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Mouse Anti-IGF2 Recombinant Antibody (CBYY-I1092) (CBMAB-I2260-YY)

This product is Mouse antibody that recognizes IGF2. The antibody CBYY-I1092 can be used for immunoassay techniques such as: WB
See all IGF2 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYY-I1092
Antibody Isotype
IgG2
Application
WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Lyophilized
Buffer
0.2μm filtered solution in PBS
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Insulin Like Growth Factor 2
Introduction
This gene encodes a member of the insulin family of polypeptide growth factors, which are involved in development and growth. It is an imprinted gene, expressed only from the paternal allele, and epigenetic changes at this locus are associated with Wilms tumour, Beckwith-Wiedemann syndrome, rhabdomyosarcoma, and Silver-Russell syndrome. A read-through INS-IGF2 gene exists, whose 5' region overlaps the INS gene and the 3' region overlaps this gene. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Entrez Gene ID
3481
UniProt ID
P01344
Alternative Names
Insulin Like Growth Factor 2
Function
The insulin-like growth factors possess growth-promoting activity (By similarity).

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 (PubMed:28873464).

Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity).

Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate (By similarity).

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.
Biological Process
Animal organ morphogenesis Source: Ensembl
Embryonic placenta development Source: UniProtKB
Embryonic placenta morphogenesis Source: UniProtKB
Exocrine pancreas development Source: Ensembl
Glucose metabolic process Source: UniProtKB-KW
Insulin receptor signaling pathway Source: ProtInc
Insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: BHF-UCL
In utero embryonic development Source: UniProtKB
Negative regulation of muscle cell differentiation Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Osteoblast differentiation Source: Ensembl
Positive regulation of activated T cell proliferation Source: BHF-UCL
Positive regulation of catalytic activity Source: BHF-UCL
Positive regulation of cell division Source: UniProtKB-KW
Positive regulation of cell population proliferation Source: UniProtKB
Positive regulation of glycogen (starch) synthase activity Source: BHF-UCL
Positive regulation of glycogen biosynthetic process Source: BHF-UCL
Positive regulation of insulin receptor signaling pathway Source: BHF-UCL
Positive regulation of MAPK cascade Source: BHF-UCL
Positive regulation of mitotic nuclear division Source: BHF-UCL
Positive regulation of multicellular organism growth Source: Ensembl
Positive regulation of organ growth Source: Ensembl
Positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
Positive regulation of protein kinase B signaling Source: BHF-UCL
Positive regulation of protein phosphorylation Source: BHF-UCL
Positive regulation of skeletal muscle tissue growth Source: Ensembl
Positive regulation of transcription by RNA polymerase II Source: GO_Central
Positive regulation of vascular endothelial cell proliferation Source: GO_Central
Regulation of gene expression by genetic imprinting Source: ProtInc
Regulation of histone modification Source: UniProtKB
Regulation of muscle cell differentiation Source: UniProtKB
Regulation of transcription, DNA-templated Source: BHF-UCL
Spongiotrophoblast cell proliferation Source: Ensembl
Striated muscle cell differentiation Source: Ensembl
Cellular Location
Secreted
Involvement in disease
Silver-Russell syndrome 1 (SRS1):
A form of Silver-Russell syndrome, a clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age. SRS1 is caused by epigenetic changes of DNA hypomethylation at the telomeric imprinting control region (ICR1) on chromosome 11p15, involving the H19 and IGF2 genes.
Silver-Russell syndrome 3 (SRS3):
A form of Silver-Russell syndrome, a clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age. SRS3 inheritance is autosomal dominant.
PTM
O-glycosylated with core 1 or possibly core 8 glycans. Thr-96 is a minor glycosylation site compared to Thr-99.
Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128 and Arg-92 to generate big-IGF2 and mature IGF2.

Fernández-Pereira, C., Penedo, M. A., Rivera-Baltanas, T., Fernández-Martínez, R., Ortolano, S., Olivares, J. M., & Agís-Balboa, R. C. (2022). Insulin-like Growth Factor 2 (IGF-2) and Insulin-like Growth Factor Binding Protein 7 (IGFBP-7) Are Upregulated after Atypical Antipsychotics in Spanish Schizophrenia Patients. International Journal of Molecular Sciences, 23(17), 9591.

Cao, J., Yan, W., Ma, X., Huang, H., & Yan, H. (2021). Insulin-like growth factor 2 mRNA-binding protein 2—A potential link between type 2 diabetes mellitus and cancer. The journal of clinical endocrinology & metabolism, 106(10), 2807-2818.

Jin, Y., Kotler, J. L., Wang, S., Huang, B., Halpin, J. C., & Street, T. O. (2021). The ER chaperones BiP and Grp94 regulate the formation of insulin-like growth factor 2 (IGF2) oligomers. Journal of molecular biology, 433(13), 166963.

Vafaee, F., Zarifkar, A., Emamghoreishi, M., Namavar, M. R., Shirzad, S., Ghazavi, H., & Mahdavizadeh, V. (2020). Insulin-like growth factor 2 (IGF-2) regulates neuronal density and IGF-2 distribution following hippocampal intracerebral hemorrhage. Journal of Stroke and Cerebrovascular Diseases, 29(10), 105128.

García-Huerta, P., Troncoso-Escudero, P., Wu, D., Thiruvalluvan, A., Cisternas-Olmedo, M., Henríquez, D. R., ... & Hetz, C. (2020). Insulin-like growth factor 2 (IGF2) protects against Huntington’s disease through the extracellular disposal of protein aggregates. Acta neuropathologica, 140, 737-764.

van Doorn, J. (2020). Insulin‐like growth factor‐II and bioactive proteins containing a part of the E‐domain of pro‐insulin‐like growth factor‐II. Biofactors, 46(4), 563-578.

Yang, Y. J., Luo, T., Zhao, Y., Jiang, S. Z., Xiong, J. W., Zhan, J. Q., ... & Wei, B. (2020). Altered insulin-like growth factor-2 signaling is associated with psychopathology and cognitive deficits in patients with schizophrenia. PLoS One, 15(3), e0226688.

Kasprzak, A., & Adamek, A. (2019). Insulin-like growth factor 2 (IGF2) signaling in colorectal cancer—from basic research to potential clinical applications. International journal of molecular sciences, 20(19), 4915.

Rotwein, P. (2018). The complex genetics of human insulin-like growth factor 2 are not reflected in public databases. Journal of Biological Chemistry, 293(12), 4324-4333.

Cao, J., Mu, Q., & Huang, H. (2018). The roles of insulin-like growth factor 2 mRNA-binding protein 2 in cancer and cancer stem cells. Stem cells international, 2018.

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For research use only. Not intended for any clinical use.

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