Goat Anti-SNX9 Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q9Y5X1 |
Other Accession | NP_057308, 51429 |
Reactivity | Human |
Predicted | Mouse, Dog |
Host | Goat |
Clonality | Polyclonal |
Concentration | 0.5 mg/ml |
Isotype | IgG |
Calculated MW | 66592 Da |
Gene ID | 51429 |
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Other Names | Sorting nexin-9, SH3 and PX domain-containing protein 1, Protein SDP1, SH3 and PX domain-containing protein 3A, SNX9, SH3PX1, SH3PXD3A |
Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Goat Anti-SNX9 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SNX9 |
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Synonyms | SH3PX1, SH3PXD3A |
Function | Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin- independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3- phosphate. |
Cellular Location | Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network. Cell projection, ruffle. Cytoplasm Note=Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Transiently recruited to clathrin- coated pits at a late stage of clathrin-coated vesicle formation Colocalizes with the actin cytoskeleton at the cell membrane |
Tissue Location | Widely expressed, with highest levels in heart and placenta, and lowest levels in thymus and peripheral blood leukocytes |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein does not contain a coiled coil region, like some family members, but does contain a SH3 domain near its N-terminus. This protein interacts with the cytoplasmic domains of the precursor but not the processed forms of a disintegrin and metalloprotease domain 9 and 15. This protein binds the beta-appendage domain of adaptor protein 2 and may function to assist adaptor protein 2 in its role at the plasma membrane. This protein interacts with activated Cdc42-associated kinase-2 to regulate the degradation of epidermal growth factor receptor protein.
References
The E3 ubiquitin ligase Itch regulates sorting nexin 9 through an unconventional substrate recognition domain. Baumann C, et al. FEBS J, 2010 Jul. PMID 20491914.
Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score. Rose JE, et al. Mol Med, 2010 Jul-Aug. PMID 20379614.
Mechanism of aldolase control of sorting nexin 9 function in endocytosis. Rangarajan ES, et al. J Biol Chem, 2010 Apr 16. PMID 20129922.
Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening. Voss M, et al. BMC Immunol, 2009 Oct 6. PMID 19807924.
Structure and plasticity of Endophilin and Sorting Nexin 9. Wang Q, et al. Structure, 2008 Oct 8. PMID 18940612.
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