Product Name: Cellular Apoptosis Susceptibility Antibody
Species Reactivity: Human, Mouse
Tested Applications: IF, IHC-P, WB
Applications: For IHC-P starting dilution is: 1:100For IF starting dilution is: 1:100For WB starting dilution is: 1:1000
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 110 kDa
Immunogen: This Cellular Apoptosis Susceptibility antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 55-84 amino acids from the N-terminal region of human Cellular Apoptosis Susceptibility.
Host Species: Rabbit
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Physical State: Liquid
CAS NO.: 15574-49-9
Product: Mecarbinate
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: Exportin-2, Exp2, Cellular apoptosis susceptibility protein, Chromosome segregation 1-like protein, Importin-alpha re-exporter, CSE1L, CAS, XPO2
Accession NO.: P55060
Protein Ino: 62297557
Official Symbol: CSE1L
Geneid: 1434
Background: Proteins that carry a nuclear localization signal (NLS) are transported into the nucleus by the importin-alpha/beta heterodimer. Importin-alpha binds the NLS, while importin-beta mediates translocation through the nuclear pore complex. After translocation, RanGTP binds importin-beta and displaces importin-alpha. Importin-alpha must then be returned to the cytoplasm, leaving the NLS protein behind. CSE1L binds strongly to NLS-free importin-alpha, and this binding is released in the cytoplasm by the combined action of RANBP1 and RANGAP1. In addition, CSE1L may play a role both in apoptosis and in cell proliferation.
PubMed ID:http://aac.asm.org/content/35/11/2185.abstract
