Detects human IGFBP-5 in direct ELISAs and Western blots. In direct ELISAs, less than 25% cross-reactivity with recombinant mouse IGFBP-5 is observed and less than 5% cross-reactivity with recombinant human (rh) IGFBP-1, rhIGFBP-2, rhIGFBP-3, rhIGFBP-4, rhIGFBP-6, and rhIGFBP-7 is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human IGFBP-5 Glu28-Glu272 Accession # P24593
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
IGFBP‑5 was detected in immersion fixed paraffin-embedded sections of human placenta using Goat Anti-Human IGFBP‑5 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF875) at 1.7 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to syncytiotrophoblasts. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
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.
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-transitional modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Human IGFBP-5 cDNA encodes a 272 amino acid (aa) residue precursor protein with a putative 20 aa residue signal peptide that is processed to generate the 252 aa residue mature protein that is post-translationally modified by O-glycosylations and serine phosphorylations. IGFBP-5 is expressed by fibroblasts, myoblasts and osteoblasts, making it the predominant IGFBP found in bone extracts. IGFBP-5 has a strong affinity for hydroxyapatite, allowing it to bind to bone cells. When bound to extracellular matrix, IGFBP-5 is protected from proteolysis and potentiates IGF activity, but when it is soluble, IGFBP-5 is cleaved to a biologically inactive 21 kDa fragment (1, 2).
Jones, J.I. and D.R. Clemmons (1995) Endocrine Rev. 16:3.
Kelley, K.M. et al. (1996) Int. J. Biochem. Cell Biol. 28:619.
Insulin-like Growth Factor Binding Protein 5
Entrez Gene IDs:
3488 (Human); 16011 (Mouse)
IBP5IBP-5; IGF-binding protein 5; IGFBP5; IGFBP-5; insulin-like growth factor binding protein 5; insulin-like growth factor-binding protein 5
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The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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