Mouse IGFBP-2 Antibody

Catalog # Availability Size / Price Qty
MAB797
MAB797-SP
IGFBP‑2 Inhibition of IGF‑II-dependent Cell Proliferation and Neutralization by Mouse IGFBP‑2 Antibody.
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Product Details
Citations (3)
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Mouse IGFBP-2 Antibody Summary

Species Reactivity
Mouse
Specificity
Detects mouse IGFBP-2 in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant human IGFBP-1, -2, -3, -4, -5, -6, recombinant mouse (rm) IGFBP-1, -3, -5, or -6 is observed. In direct ELISAs, no cross-reactivity with rmIGFBP-4 is observed.
Source
Monoclonal Rat IgG2A Clone # 150101
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse IGFBP‑2
Glu35-Gln305
Accession # CAA57270
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Endotoxin Level
<0.10 EU per 1 μg of the antibody by the LAL method.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
1 µg/mL
Recombinant Mouse IGFBP‑2 (Catalog # 797-B2) under non-reducing conditions only
Neutralization
Measured by its ability to neutralize IGFBP‑2 inhibition of IGF‑II-dependent proliferation in the MCF‑7 human breast cancer cell line. Karey, K. P. et al. (1988) Cancer Research 48:4083. The Neutralization Dose (ND50) is typically 5‑20 µg/mL in the presence of 0.75 µg/mL Recombinant Mouse IGFBP‑2 and 30 ng/mL Recombinant Mouse IGF‑II.

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Neutralization IGFBP‑2 Inhibition of IGF‑II-dependent Cell Proliferation and Neutralization by Mouse IGFBP‑2 Antibody. View Larger

IGFBP‑2 Inhibition of IGF‑II-dependent Cell Proliferation and Neutralization by Mouse IGFBP‑2 Antibody. Recombinant Mouse IGFBP-2 (Catalog # 797-B2) inhibits Recombinant Mouse IGF-II (Catalog # 792-MG) induced proliferation in the MCF-7 human breast cancer cell line in a dose-dependent manner (orange line). Inhibition of Recombinant Mouse IGF-II (30 ng/mL) activity elicited by Recombinant Mouse IGFBP-2 (0.75 µg/mL) is neutralized (green line) by increasing concentrations of Rat Anti-Mouse IGFBP-2 Monoclonal Antibody (Catalog # MAB797). The ND50 is typically 5-20 µg/mL.

Preparation and Storage

Reconstitution
Reconstitute at 0.5 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: IGFBP-2

The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and at least four additional low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-translational modifications of IGFBPs, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF. Mouse IGFBP-2 cDNA encodes a 305 amino acid (aa) precursor protein with a 34 aa residue signal peptide and a 271 aa mature protein. Mouse and human IGFBP-2 share approximately 82% aa identity. IGFBP-2 contains an integrin receptor recognition sequence (RGD sequence) but lacks potential N-linked glycosylation sites. During development, IGFBP-2 is expressed in a number of tissues. The highest expression level is found in the central nervous system. In adults, high expression levels are also detected in the central nervous system and in a number of reproductive tissues. IGFBP-2 binds preferentially to IGF-II, exhibiting a 2-10 fold higher affinity for IGF-II than for IGF-I.

References
  1. Jones, J.I. and D.R. Clemmons (1995) Endocrine Rev. 16:3.
  2. Kelley, K.M. et al. (1996) Int. J. Biochem. Cell Biol. 28:619.
  3. Schuller, A.G.P. et al. (1994) Mol. Cell. Endoc. 104:57.
  4. Landwehr, J. et al. (1993) Gene 124:281.
Long Name
Insulin-like Growth Factor Binding Protein 2
Entrez Gene IDs
3485 (Human); 16008 (Mouse)
Alternate Names
BP2; IBP2; IBP-2; IGF-binding protein 2; IGFBP2; IGFBP-2; IGF-BP53; insulin-like growth factor binding protein 2 (36kD); insulin-like growth factor binding protein 2, 36kDa; insulin-like growth factor-binding protein 2

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Citations for Mouse IGFBP-2 Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. Aberrant astrocyte protein secretion contributes to altered neuronal development in multiple models of neurodevelopmental disorders
    Authors: ALM Caldwell, L Sancho, J Deng, A Bosworth, A Miglietta, JK Diedrich, MN Shokhirev, NJ Allen
    Nature Neuroscience, 2022-08-30;25(9):1163-1178.
    Species: Mouse
    Sample Types: In Vivo, Whole Cells
    Applications: IHC, Neutralization
  2. Patched1 inhibits epidermal progenitor cell expansion and basal cell carcinoma formation by limiting Igfbp2 activity.
    Authors: Villani RM, Adolphe C, Palmer J, Waters MJ, Wainwright BJ
    Cancer Prev Res (Phila), 2010-09-21;3(10):1222-34.
    Species: Mouse
    Sample Types: Whole Tissue
    Applications: Neutralization
  3. The lysosomal trafficking regulator is necessary for normal wound healing
    Authors: Jacob C. Zbinden, Gabriel J. M. Mirhaidari, Kevin M. Blum, Andrew J. Musgrave, James W. Reinhardt, Christopher K. Breuer et al.
    Wound Repair and Regeneration

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