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P7749

Sigma-Aldrich

Anti-Profilin 1 (N-terminal)

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-PFN1

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About This Item

Numéro MDL:
MFCD09265369
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~15 kDa

Espèces réactives

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

Numéro d'accès UniProt

P15735

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... PFN1(5216)
mouse ... Pfn1(18643)
rat ... Pfn1(64303)

Description générale

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.

Immunogène

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.

Actions biochimiques/physiologiques

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.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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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
Identification of the functional profilin gene, its localization to chromosome subband 17p13. 3, and demonstration of its deletion in some patients with Miller-Dieker syndrome.
Kwiatkowski DJ, et al.
American Journal of Human Genetics, 46(3), 559-559 (1990)
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