Product Name: ACTN4 Antibody
Species Reactivity: Human
Tested Applications: WB
Applications: For WB starting dilution is: 1:1000
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 105 kDa
Immunogen: This ACTN4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 192-220 amino acids from the N-terminal region of human ACTN4.
Host Species: Rabbit
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Physical State: Liquid
CAS NO.: 1208243-50-8
Product: ARA290
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: 2 mg/ml
Storage Conditions: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: Alpha-actinin-4, F-actin cross-linking protein, Non-muscle alpha-actinin 4, ACTN4
Accession NO.: O43707
Protein Ino:
Official Symbol: ACTN4
Geneid: 81
Background: Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This protein is a nonmuscle, alpha actinin isoform which is concentrated in the cytoplasm, and is thought to be involved in metastatic processes. Mutations in the gene encoding this protein have been associated with focal and segmental glomerulosclerosis.
PubMed ID:http://aac.asm.org/content/52/3/1201.abstract
