Product Name: CASKIN1 Antibody
Species Reactivity: Human
Tested Applications: ELISA, WB
Applications: CASKIN1 antibody can be used for detection of CASKIN1 by Western blot at 1 μg/mL.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: Predicted: 157 kDa Observed: 160 kDa
Immunogen: CASKIN1 antibody was raised against a 17 amino acid synthetic peptide near the center of human CASKIN1.The immunogen is located within amino acids 720 – 770 of CASKIN1.
Host Species: Rabbit
Purification: CASKIN1 Antibody is affinity chromatography purified via peptide column.
Physical State: Liquid
CAS NO.: 934343-74-5
Product: NVP-HSP990
Buffer: CASKIN1 Antibody is supplied in PBS containing 0.02% sodium azide.
Concentration: 1 mg/mL
Storage Conditions: CASKIN1 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: CASKIN1 Antibody: ANKS5A, KIAA1306, Caskin-1, CASK-interacting protein 1
Accession NO.: NP_065815
Protein Ino: 18079216
Official Symbol: CASKIN1
Geneid: 57524
Background: CASKIN1 Antibody: Calcium/calmodulin-dependent serine protein kinase (CASK) is a conserved multi-domain scaffolding protein involved in brain development, synapse formation, and establishment of cell polarity. CASKINs (CASK interacting proteins) interact with CASK and is thought to play a role in CASK function, specifically by coupling CASK to distinct downstream effectors. CASKIN1 is a multidomain protein containing six N-terminal ankyrin repeats, one SH3 domain, and two sterile alpha motif domains followed by a long proline-rich sequence and a short conserved C-terminal domain. CASKIN1 coassembles with CASK on the cytoplasmic tail of neurexin 1, suggesting that CASKIN and CASK coat the cytoplasmic tails of neurexins and other cell-surface proteins.
PubMed ID:http://aac.asm.org/content/43/4/920.abstract