Product Name: CACNA2D4 Antibody
Species Reactivity: Human
Tested Applications: Flow, WB
Applications: For WB starting dilution is: 1:1000For FACS starting dilution is: 1:10~50
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 128 kDa
Immunogen: This CACNA2D4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 89-118 amino acids from the N-terminal region of human CACNA2D4.
Host Species: Rabbit
Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.
Physical State: Liquid
CAS NO.: 876708-01-9
Product: Nucleoside-Analog-2
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: 0.5 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: Voltage-dependent calcium channel subunit alpha-2/delta-4, Voltage-gated calcium channel subunit alpha-2/delta-4, Voltage-dependent calcium channel subunit alpha-2-4, Voltage-dependent calcium channel subunit delta-4, CACNA2D4
Accession NO.: Q7Z3S7
Protein Ino: 296434419
Official Symbol: CACNA2D4
Geneid: 93589
Background: CACNA2D4 is a member of the alpha-2/delta subunitfamily, a protein in the voltage-dependent calcium channel complex.Calcium channels mediate the influx of calcium ions into the cellupon membrane polarization and consist of a complex of alpha-1,alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Variousversions of each of these subunits exist, either expressed fromsimilar genes or the result of alternative splicing. Research on ahighly similar protein in rabbit suggests the protein described inthis record is cleaved into alpha-2 and delta subunits. Alternatetranscriptional splice variants of this gene have been observed buthave not been thoroughly characterized.
PubMed ID:http://aac.asm.org/content/43/1/12.abstract
