P0101
Anti-Profilin 2 (C-terminal) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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All Photos(2)
Synonym(s):
Anti-PFN2
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~14 kDa
species reactivity
rat, mouse, human
packaging
antibody small pack of 25 μL
technique(s)
western blot: 1:500-1:1,000 using whole extracts of human SH-SY5Y cells, mouse brain, and rat brain
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... PFN2(5217)
mouse ... Pfn2(18645)
rat ... Pfn2(81531)
Related Categories
General description
Profilins are actin-monomer-binding proteins, abundantly expressed in all eukaryotic cells from yeast to mammals. Profilin 2 (PFN2) is the neuronal specific isoform. It is an actin-binding protein and is a member of the small G-actin-binding class of protein.
Immunogen
synthetic peptide corresponding to amion acid residues 128-140 of human profilin 2 conjugated to KLH. The corresponding sequence is identical in mouse and rat.
Application
Anti-Profilin 2 (C-terminal) antibody produced in rabbit has been used in immunostaining and immunoblotting.
Biochem/physiol Actions
Profilins are key regulators of actin dynamics. Profilin 2 (PFN2) associates with a number of proteins involved in membrane trafficking and endocytosis, such as synapsin and dynamin 1. It associates with dynamin 1 through the C-terminal proline-rich domain of dynamin 1 and thereby competes with the binding of SH3 ligands, such as endophilin and amphiphysin, thus interfering with the assembly of the endocytic machinery. Overexpression of profilin 2 inhibits endocytosis. Absence of profilin 2 in neurons increases endocytosis and membrane recycling. Profilin 2 is required for stimulated actin polymerization in the synapse and is involved in the regulation of synaptic vesicle exocytosis, neuronal excitability and complex behavior.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Profilin2 contributes to synaptic vesicle exocytosis, neuronal excitability, and novelty-seeking behavior
Boyl PP, et al.
The Embo Journal, 26(12), 2991-2991 (2007)
Loss of profilin 2 contributes to enhanced epithelial-mesenchymal transition and metastasis of colorectal cancer
Zhang H, et al.
International Journal of Oncology, 53(3), 1118-1118 (2018)
Mouse profilin 2 regulates endocytosis and competes with SH3 ligand binding to dynamin 1
Gareus R, et al.
The Journal of biological chemistry, 281(5), 2803-2811 (2006)
Lisa Marie Walter et al.
Scientific reports, 11(1), 10287-10287 (2021-05-15)
Nuclear and cytoplasmic actin-cofilin rods are formed transiently under stress conditions to reduce actin filament turnover and ATP hydrolysis. The persistence of these structures has been implicated in disease pathology of several neurological disorders. Recently, the presence of actin rods
Lisa Marie Walter et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 34(2), 2147-2160 (2020-01-08)
Profilin is a major regulator of actin dynamics in multiple specific processes localized in different cellular compartments. This specificity is not only meditated by its binding to actin but also its interaction with phospholipids such as phosphatidylinositol (4,5)-bisphosphate (PIP2 )
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