- Regulatory Status
- RUO
- Other Names
- Insulin like growth factor-binding protein 2, IGFBP-2, IGF-BP2, IGF-BP53, IBP2, BP2, IBP-2
- Ave. Rating
- Submit a Review
- Product Citations
- publications
Cat # | Size | Price | Quantity Check Availability | Save | ||
---|---|---|---|---|---|---|
793404 | 25 µg | $347 | ||||
793406 | 100 µg | $1026 |
Seven IGFBPs have been described to modulate the IGF activity. IGFBPs transport IGFs, which means they may inhibit mitogenesis, differentiation, survival, and other IGF-stimulated events. IGFBPs are structurally characterized by three domains: the amino-terminal, the carboxy-terminal, and a central L-domain. Members of the IGFBP family exhibit 67 - 70% structural homology. The greatest homology among the IGFBPs is in the N- and C-terminal regions. Some IGFBPs bind to the extracellular matrix (IGFBP-2, IGFBP-3, IGFBP-5, and IGFBP-6). In fact, a heparin-binding domain (HBD) has been identified in the C-terminal region of these binding proteins. In addition to C-terminal HBD, IGFBP-2 contains a HBD located in the linker region. The arginine glycine aspartic acid (RGD) sequence is present in IGFBP-1 and IGFBP-2. This RGD sequence binds to the αVβ1 integrin. IGFBP-2 has a high affinity for IGF-I/IGF-II. It is the second most abundant circulating IGFBP and is expressed in several mammalian tissues. IGFBP-2 and other IGFBPs stimulate biological responses that are independent of their binding to IGFs. IGFBP-2 levels are associated with reduced adipose tissue mass and improved glucose metabolism both in human and mouse models. The HBD of IGFBP-2 has IGF binding-independent biological activity in the growing skeleton. IGFBP-2 mice have impaired bone formation, reduced trabecular bone volume fraction, altered microarchitecture, and low bone turnover. IGFBP-2 is overexpressed in a wide variety of human malignancies, which include glioma, prostate cancer, lung cancer, colorectal cancer, ovarian cancer, adrenocortical tumor, breast cancer, and leukemia.
Product DetailsProduct Details
- Source
- Human IGFBP-2, amino acid (Glu37-Gln325) (Accession: # P18065), with a C-terminal 6His tag, was expressed in CHO cells.
- Molecular Mass
- The 298 amino acid recombinant protein has a predicted molecular mass of approximately 32.4 kD. The DTT-reduced and non-reduced protein migrates at approximately 36 kD by SDS-PAGE. The predicted N-terminal amino acid is Glu.
- Purity
- > 95%, as determined by Coomassie stained SDS-PAGE
- Formulation
- 0.22 µm filtered protein solution is in acetonitrile, trifluoroacetic acid (TFA).
- Endotoxin Level
- Less than 0.1 EU per µg cytokine as determined by the LAL method
- Concentration
- 10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for up to 2 weeks at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2ᵒC and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
- Activity
- Recombinant human IGFBP-2 binds to immobilized human IGF-II at 1 µg/mL in a dose-dependent manner. The ED50 for this effect is 0.01 – 0.05 µg/mL.
- Application
-
Bioassay
- Application Notes
-
BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are validated in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.
Antigen Details
- Structure
- Monomer
- Distribution
-
IGFBP-2 is expressed in a big range of cell types and tissues, preadipocytes, adipocytes, neurons, astrocytes, cancer cells, acute myeloid leukemia cells.
- Function
- IGFBP-2 inhibits the action of IGF-I and IGF-II by preventing their binding to their receptors.
- Interaction
- Binds to extra cellular matrix, αVβ1 integrin, heparin
- Ligand/Receptor
- IGF-I and IGF-II
- Bioactivity
- Human IGFBP-2 binds with high affinity to IGF-II in a dose dependent-manner.
- Cell Type
- Astrocytes, Leukemia, Mesenchymal cells, Neurons
- Biology Area
- Angiogenesis, Cancer Biomarkers, Cell Biology, Cell Proliferation and Viability, Inhibitory Molecules, Neuroscience, Stem Cells
- Molecular Family
- Growth Factors
- Antigen References
-
- Wheatcroft SB, et al. 2007. Diabetes 56:285-94.
- Schutt BS, et al. 2004. J Mol Endocrinol. 32:859-68.
- DeMambro VE, et al. 2008. Endocrinology 149:2051-61.
- Lin Y, et al. 2009. Neuro Oncol. 11:468-76.
- Migita T, et al. 2010. Am J Pathol. 176:1756-66.
- Kawai M, et al. 2011. J Biol Chem. 286:14670-80.
- Chen X, et al., 2013. J Hematol Oncol 6:72.
- Allard JB and Duan C 2018. Front Endocrinol. 9:117.
- Jin L, et al. 2020 Front Oncol. 10:727.
- Gene ID
- 3485 View all products for this Gene ID
- UniProt
- View information about IGFBP-2 on UniProt.org
Related FAQs
- Why choose BioLegend recombinant proteins?
-
• Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
• Greater than 95% Purity or higher, tested on every lot of product.
• 100% Satisfaction Guarantee for quality performance, stability, and consistency.
• Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
• Bulk and customization available. Contact us.
• Learn more about our Recombinant Proteins. - How does the activity of your recombinant proteins compare to competitors?
-
We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
-
The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.
- Have your recombinants been tested for stability?
-
Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- Does specific activity of a recombinant protein vary between lots?
-
Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
-
Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)
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