raised against amino acids 1128-1427 mapping at the C-terminus of CLIP-170 of human origin
Modification Notes
Cytoplasmic linker protein (CLIP-170) is the original member of a group of microtuble binding proteins designated as plus-end-binding proteins (+TIPs). CLIP-170 binds to the growing plus ends of microtubules and acts as a linker between the dynamic microtubule ends and organelle membranes. The protein acts as an anticatastrophic factor, promoting microtubule rescue near the cell periphery. Fluorescently labeled CLIP-170 can be visualized as a comet like streak around the growing ends of microtubules. CLIP-170 co-localizes with Dynactin and Dynein at microtubule ends and also at the kinetochore. Restin, first identified as a marker for Hodgkin and Reed-Sternberg (HRS) cells, is a splice variant of the gene that includes a 35 amino acid stretch not present in CLIP-170. CLIP-170/restin is highly expressed in HRS cells, monocyte-derived dendritic cells, IL-4 + CD40L activated B cells and Ki-1 lymphoma.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of CLIP-170 and restin of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including canine, bovine and porcine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
raised against amino acids 1128-1427 mapping at the C-terminus of CLIP-170 of human origin
Tissue Specificity
raised against amino acids 1128-1427 mapping at the C-terminus of CLIP-170 of human origin
Western blot analysis of CLIP-170 expression in T2.DR3 whole cell lysate.
Application Notes
recommended for detection of CLIP-170 and restin of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including canine, bovine and porcine:
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.