P7749
Anti-Profilin 1 (N-terminal) antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-PFN1
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About This Item
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biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~15 kDa
species reactivity
human, rat, mouse
concentration
~1 mg/mL
technique(s)
indirect immunofluorescence: 10-20 μg/mL using rat NRK cells
western blot (chemiluminescent): 1-2 μg/mL using whole extracts of mouse NIH3T3 and human HeLa cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... PFN1(5216)
mouse ... Pfn1(18643)
rat ... Pfn1(64303)
Related Categories
General description
Anti-Profilin 1 (N-terminal) is developed in rabbit using as immunogen a synthetic peptide corresponding to amino acid residues of human profilin 1, conjugated to keyhole limpet hemocyanin (KLH). Profilin 1 is a ubiquitous actin monomer-binding protein. Profilin 1 is highly expressed throughout development and adulthood in most of the tissues including brain.
Immunogen
synthetic peptide corresponding to amino acid residues 2-17 of human profilin 1, conjugated to KLH. The correspopnding rat and mouse sequence differs by one amino acid. This sequence is 70% similar to the corresponding sequence in profilin 2.
Application
Anti-Profilin 1 (N-terminal) antibody produced in rabbit has been used in immunoblotting and immunofluorescence.
Biochem/physiol Actions
Profilin 1 is involved in actin polymerization in response to extracellular signals. Profilins were shown to be important for normal cell proliferation, differentiation and motility.. Profilin 1 is a potent regulator of actin filament dynamics. Profilin 1 was suggested to act as a tumor suppressor protein based on its reduced expression in several types of invasive cancers and its ability to suppress tumorigenicity when overexpressed in breast cancer cells. Deletion of profilin 1 gene leads to an embryonic lethal phenotype and Miller-Dieker syndrome.
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.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Megakaryocyte-specific Profilin1-deficiency alters microtubule stability and causes a Wiskott-Aldrich syndrome-like platelet defect
Bender M, et al.
Nature Communications, 5(4746), 1-14 (2014)
Mina Nekouei et al.
Basic and clinical neuroscience, 12(2), 213-222 (2021-12-21)
Profilin1 (PFN1) is a ubiquitously expressed protein known for its function as a regulator of actin polymerization and dynamics. A recent discovery linked mutant PFN1 to Amyotrophic Lateral Sclerosis (ALS), which is a fatal and progressive motor neuron disease. We
Mina Nekouei et al.
Metabolic brain disease, 33(6), 1975-1984 (2018-09-12)
Single amino acid mutations in profilin 1 (PFN1) have been found to cause amyotrophic lateral sclerosis (ALS). Recently, we developed a mouse model for ALS using a PFN1 mutation (glycine 118 to valine, G118V), and we are now interested in
Michaela Nejedlá et al.
Life science alliance, 4(1) (2020-11-14)
Profilin 1 is a crucial actin regulator, interacting with monomeric actin and several actin-binding proteins controlling actin polymerization. Recently, it has become evident that this profilin isoform associates with microtubules via formins and interferes with microtubule elongation at the cell
Daniel Fil et al.
Human molecular genetics, 26(4), 686-701 (2017-01-04)
The recent identification of profilin1 mutations in 25 familial ALS cases has linked altered function of this cytoskeleton-regulating protein to the pathogenesis of motor neuron disease. To investigate the pathological role of mutant profilin1 in motor neuron disease, we generated
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