Összes fotó(6)
Fontos dokumentumok
A5044
Monoclonal Anti-α-Actinin antibody produced in mouse
clone BM-75.2, ascites fluid
Szinonimák:
Anti-BDPLT15
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(6)
About This Item
konjugátum:
unconjugated
application:
ARR
IF
WB
IF
WB
klón:
BM-75.2, monoclonal
faj reaktivitás:
mouse, bovine, human, chicken
citations:
133
technika/technikák:
indirect immunofluorescence: 1:200 using cultured chicken fibroblasts
microarray: suitable
western blot: suitable
microarray: suitable
western blot: suitable
Javasolt termékek
biológiai forrás
mouse
Minőségi szint
konjugátum
unconjugated
antitest forma
ascites fluid
antitest terméktípus
primary antibodies
klón
BM-75.2, monoclonal
molekulatömeg
antigen 100 kDa
tartalmaz
15 mM sodium azide
faj reaktivitás
mouse, bovine, human, chicken
technika/technikák
indirect immunofluorescence: 1:200 using cultured chicken fibroblasts
microarray: suitable
western blot: suitable
izotípus
IgM
UniProt elérési szám
kiszállítva
dry ice
tárolási hőmérséklet
−20°C
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... ACTN1(87)
mouse ... Actn1(109711)
Related Categories
Általános leírás
α-actinin is a 100kD actin binding protein found in muscle as well as non-muscle cells. In smooth muscle, α-actinin is identified in dense bodies and plaques characteristic of tissues whereas it is associated with z-discs that define muscle sarcomas in normal skeletal muscle. Monoclonal anti-α-actinin antibody can be used in immunoblotting to study the membrane anchorage sites and immunochemical identification of α-actinin. It can also be used in immunofluorescence to study the localization of α-actinin in cultured cells and tissues. Mouse anti-α-actinin antibody reacts specifically with chicken fibroblasts. The product has also shown reactivity for mouse and human cells.
The gene encoding α-actinin is mapped to the human chromosome 11q13.2. α-actinin belongs to the spectrin protein superfamily.
Immunogén
cytoskeletal fraction of bovine mammary gland epithelial (BMGE) cells.
Alkalmazás
Immunofluorescence of cardiomyocytes from neonatal and adult mouse hearts was performed using monoclonal mouse anti-α actinin (clone EA-53) at 1:1000.
May be used in the study of skeletal muscle organization and in studies of the membrane anchorage sites of actin.
Monoclonal anti-α-actinin antibody (diluted 1: 500) can be used in native protein binding assays. It can also be used in western blot, microarray, immunohistochemistry and in Immunofluorescence microscopy.
Biokémiai/fiziológiai hatások
α−actinin regulates muscle contraction and cytoskeletal organization. It promotes cell migration and acts as an actin crosslinker. Mutations in the α-actinin gene is observed in heterogeneous hypertrophic cardiomyopathy and in juvenile onset atrial fibrillation.
Egyéb megjegyzések
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
10 - Combustible liquids
WGK
nwg
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
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Analitikai tanúsítványok (COA)
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Az ügyfelek ezeket is megtekintették
Protein Interactions with the Glucose Transporter Binding Protein GLUT1CBP That Provide a Link between GLUT1 and the Cytoskeleton.
Robert C. Bunn, Mari Anne Jensen
Molecular and Cellular Biology, 10(4), 819-832 (1999)
Thomas A Hawkins et al.
Development (Cambridge, England), 135(6), 1147-1156 (2008-02-08)
The mechanisms that regulate sarcomere assembly during myofibril formation are poorly understood. In this study, we characterise the zebrafish sloth(u45) mutant, in which the initial steps in sarcomere assembly take place, but thick filaments are absent and filamentous I-Z-I brushes
C M Laukaitis et al.
The Journal of cell biology, 153(7), 1427-1440 (2001-06-27)
To investigate the mechanisms by which adhesions form and disperse in migrating cells, we expressed alpha 5 integrin, alpha-actinin, and paxillin as green fluorescent protein (GFP) fusions. All localized with their endogenous counterparts and did not perturb migration when expressed
C A Conley
American journal of physiology. Cell physiology, 280(6), C1645-C1656 (2001-05-15)
Evidence is accumulating to suggest that actin filament remodeling is critical for smooth muscle contraction, which implicates actin filament ends as important sites for regulation of contraction. Tropomodulin (Tmod) and smooth muscle leiomodin (SM-Lmod) have been found in many tissues
Zongwen Tian et al.
PloS one, 9(6), e100715-e100715 (2014-06-25)
Intracellular protein degradation is primarily performed by the ubiquitin-proteasome system (UPS) and the autophagic-lysosomal pathway (ALP). The interplay between these two pathways has been rarely examined in intact animals and the mechanism underlying the interplay remains unclear. Hence, we sought
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