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IGFBP2 Protein (AA 35-305, N-Term)

This Recombinant IGFBP2 protein is produced in HEK-293 Cells.
Catalog No. ABIN2666958
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Quick Overview for IGFBP2 Protein (AA 35-305, N-Term) (ABIN2666958)

Target

See all IGFBP2 Proteins
IGFBP2 (Insulin-Like Growth Factor Binding Protein 2, 36kDa (IGFBP2))

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 12
  • 7
  • 3
  • 3
  • 3
  • 2
  • 2
  • 1
  • 1
  • 1
Mouse

Source

  • 13
  • 8
  • 7
  • 3
  • 1
  • 1
  • 1
  • 1
HEK-293 Cells

Application

Flow Cytometry (FACS)

Purity

> 95 % , as determined by Coomassie stained SDS-PAGE.
  • 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.

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  • 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.
  • Target

    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
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