This rabbit IgG polyclonal antibody was generated against amino acids 6-595 of SNX9 (SH3PX1) and is specific for mouse SNX9.
Sorting nexin (SNX) proteins are members of a large family of hydrophilic PX (phospholipid-binding motif) domain-containing proteins that interact with a variety of receptor types. The ability of SNXs to bind specific phospholipids, as well as their tendency to form protein-protein complexes, suggests a role for these proteins in cellular membrane trafficking and protein sorting.
Sorting nexin-9 (SNX9, or SH3PX1) binds to the cytoplasmic domain of ADAMs9 and 15 and to the Cdc42-associated kinase to regulate the degradation of epidermal growth factor receptor protein.
From the laboratory of Carl P. Blobel, MD, PhD, Hospital for Special Surgery.
Part of The Investigator's Annexe program.
Product Type: | Antibody |
Antigen: | SNX9 |
Accession ID: | Q9Y5X1 |
Isotype: | IgG |
Clonality: | Polyclonal |
Reactivity: | Mouse |
Immunogen: | GST fusion protein with amino acids 6-595 of SNX9 |
Species Immunized: | Rabbit |
Purification Method: | Serum, not purified |
Tested Applications: | WB (1:1000) |
Storage: | -80C |
Shipped: | Dry ice |
Antibody | Species Reactivity | Specificity |
ADAM9 | Human | Cytoplasmic Domain |
ADAM9 | Mouse | Cytoplasmic Domain |
ADAM12 | Mouse | Cytoplasmic Domain |
ADAM15 | Human | Cytoplasmic Domain |
ADAM15 | Mouse | Cytoplasmic Domain |
ADAM15 | Human | Extracellular Domain |
ADAM15 | Mouse | Disintegrin Domain |
ADAM17 | Mouse | Cytoplasmic Domain |
ADAM17 | Mouse | Pro domain |
ADAM19 | Mouse | Cytoplasmic Domain |
ADAM28 | Mouse | Cytoplasmic Domain |
ADAM28 | Mouse | Extracellular Domain |
SNX9 | Mouse | Cytoplasmic Domain |
Western Blot Analysis
A Western blot analysis of cell lysates from transformed primary human embryonal kidney cells (293), HeLa cells, control transfected COS-7 cells, or COS-7 cells transfected with full-length SNX9 (SH3PX1). Blots were probed with rabbit polyclonal SNX9 Antibody or with a preimmune antiserum.
Adapted from: Howard L, et al. Biochem J. 2000, 348, 21-27.
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