Ugrás a tartalomra
Merck

A2103

Sigma-Aldrich

Anti-Actin, N-terminal antibody produced in rabbit

enhanced validation

~0.5 mg/mL, affinity isolated antibody, buffered aqueous solution

Szinonimák:

Actin Detection Antibody, Rabbit Anti-Actin

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.41
konjugátum:
unconjugated
application:
ICC
IF
IHC (p)
WB
klón:
polyclonal
faj reaktivitás:
frog, rat, mouse, chicken, human
citations:
226
technika/technikák:
immunocytochemistry: 1-2 μg/mL using cultured chicken fibroblasts
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 2-4 μg/mL using sections of human appendix, mouse heart, and frog skeletal muscle
indirect immunofluorescence: suitable
western blot: 0.5-1 μg/mL using whole extract of the human epitheloid carcinoma HeLa cell line.
western blot: 2-4 ng/mL using whole extract of rat skeletal muscle

biológiai forrás

rabbit

Minőségi szint

konjugátum

unconjugated

antitest forma

affinity isolated antibody

antitest terméktípus

primary antibodies

klón

polyclonal

Forma

buffered aqueous solution

molekulatömeg

antigen 42 kDa

faj reaktivitás

frog, rat, mouse, chicken, human

kiszerelés

antibody small pack of 25 μL

fejlettebb validálás

independent
Learn more about Antibody Enhanced Validation

koncentráció

~0.5 mg/mL

technika/technikák

immunocytochemistry: 1-2 μg/mL using cultured chicken fibroblasts
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 2-4 μg/mL using sections of human appendix, mouse heart, and frog skeletal muscle
indirect immunofluorescence: suitable
western blot: 0.5-1 μg/mL using whole extract of the human epitheloid carcinoma HeLa cell line.
western blot: 2-4 ng/mL using whole extract of rat skeletal muscle

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Általános leírás

Actin is a cytoskeletal protein that regulates cell motility, secretion, phagocytosis and cytokinesis. The NH2-terminal of actin may function as an antigen. This terminal may also modulate actin interactions and may associate with proteins such as myosin.
Actin is one of the most conserved eukaryotic proteins, which is expressed in mammals and birds as at least six major different isoforms. Four of them represent the differentiation markers of muscle tissues and two are found practically in all non-muscle cells. Actin isoforms show >90% overall sequence homology, but only 50-60% homology in their 18 N-terminal residues. Actin is present in cells both as a globular monomer (G-actin) and as a polymer in filamentous actin (F-actin) that participates in the formation of a variety of stable and labile structures. The presence of actin in cell nuclei and cell membranes has been reported.

Immunogén

synthetic actin N-terminal nonapeptide conjugated to KLH.

Alkalmazás

Anti-Actin, N-terminal antibody produced in rabbit has been used in
  • immunoblotting
  • quantitative chromatin immunoprecipitation (qChIP)

Protein lysates generated from embryonic mouse limb tissue was analyzed by western blot using actin as the loading control. Actin was detected using rabbit anti-actin at 1:8000. Actin detected by a rabbit anti-actin antibody was used as a loading control for MCF7 cell lysates . Actin was detected at 42 kDa.
Rabbit anti-actin, N-terminal antibody can be used for western blotting assays. The antibody can also be used for immunocytochemistry at 1-2μg/mL using cultured chicken fibroblasts. Furthermore, the antibody is suitable for use in immunohistochemistry at a concentration of 2-4μg/mL using sections of human appendix, mouse heart, and frog skeletal muscle.

Biokémiai/fiziológiai hatások

Actin and myosin are constituents of many cell types and are involved in a myriad of cellular processes including maintenance of cell shape, locomotion, secretion, cytoplasmic streaming, phagocytosis, and cytokinesis. The N-terminal domain of actin appears to be a major antigenic region of the molecule. Different isoforms can coexist in the same cell but are differentially regulated, and in most cases cannot substitute for each other functionally.

Fizikai forma

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide.

Egyéb megjegyzések

To view an Actin antibody selection guide, please visit www.sigmaaldrich.com/actin.

Jogi nyilatkozat

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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Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 2

Egyéni védőeszköz

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


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Nuclear actin polymerization is required for transcriptional reprogramming of Oct4 by oocytes
Miyamoto K, et al.
Genes & Development, 25(9), 946-958 (2011)
Monoclonal antibodies against muscle actin isoforms: epitope identification and analysis of isoform expression by immunoblot and immunostaining in normal and regenerating skeletal muscle
Chaponnier C and Gabbiani G
F1000Research, 5 (2016)
Kristine Raaby Jakobsen et al.
Journal of molecular signaling, 8(1), 9-9 (2013-09-06)
Protrusions of cancer cells conferrers a vital function for cell migration and metastasis. Protein and RNA localization mechanisms have been extensively examined and shown to play pivotal roles for the functional presence of specific protein components in cancer cell protrusions.
Luciferase expression and bioluminescence does not affect tumor cell growth in vitro or in vivo
Tiffen JC, et al.
Molecular Cancer, 9(1), 299-299 (2010)
Kale S Bongers et al.
American journal of physiology. Endocrinology and metabolism, 305(7), E907-E915 (2013-08-15)
Skeletal muscle denervation causes muscle atrophy via complex molecular mechanisms that are not well understood. To better understand these mechanisms, we investigated how muscle denervation increases growth arrest and DNA damage-inducible 45α (Gadd45a) mRNA in skeletal muscle. Previous studies established

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