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Merck

SAB4200357

Sigma-Aldrich

Anti-Profilin 1 antibody, Mouse monoclonal

clone Profilin 1-3, purified from hybridoma cell culture

Sinónimos:

Anti-PFN1

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

mouse

conjugado

unconjugated

forma del anticuerpo

purified from hybridoma cell culture

tipo de anticuerpo

primary antibodies

clon

Profilin 1-3, monoclonal

formulario

buffered aqueous solution

mol peso

antigen ~15 kDa

reactividad de especies

rat, bovine, human, mouse, canine

concentración

~1.0 mg/mL

técnicas

immunoprecipitation (IP): suitable
western blot: 1-2 μg/mL using whole extracts of HeLa or NRK cells

isotipo

IgG1

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

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

Categorías relacionadas

Descripción general

Monoclonal Anti-Profilin 1 (mouse IgG1 isotype) is derived from the hybridoma Profilin1-3 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to a sequence located near the C-terminus of human profiling 1, conjugated to keyhole limpet hemocyanin (KLH). Profilin-1 (Pfn1), a major actin-regulatory protein is mapped to human chromosome17p13. It is the most ubiquitous and abundant protein and is highly expressed throughout development and adulthood in most tissues including brain.

Inmunógeno

synthetic peptide corresponding to a sequence located near the C-terminus of human profilin 1, conjugated to KLH. The corresponding sequence is identical in mouse and rat profilin 1.

Aplicación

Monoclonal Anti-Profilin 1 antibody produced in mouse has been used in immunoblotting and immunoprecipitation.

Acciones bioquímicas o fisiológicas

Profilin-1 (Pfn1) 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. It is 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 over expressed in breast cancer cells. Deletion of the profilin 1 gene leads to an embryonic lethal phenotype.

Forma física

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

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

10 - Combustible liquids

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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PFN1 mutations are rare in Han Chinese populations with amyotrophic lateral sclerosis
Chen YP, et al.
Neurobiology of Aging, 34(7) (2013)
Profilin I is essential for cell survival and cell division in early mouse development
Witke W, et al.
Proceedings of the National Academy of Sciences of the USA, 98(7), 3832-3836 (2001)
Sung Haeng Lee et al.
Molecules and cells, 29(4), 311-325 (2010-05-07)
The dynamic remolding of the actin cytoskeleton is a critical part of most cellular activities, and malfunction of cytoskeletal proteins results in various human diseases. The transition between two forms of actin, monomeric or G-actin and filamentous or F-actin, is
A balanced level of profilin-1 promotes stemness and tumor-initiating potential of breast cancer cells
Jiang C, et al.
Cell Cycle, 16(24) (2017)
Structure and functions of profilins
Krishnan K, et al.
Biophysical Reviews, 1(2), 71-71 (2009)

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