with Pancreatic Cancer. PMID: 28681154
Rapamycin-independent IGF2 expression in Tsc2-null mouse embryo fibroblasts and human lymphangioleiomyomatosis cells. PMID: 29758070
IGF2 rs680 polymorphism may have a role in endurance among Israeli athletes PMID: 29107196
low methylation of the Igf2 gene promoter region may promote the expression of Igf2 and miR4835p; this, in turn, induces the degradation of miR4835p target genes, and leads to the upregulation of oncogenes and the downregulation of tumor suppressors, which promotes the development of ESCC. PMID: 29207103
Results found IGF2 as a direct target gene of miR615 and restoring its expression reverses the inhibitory effects of miR615 in human esophageal squamous cell carcinoma cell motility. PMID: 29115555
A common indel variant in the 3'UTR of the IGF2 gene was associated with the risk of impaired renal function in an elderly population. PMID: 29889555
High molecular weight IGF-2 was associated with hypoglycemia in Recurrent Renal Cell Carcinoma. PMID: 24711554
Impairment of IGF2 gene expression in prostate cancer is triggered by epigenetic dysregulation of IGF2-DMR0 and its interaction with KLF4 PMID: 29017567
HMGA1P7 mRNA sustains the H19 and Igf2 overexpression by acting as miRNA decoy. PMID: 27874091
Data suggest that blocking insulin-like growth factor 2 (IGF2) is a potential therapeutic mechanism for hepatocellular carcinoma (HCC). PMID: 29413895
IGF2 expression varies among mesenchymal stem cells derived from amniotic fluid, amnion, endometrium, and Wharton's jelly during culture period. PMID: 28629288
Results showed that IGF-2 was persistently expressed in oculomotor neurons in health and amyotrophic lateral sclerosis (ALS) and thus could play a role in oculomotor resistance in this disease. PMID: 27180807
Studies indicate that miR-663b is epigenetically repressed by long non-coding RNA HOTAIR and exerts its tumor-suppressive function via targeting insulin-like growth factor 2 (IGF2) in pancreatic cancer. PMID: 27895308
IGF-II-mediated loss of E-cadherin is central in developing hepatomegaly in mice and abnormal cell growth in the hepatoma cell line PMID: 27486970
Aberrant IGF2 imprinting may be an intrinsic epigenetic control mechanism that enhances stemness, self-renewal and chemo/radiotherapy resistance in cancer stem cells. PMID: 27275535
DNMT1-mediated transcriptional upregulation of IGF2 is a novel mechanism of resistance to HDIs, highlighting the role of epigenetic deregulation of IGF2 in HDI resistance and the potential value of the H19/IGF2 ICR hypermethylation and DNMT1 expression as predictive biomarkers in HDI-based anticancer therapies. PMID: 27582487
Human H19/Igf2 imprinting control regions can functionally replace mouse H19/Igf2 imprinting control regions on the maternal allele. PMID: 27621468
IGF2 may exert its oncofunction, at least partly, through its parasitic miR-483 which suppressed DLC-1 in colorectal cancer cells. PMID: 27366946
We report here the first deletions of ICR1 associated with hypomethylation of the IGF2/H19 domain leading to SRS. PMID: 27701793
Methylation patterns of IGF2 regulatory regions can discriminate adrenocortical carcinomas from adrenocortical adenomas with high diagnostic accuracy. PMID: 27535174
IGF-II siRNA inactivates the FAK/PI3K/Akt signaling pathway, and further reduces cell proliferation, N-ras and C-myc levels in SMMC-7721 cells. PMID: 27768959
Study shows impact of folic acid intake during pregnancy on genomic imprinting of IGF2/H19 and 1-carbon metabolism PMID: 28778973
produced by pericentral hepatocytes to promote hepatocyte proliferation and repair tissue damage in the setting of chronic liver injury PMID: 28653763
These findings suggest that reducing IGF2 isoform 2 expression in relevant tissues has potential as a new therapeutic strategy for type 2 diabetes, even beyond the Latin American population, with no major adverse effects on health or reproduction. PMID: 28838971
this is the first report of IGF2/H19 domain triplication associated with BWS or SRS and the second report of a maternal amplification of this region in a patient with clinical features of SRS. This study further supports the hypotheses that the amplification of the H19/IGF2 region on the maternal chromosome can lead to an SRS phenotype. PMID: 27612309
stroma-induced IGF2 promotes colon cancer progression in a paracrine and autocrine manner and propose IGF2 as potential target for tumor stroma cotargeting strategies. PMID: 28534511
We identified vascular INSR expression as a potential biomarker for progression in bladder cancer. The data suggest that IGF-2/INSR mediated paracrine crosstalk between bladder cancer cells and endothelial cells is functionally involved in tumour angiogenesis and may thus represent a new therapeutic target. PMID: 28295307
Methylation of IGF2AS is altered 20 years after preterm birth at VLBW. Altered methylation may be a mechanism of later increased disease risk but more data are needed to indicate causality PMID: 23840686
Prenatal 'unhealthy diet' was positively associated with IGF2 methylation at birth, and with ADHD and conduct disorder. PMID: 27535767
High IGF2 expression is associated with breast cancer. PMID: 27546618
IGF2 and insulin receptor A are important for uterine leiomyoma stem cell proliferation and may represent paracrine signaling between leiomyoma cell types. PMID: 28324020
IGF2 overexpression is associated with cancer. PMID: 27869826
Long non-coding RNA 91H is overexpressed in breast cancer and 91H-induced epigenetic modifications on H19/IGF2 locus suggest that 91H may play essential role in breast cancer development. PMID: 27780718
our results suggest that IGF2 via AKT1 contributes to non-canonical wnt signaling. PMID: 26984550
Elevated insulin-like growth factor 2 expression is associated with Beckwith-Wiedemann syndrome. PMID: 27650505
Here we present IGF2, which is re-expressed through epigenetic mechanisms, as the first actionable validated epi-driver in hepatocellular carcinoma. PMID: 27614046
results demonstrate that the H19-Igf2 axis is negatively regulated by CTCF-PHB1 cooperation and that H19 is involved in modulating the growth-suppressive effect of PHB1 in the liver. PMID: 27687727
Compared with obstructive azoospermia (OA) as normal control, our results suggest that miR-210 was significantly up-regulated in testis of patients with non-obstructive azoospermia (P<0.05), and IGF2 was down-regulated, but without a significant difference. PMID: 27535712
The identification of the INS-IGF2 read-through transcript specifically in tumor tissue but not in normal pancreatic tissue suggests that high expression of INS-IGF2 could be neoplasiaspecific PMID: 27667266
DNA methylation of imprinted loci of IGF2 is not affected in Parkinson's disease patients. PMID: 28081695

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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.