epitope corresponding to amino acids 157-286 mapping at the C-terminus of CapZ-α1 of human origin
Modification Notes
The F-Actin family of capping proteins includes CapZ-å1, CapZ-å2, CapZ-å3 and CapZ-∫3, all of which function in a calcium-dependent manner and bind to the fast growing barbed end of Actin filaments, thereby blocking protein exchange at these ends. The F-Actin capping protein complex is a heterodimer consisting of å and ∫ subunits that caps the barbed ends of Actin filaments and nucleates the polymerization of Actin monomers, yet does not sever Actin filaments. CapZ-å1, also known as F-Actin-capping protein subunit alpha-1, is a 286 amino acid subunit of the heterodimer that forms the F-Actin capping protein complex. CapZ-å1 also has been shown to bind S-100 ∫ chain, a signaling molecule involved in the calcium-sensitive assembly of intermediate filaments that has been linked to Alzheimer’s disease.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of CapZ-α1 and CapZ-α2 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 157-286 mapping at the C-terminus of CapZ-&alpha 1 of human origin
Tissue Specificity
epitope corresponding to amino acids 157-286 mapping at the C-terminus of CapZ-α1 of human origin
Western blot analysis of CapZ-α expression in A-431 (A) and T24 (B) whole cell lysates.
Application Notes
recommended for detection of CapZ-α1 and CapZ-α2 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.