IGFBP2 Protein (AA 35-305, N-Term)
Quick Overview for IGFBP2 Protein (AA 35-305, N-Term) (ABIN2666958)
Target
See all IGFBP2 ProteinsProtein Type
Biological Activity
Origin
Source
Application
Purity
-
-
Protein Characteristics
- AA 35-305, N-Term
-
Sterility
- 0.22 μm filtered
-
Endotoxin Level
-
Less than 0.01 ng per μg cytokine as determined by the LAL method.
-
-
Want other Options for this Protein ?
!Discover Our Predefined Custom Proteins and Custom Protein Services!Your project requires further customization? Contact us and discover our custom protein solutions
-
-
-
Application Notes
- Optimal working dilution should be determined by the investigator.
-
Comment
-
Biological activity: ED50 = 0.03 - 0.18 μg/mL as determined by the inhibition of MCF-7 cell proliferation induced by mouse IGF-II (18 ng/mL).
-
Restrictions
- For Research Use only
-
-
-
Format
- Liquid
-
Reconstitution
- For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20 °C to -70 °C. Stock solutions can also be prepared at 50 - 100 μg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 0.2 - 1 % BSA or HSA and stored in working aliquots at -20 °C to -70 °C.
-
Buffer
- 0.22 μm filtered protein solution is < 30 % ACN and 0.1 % TFA.
-
Handling Advice
- Avoid repeated freeze/thaw cycles.
-
Storage
- -20 °C
-
Storage Comment
- Unopened vial can be stored between 2°C and 8°C for three months, at -20°C for six months, or at -70°C for one year.
-
-
- IGFBP2 (Insulin-Like Growth Factor Binding Protein 2, 36kDa (IGFBP2))
-
Alternative Name
- IGFBP-2
-
Background
- 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 carboxi-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.
-
Molecular Weight
- The 292 amino acid recombinant protein has a predicted molecular mass of approximately 31.7 kDa. The protein migrates approximately at 40 kDa in DTT-reducing conditions and 43 kDa in non-reducing conditions by SDS-PAGE. The predicted N-terminal amino acid
-
Pathways
- Myometrial Relaxation and Contraction, Growth Factor Binding, Activated T Cell Proliferation
Target
-