Recombinant Bovine Insulin-Like Growth Factor Ii (IGF2) Protein (His&Myc)

Name: Recombinant Bovine Insulin-Like Growth Factor Ii (IGF2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07385P
Availability: InStock

Greater than 90% 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 Bovine Insulin-Like Growth Factor Ii (IGF2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P07456
Target Symbol	IGF2
Species	Bos taurus (Bovine)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	AYRPSETLCGGELVDTLQFVCGDRGFYFSRPSSRINRRSRGIVEECCFRSCDLALLETYCATPAKSE
Expression Range	25-91aa
Protein Length	Full Length of Mature Protein
Mol. Weight	15.0 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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. 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	KEGG: bta:281240 STRING: 9913.ENSBTAP00000017372 UniGene: Bt.106739

Gene Functions References

Methylation pattern in a CpG island of the IGF2 gene in cumulus cells from 1-3 mm and >/= 8.0 mm follicles and the effects of in vitro maturation on this pattern. PMID: 24174298
Our results provide evidence that polymorphisms in the IGF2 gene are associated with growth traits, and may be used for marker-assisted selection in beef cattle breeding program PMID: 24374893
The identification of the polymorphisms in the IGF2 gene that were significantly associated with growth traits in cattle. PMID: 23957672
Polymorphisms in the IGF2 gene are associated with cattle growth traits. PMID: 23900197
The LEP, IGF2 and CCL2 genes showed allelic expression imbalance in liver, kidney and pituitary glands of Polish Holstein-Friesian bulls. PMID: 23184004
Sex-sorting procedure by flow cytometry did not affect the overall DNA methylation patterns of the IGF2 and IGF2R genes, although individual variation in their methylation patterns among bulls was observed. PMID: 22128039
The reduction in IGFs mRNA level after 5 days of life in the duodenum (IGF-1 and IGF-2) and in the jejunum (IGF-1) was associated with reduction in villi length (duodenum and jejunum) and the increase of crypt depth (duodenum). PMID: 22439332
Changes in the methylation pattern of IGF2 during in vitro maturation were different between incompetent and competent oocytes, and this characteristic may be useful as a molecular marker in studies of oocyte competence in cattle. PMID: 20833870
Data describes the long-term changes to skeletal muscle growth and IGF1, 2, 1R, and 2R mRNA expression in progeny after exposure to high and low levels of maternal nutrient intake during the first two trimesters of gestation in the bovine. PMID: 21056085
findings support work which suggests that the insulin-like growth factor 2 locus is an important biological regulator of milk production in dairy cattle PMID: 20822563
effects of insulin, IGF-I and IGF-II on apoptosis and cell proliferation in bovine blastocysts in vitro PMID: 12112582
IGF2 is subjected to extensive transcriptional regulation through multiple promoters, alternative splicing and polyadenylation, as well as genetic imprinting.IGF2 regulation is age-, tissue-, promoter-, and allele-specific PMID: 16120826
Identification of a previously unknown differentially methylated region in exon 10 of the bovine IGF2 gene. PMID: 16644179
Indel polymorphism associated with breeding value in bulls. PMID: 17242995
The role of insulin-like growth factor 2 (IGF2) and the regulation of the IGF2 receptor (IGF2R) during follicular development were studied. PMID: 17360960
Embryonic tissues from NT-derived embryos had higher expression of IGF-II mRNA than in vitro production embryonic tissues. PMID: 17628655
The effect of single nucleotide polymorphisms in 6 genes and their associations with production factors in beef cattle are reported. PMID: 17785604
study to assess the mRNA expression of IGF-I, IGF-II, IGF-IR and IGF-IIR in bovine oocytes and different stages of preimplantation embryos PMID: 19013732
Dats detected that SNPs of IGF2 gene has close relationship with carcass and meat quality traits in Qinchuan cattle PMID: 19073573
Hypomethylation trends in the intergenic region of the imprinted IGF2 and H19 genes in cloned cattle. PMID: 19282114
Among embryos developing in vivo, the level of DNA methylation in the IGF2 intragenic DMR was significantly lower in female than in male blastocysts PMID: 19341790

FAQs

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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.