Dematin (phospho Ser403) rabbit pAb

Sizes: 50μL, 100μL

Catalogue Numbers: ES5124-50, ES5124-100

Citations, Manuals and MSDS Available upon request.

Background: The protein encoded by this gene is an actin binding and bundling protein that plays a structural role in erythrocytes, by stabilizing and attaching the spectrin/actin cytoskeleton to the erythrocyte membrane in a phosphorylation-dependent manner. This protein contains a core domain in the N-terminus, and a headpiece domain in the C-terminus that binds F-actin. When purified from erythrocytes, this protein exists as a trimer composed of two 48 kDa polypeptides and a 52 kDa polypeptide. The different subunits arise from alternative splicing in the 3' coding region, where the headpiece domain is located. Disruption of this gene has been correlated with the autosomal dominant Marie Unna hereditary hypotrichosis disease, while loss of heterozygosity of this gene is thought to play a role in prostate cancer progression. Alternative splicing results in multiple transcript variants encoding di

Alternate Name: EPB49; DMT; Dematin; Erythrocyte membrane protein band 4.9

Source: Rabbit

Applications: WB; IHC; IF; ELISA

Dilution: Western Blot: 1/500 - 1/2000. Immunohistochemistry: 1/100 - 1/300. ELISA: 1/10000. Not yet tested in other applications.

Reactivity: Human; Mouse

Immunogen: The antiserum was produced against synthesized peptide derived from human Dematin around the phosphorylation site of Ser403. AA range:356-405

Storage and Stability: -20°C/1 year

Clonality: Polyclonal

Isotype: IgG

Concentration: 1 mg/ml

Observed Band (KD): 55kD

Human Gene ID: 2039

Human SWISS Prot NO: Q08495

Subcellular Location: Cytoplasm. Cytoplasm, cytosol. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Cell membrane. Membrane. Endomembrane system. Cell projection. Localized at the spectrin-actin junction of erythrocyte plasma membrane. Localized to intracellular membranes and the cytoskeletal network. Localized at intracellular membrane-bounded organelle compartment in platelets that likely represent the dense tubular network membrane. Detected at the cell membrane and at the parasitophorous vacuole in malaria-infected erythrocytes at late stages of plasmodium berghei or falciparum development.

Research Use Only