Mitofusin 2 in Mouse Skeletal Muscle.
Mitofusin 2 was detected in perfusion fixed frozen sections of mouse skeletal muscle using Sheep Anti-Human/Mouse/Rat Mitofusin 2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7884) at 1.7 µg/mL overnight at 4 °C. Tissue was stained using the NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (red; Catalog # NL010) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Sterile PBS to a final concentration of 0.2 mg/mL.
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: Mitofusin 2
MFN-2 (Mitofusin 2; also Hypertension-related protein 1, Mitochondrial assembly regulatory factor, HSG protein, and Transmembrane GTPase MFN-2) is an 85‑100 kDa mitochondrial member of the dynamin family of molecules. It is ubiquitously expressed, and found in both the ER and outer mitochondrial membrane. Through trans-interactions with MFN-1 and/or MFN-2, MFN-2 apparently mediates the fusion of individual mitochondria with either the ER or with adjacent mitochondria. Pertubations with this process result in both a general failure of mitochondria to fuse, and in cell-specific effects such as a reduction in oxidative phosphorylation, a decrease in the axonal transport of mitochondria, and a deficit in the expression of respiratory chain components. MFN-2 has two key domains. One is a coiled-coil region that mediates MFN-2:MFN-1/2 binding, and a second is a GTPase domain that likely plays a role in fusion. While active, the MFN-2 GTPase domain is 8-fold lower in activity than that for MFN-1. Human MFN-2 is a 757 amino acid (aa) two transmembrane protein that contains a cytoplasmic N- and C‑terminus. The cytoplasmic N‑terminus (aa 1-604) contains the GTPase domain (aa 99-258) while the cytoplasmic C‑terminus possesses a critical coiled-coil motif (aa 696-738). MFN-2 is known to form oligomers, either with itself or MFN-1. Two potential splice variants are reported, one that shows a deletion of aa 245-273, and a second that contains a 33 aa substitution for aa 573-757, suggesting this might be a soluble for of MFN-2. Over aa 364-599, human and mouse MFN-2 share 93% aa sequence identity. Full-length human MFN-2 and MFN-1 share 61% aa sequence identity.
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