Product Name: CaBP8 Antibody
Species Reactivity: Human, Mouse, Rat
Tested Applications: ELISA, WB
Applications: CaBP8 antibody can be used for detection of CaBP8 by Western blot at 1 – 2 μg/mL. For immunofluorescence start at 20 μg/mL.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight:
Immunogen: CaBP8 antibody was raised against a 16 amino acid synthetic peptide near the amino terminus of human CaBP8.The immunogen is located within the first 50 amino acids of CaBP8.
Host Species: Rabbit
Purification: CaBP8 Antibody is affinity chromatography purified via peptide column.
Physical State: Liquid
CAS NO.: 894187-61-2
Product: STF-118804
Buffer: CaBP8 Antibody is supplied in PBS containing 0.02% sodium azide.
Concentration: 1 mg/mL
Storage Conditions: CaBP8 antibody can be stored 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: CaBP8 Antibody: CABP8, CABP8, Calcium-binding protein 8, Calneuron I, CaBP8
Accession NO.: NP_113656
Protein Ino: 157743275
Official Symbol: CALN1
Geneid: 83698
Background: CaBP8 Antibody: Calcium binding proteins (CaBP) play a crucial role in the calcium-mediated cellular signal transduction pathway in the central nervous system. The CaBP family shares much similarity with CaM I (calmodulin), and it has been shown that CaBP proteins can substitute functionally for, and possibly augment the function of, CaM I. CaBP8, contains two EF-hand domains for calcium binding and shares 70% homology with CaBP7 and 50% homology with CaM I. It negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. Both CaBP8 and CaBP7 possess a targeting mechanism that is unique amongst the CaBPs that may contribute to differential functional Ca2+-sensing by these family members.
PubMed ID:http://aac.asm.org/content/42/12/3200.abstract
