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P7749

Sigma-Aldrich

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

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

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)

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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.
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
Dynamic actin structures stabilized by profilin
Finkel T, et al.
Proceedings of the National Academy of Sciences of the USA, 91(4), 1510-1510 (1994)

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