biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized powder
species reactivity
human
technique(s)
western blot: suitable
immunogen sequence
GRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI
NCBI accession no.
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... ACTB(60)
General description
Actin, a highly conserved protein, is a major component of both the cytoskeletal and contractile structures in all cell types. It varies in amount, being related to the type of differentiation and to the functional state of cells and tissues. Actin can be found in two different forms of aggregation, the globular or the fibrillar state, and at least six distinct isoforms occur in vertebrates. The actins exhibit over 90% sequence homology, but each isoform has a unique NH2-terminal sequence. The isoforms are comprised of three α actins (skeletal, cardiac, smooth), one β actin (β-non-muscle) and two gamma actins (gamma smooth muscle and gamma non-muscle). Difficulties have been encountered in producing polyclonal antibodies due to the highly conserved nature of actin.
Immunogen
synthetic peptide corresponding to a region of human ACTB with an internal ID of P22019
Application
β-actin is a nonmuscle actin involved in cytoskeletal structures. Anti-ACTB (anti-β-Actin) is a rabbit IgG polyclonal antibody used to tag β-Actin protein(s) for detection and quantitation by Western blotting and in cells and tissues by immunohistochemical (IHC) techniques.
Rabbit Anti-ActinB is useful for studying actin structure and function, and to probe binding sites of actin-binding proteins.
Rabbit Anti-ActinB is useful for studying actin structure and function, and to probe binding sites of actin-binding proteins.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Biochem/physiol Actions
Anti-ACTB (anti-β-Actin) antibody recognizes an internal sequence of human β-actin.
Physical form
Lyophilized from PBS buffer with 2% sucrose
Disclaimer
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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存储类别
13 - Non Combustible Solids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Megan R Fisher et al.
Journal of immunology (Baltimore, Md. : 1950), 198(7), 2943-2956 (2017-02-19)
Mammalian cells have evolved a common DNA damage response (DDR) that sustains cellular function, maintains genomic integrity, and suppresses malignant transformation. In pre-B cells, DNA double-strand breaks (DSBs) induced at Igκ loci by the Rag1/Rag2 (RAG) endonuclease engage this DDR
Yueh-Lin Tsai et al.
Scientific reports, 12(1), 8180-8180 (2022-05-18)
Fused in Sarcoma (FUS) is a nuclear RNA/DNA binding protein that mislocalizes to the cytoplasm in the neurodegenerative diseases ALS and FTD. Despite the existence of FUS pathogenic mutations that result in nuclear import defects, a subset of ALS/FTD patients
Lori A Ehrlich et al.
Cell cycle (Georgetown, Tex.), 14(3), 388-398 (2015-02-07)
T-cell acute lymphoblastic leukemia (T-ALL) is a cancer of immature T cells that exhibits heterogeneity of oncogenic lesions, providing an obstacle for development of more effective and less toxic therapies. Inherited deficiency of ATM, a regulator of the cellular DNA
Jing Wang et al.
Molecular medicine reports, 11(5), 3505-3510 (2015-01-13)
A high expression of CD44v6 has been reported in numerous malignant cancers, including stomach, prostate, lung and colon. However, the pathological role and the regulatory mechanisms of CD44v6 have yet to be elucidated. In the present study, the expression levels
Ekkehart Lausch et al.
American journal of human genetics, 85(2), 168-178 (2009-07-21)
The matrix metalloproteinases MMP9 and MMP13 catalyze the degradation of extracellular matrix (ECM) components in the growth plate and at the same time cleave and release biologically active molecules stored in the ECM, such as VEGFA. In mice, ablation of
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