IGFBP4 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, FC, E |
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Primary Accession | P22692 |
Other Accession | P24854, Q05716 |
Reactivity | Human, Mouse, Rat |
Predicted | Bovine, Pig |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 27934 Da |
Antigen Region | 66-92 aa |
Gene ID | 3487 |
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Other Names | Insulin-like growth factor-binding protein 4, IBP-4, IGF-binding protein 4, IGFBP-4, IGFBP4, IBP4 |
Target/Specificity | This IGFBP4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 66-92 amino acids from the N-terminal region of human IGFBP4. |
Dilution | WB~~1:2000 FC~~1:25 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | IGFBP4 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | IGFBP4 |
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Synonyms | IBP4 |
Function | IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. |
Cellular Location | Secreted. |
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Provided below are standard protocols that you may find useful for product applications.
Background
IGFBP4 has an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma in both glycosylated and non-glycosylated forms. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors.
References
Durai,R., et.al., Colorectal Dis 9 (7), 625-631 (2007)
Laursen,L.S., et.al., Mol. Endocrinol. 21 (5), 1246-1257 (2007)
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