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SAB4200689

Sigma-Aldrich

Anti-Actin (α-Sarcomeric) antibody, Mouse monoclonal

clone 5C5, hybridoma cell culture supernatant

Synonyme(s) :

Actin alpha sarcomeric/skeletal, a-SCA, alpha-SCA, alpha-sarcomeric actin

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

200

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

5C5, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~42 kDa

Espèces réactives

rat, chicken, bovine, mouse, guinea pig, rabbit, human, planaria(flatworm), fish, Xenopus

Conditionnement

antibody small pack of 25 μL

Technique(s)

ELISA: suitable
immunoblotting: 1:500-1:1000 using rat heart tissue extracts
immunofluorescence: 1:500-1000 using human HeLa cells.
immunohistochemistry: 1:500 using formalin-fixed, paraffin-embedded human tongue sections and Biotin/ExtrAvidin®-Peroxidase staining system.

Isotype

IgM

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... ACTA2(59)

Description générale

Monoclonal Anti-Actin (-Sarcomeric) (mouse IgM isotype) is derived from the hybridoma 5C5 produced by the fusion of mouse myeloma cells and splenocytes from mice immunized with purified rabbit striated muscle. Actin is the major cytoskeletal protein in eukaryotic cells.

Immunogène

purified rabbit striated muscle

Application

Anti-Actin (α-Sarcomeric) antibody, Mouse monoclonal has been used in:
  • indirect immunofluorescence staining
  • immunohistochemistry
  • enzyme-linked immunosorbent assay (ELISA)
  • immunoblotting
  • immunofluorescence

Actions biochimiques/physiologiques

Actin plays essential roles in a number of cellular processes including cell migration, cytokinesis, vesicle transport and contractile force generation.

Forme physique

The product is supplied as a culture supernatant solution containing 15 mM sodium azide as a preservative. The product contains bovine serum albumin and a human-derived protein.

Informations légales

ExtrAvidin is a registered trademark of Merck KGaA, Darmstadt, Germany

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

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Na Tang et al.
Nature communications, 13(1), 7455-7455 (2022-12-03)
Intracellular Ca2+ dysregulation is a key marker in septic cardiac dysfunction; however, regulation of the classic Ca2+ regulatory modules cannot successfully abolish this symptom. Here we show that the knockout of transient receptor potential canonical (TRPC) channel isoforms TRPC1 and
Xinhui Fan et al.
Frontiers in pharmacology, 13, 892643-892643 (2022-07-23)
Diabetes mellitus (DM) often involves cardiovascular complications; however, treatment regimens are limited. ROCK1 (rho-associated coiled-coil containing protein kinase 1) serves as a pathological factor in several diabetic complications. Herein, we aimed to explore the effect of Fasudil (a ROCK1 inhibitor)
PEDF decreases cardiomyocyte edema during oxygen-glucose deprivation and recovery via inhibiting lactate accumulation and expression of AQP1
Huang B, et al.
International Journal of Molecular Medicine, 43(5), 1979-1990 (2019)
The actin cytoskeleton
Molecular and Cellular Biology, 1979-1990 (2000)
Actin depolymerisation and crosslinking join forces with myosin II to contract actin coats on fused secretory vesicles
Miklavc P, et al.
Journal of Cell Science, 128(6), 1193-1203 (2015)
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