Detects rat GFR alpha ‑1/GDNF R alpha ‑1 in direct ELISAs and Western blots. In direct ELISAs, no cross-reactivity with recombinant mouse (rm) Ret, recombinant human (rh) GFR alpha -2, rhGFR alpha -3 or rmGFR alpha -2 is observed.
Monoclonal Mouse IgG2B Clone # 81401
Protein A or G purified from ascites
Mouse myeloma cell line NS0-derived recombinant rat GFR alpha ‑1/GDNF R alpha ‑1 Asp25-Leu445 Accession # Q62997
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.
Detection of Rat GFR alpha ‑1/GDNF R alpha ‑1 by Western Blot.
Western blot shows lysates of rat spinal cord tissue and rat kidney tissue. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Rat GFR alpha ‑1/GDNF R alpha ‑1 Monoclonal Antibody (Catalog # MAB560) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for GFR alpha ‑1/GDNF R alpha ‑1 at approximately 60 kDa (as indicated). This experiment was conducted under non-reducing conditions (recommended) and using Immunoblot Buffer Group 1.
GFR alpha ‑1/GDNF R alpha ‑1 in Rat Spinal Cord.
GFR alpha ‑1/GDNF R alpha ‑1 was detected in perfusion fixed frozen sections of rat spinal cord using Rat GFR alpha ‑1/GDNF R alpha ‑1 Monoclonal Antibody (Catalog # MAB560) at 25 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Specific staining was localized to the dorsal horn. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
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.
Background: GFR alpha-1/GDNF R alpha-1
Glial cell line-derived growth factor (GDNF), neurturin (NTN) and persephin, distant members of the TGF-beta superfamily, are neurotrophic factors for a variety of neuronal populations in the central and peripheral nervous systems. The bioactivities of GDNF and NTN are mediated through a receptor complex composed of the non ligand-binding signaling subunit (c-Ret receptor tyrosine kinase) and either of two ligand binding subunits (GDNF receptor alpha - (GFR alpha -1) or GFR alpha -2). GFR alpha -1 and -2 are members of a family of at least four cysteine-rich glycosyl-phosphatidylinositol (GPI)-linked cell surface proteins that share conserved placements of many of their cysteine residues. Binding of GDNF to membrane-associated GFR alpha -1 or GFR alpha -2 initiates the association with and activation of the Ret tyrosine kinase. Soluble GFR alpha s released enzymatically from the cell surface-associated protein with phosphatidylinositol phospholipase C, as well as recombinantly produced soluble GFR alpha -1, can also bind with high-affinity to GDNF and trigger the activation of Ret tyrosine kinase. Rat GFR alpha -1 cDNA encodes a 468 amino acid (aa) residue protein with an N‑terminal 24 aa residue hydrophobic signal peptide. Like other GPI-linked proteins, rat GFR alpha -1 has a C-terminal hydrophobic region which is preceded by a three aa residue (ASS) GPI-binding site. Human GFR alpha -1 shares 93% amino acid identity with rat GFR alpha -1. The expression of the various GFR alpha s are differentially regulated in the central and peripheral nervous system, suggesting complementary roles for the GFR alpha s in mediating the activities of the GDNF family of neurotrophic factors.
Thompson, J. et al. (1998) Mol. Cell Neurosci. 11:117.
Trupp, M. et al. (1998) Mol. Cell Neurosci. 11:47.
Baloh, R.H. et al. (1998) Proc. Natl. Acad. Sci. USA 95:5801.
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