IGFBP2 Mouse
HEK293 cells.
IBP-2, IGF-binding protein 2, IGFBP-2, mIGFBP-2, Igfbp-2, insulin-like growth factor binding protein 2 isoform 1, insulin-like growth factor binding protein 2.
Sterile Filtered colorless solution.
Greater than 85.0% as determined by SDS-PAGE.
Description
IGFBP2 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 35-305) containing 277 amino acids and having a molecular mass of 30.3kDa. IGFBP2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
IBP-2, IGF-binding protein 2, IGFBP-2, mIGFBP-2, Igfbp-2, insulin-like growth factor binding protein 2 isoform 1, insulin-like growth factor binding protein 2.
HEK293 cells.
EVLFRCPPCT PERLAACGPP PDAPCAELVR EPGCGCCSVC ARQEGEACGV YIPRCAQTLR CYPNPGSELP LKALVTGAGT CEKRRVGTTP QQVADSDDDH SEGGLVENHV DGTMNMLGGG SSAGRKPLKS GMKELAVFRE KVNEQHRQMG KGAKHLSLEE PKKLRPPPAR TPCQQELDQV LERISTMRLP DDRGPLEHLY SLHIPNCDKH GRYNLKQCKM SLNGQRGECW CVNPNTGKPI QGAPTIRGDP ECHLFYNEQQ ETGGAHAQSV QHHHHHH.
Product Science Overview
Insulin-Like Growth Factor Binding Protein-2 (IGFBP-2) is a member of the insulin-like growth factor binding protein family, which plays a crucial role in modulating the activity of insulin-like growth factors (IGFs). IGFBP-2 is known for its high affinity for IGF-I and IGF-II, which are essential for cell growth, development, and metabolism. The recombinant form of IGFBP-2 derived from mice is widely used in research to study its biological functions and potential therapeutic applications.
IGFBP-2 is a glycoprotein consisting of approximately 328 amino acids. It contains three distinct domains: the N-terminal domain, the central domain, and the C-terminal domain. Each domain contributes to the protein’s ability to bind IGFs and modulate their activity. The N-terminal domain is responsible for high-affinity binding to IGFs, while the central domain contains a nuclear localization signal that allows IGFBP-2 to enter the nucleus and influence gene expression. The C-terminal domain is involved in interactions with cell surface receptors and extracellular matrix components.
IGFBP-2 plays a multifaceted role in regulating IGF activity. By binding to IGFs, IGFBP-2 can inhibit their interaction with IGF receptors, thereby modulating their mitogenic and metabolic effects. Additionally, IGFBP-2 can enhance IGF activity by protecting IGFs from degradation and extending their half-life in circulation. Beyond its role in IGF regulation, IGFBP-2 has been implicated in various cellular processes, including cell migration, invasion, and angiogenesis. It is also involved in the regulation of glucose metabolism and has been linked to metabolic disorders such as diabetes.
The recombinant form of IGFBP-2 (Mouse) is typically produced using recombinant DNA technology. The gene encoding IGFBP-2 is cloned into an expression vector, which is then introduced into a suitable host cell line, such as Escherichia coli or Chinese hamster ovary (CHO) cells. The host cells are cultured under optimal conditions to express the recombinant protein, which is subsequently purified using techniques such as affinity chromatography and gel filtration. The purified recombinant IGFBP-2 is then characterized to ensure its structural and functional integrity.
Recombinant IGFBP-2 (Mouse) is widely used in research to investigate its biological functions and potential therapeutic applications. It is employed in studies exploring the role of IGFBP-2 in cancer, where it has been shown to influence tumor growth, metastasis, and response to therapy. Additionally, IGFBP-2 is used in research on metabolic disorders, such as diabetes and obesity, to understand its impact on glucose metabolism and insulin sensitivity. The protein is also utilized in studies examining its role in cardiovascular diseases, neurodegenerative disorders, and tissue regeneration.
