Sf9, Insect cells.
Insulin-like growth factor-binding protein 4, IBP-4, IGF-binding protein 4, IGFBP-4, IGFBP4, IBP4, BP-4, HT29-IGFBP.
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Insulin Like Growth Factor Binding Protein-4 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 237 amino acids and having a molecular mass of 30kDa. The IGFBP4 is purified by proprietary chromatographic techniques.
Insulin-like growth factor-binding protein 4 (IGFBP-4) belongs to the insulin-like growth factor binding protein (IGFBP) family. This protein contains an IGFBP domain and a thyroglobulin type-I domain. IGFBP-4 can bind to both insulin-like growth factors (IGFs) I and II. It circulates in the plasma in both glycosylated and non-glycosylated forms. IGFBPs exhibit various functions, including inhibiting or enhancing the biological activities of IGF or acting independently of IGF. IGFBP-4 has shown consistent inhibitory effects on various cancer cells both in vivo and in vitro, suggesting its potential role as an apoptotic factor. Notably, IGFBP4 is produced by all colon cancer cells. Its binding to IGFs prolongs their half-life and alters their interaction with cell surface receptors.
Recombinant Human Insulin Like Growth Factor Binding Protein-4, produced in Sf9 Insect cells, is a single, glycosylated polypeptide chain. It comprises 237 amino acids, resulting in a molecular mass of 30kDa. The purification of IGFBP4 is achieved using proprietary chromatographic techniques.
Sterile Filtered White lyophilized (freeze-dried) powder.
The protein is lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.0 and 150mM NaCl.
To reconstitute the lyophilized Insulin Like Growth Factor Binding Protein-4, it is recommended to dissolve it in sterile 18MΩ-cm H2O to a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Lyophilized IGFBP4 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated below -18°C. Once reconstituted, Insulin Like Growth Factor Binding Protein-4 should be stored at 4°C for 2-7 days. For extended storage, it should be kept at -18°C. Repeated freeze-thaw cycles should be avoided.
The purity of the protein is greater than 97.0%, as determined by the following methods:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
The ED50, which represents the protein's ability to inhibit IGF-II induced proliferation of MCF-7 cells, is determined to be less than 0.1 µg/ml. This corresponds to a specific activity of greater than 1.0 × 104 IU/mg in the presence of 14 ng/ml of recombinant human IGF-II.
Insulin-like growth factor-binding protein 4, IBP-4, IGF-binding protein 4, IGFBP-4, IGFBP4, IBP4, BP-4, HT29-IGFBP.
Sf9, Insect cells.
DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE.
Insulin-Like Growth Factor Binding Protein-4 (IGFBP-4) is a member of the insulin-like growth factor binding protein (IGFBP) family. These proteins play a crucial role in modulating the activity of insulin-like growth factors (IGFs), which are involved in various cellular processes such as proliferation, differentiation, and survival .
IGFBP-4 is a protein that binds both IGF-I and IGF-II, circulating in the plasma in both glycosylated and non-glycosylated forms . The binding of IGFBP-4 to IGFs prolongs their half-life and alters their interaction with cell surface receptors . This protein has an IGFBP domain and a thyroglobulin type-I domain .
IGFBP-4 consistently inhibits IGF-mediated cell proliferation across various cell types tested in vitro . It plays a significant role in regulating the IGF pathway, which is involved in tumor development and progression . The proteolytic cleavage of IGFBP-4 by pregnancy-associated plasma protein-A (PAPP-A) releases active IGF-I, which can then promote cell growth and survival .
Studies have highlighted the therapeutic potential of dBP4 in cancer treatment. For instance, intra-tumor injections of dBP4 in a murine model of breast cancer significantly reduced angiogenesis and metastasis . This suggests that dBP4 could be a promising approach to block the tumor-promoting actions of IGF-I.