T1816
Anti-Tumor Necrosis Factor-α antibody produced in goat
affinity isolated antibody, lyophilized powder
Synonym(s):
Anti-TNF-α
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About This Item
UNSPSC Code:
51111800
NACRES:
NA.41
conjugate:
unconjugated
application:
ELISA (i)
IHC
Neutral
WB
IHC
Neutral
WB
clone:
polyclonal
species reactivity:
pig
citations:
4
technique(s):
immunohistochemistry: 15 μg/mL
indirect ELISA: 0.5-1.0 μg/mL
neutralization: suitable
western blot: 0.1-0.2 μg/mL
indirect ELISA: 0.5-1.0 μg/mL
neutralization: suitable
western blot: 0.1-0.2 μg/mL
Recommended Products
biological source
goat
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized powder
species reactivity
pig
technique(s)
immunohistochemistry: 15 μg/mL
indirect ELISA: 0.5-1.0 μg/mL
neutralization: suitable
western blot: 0.1-0.2 μg/mL
UniProt accession no.
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
pig ... TNF(397086)
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General description
Tumor Necrosis Factor-α (TNF-α) also refers as cachectin is a cytokine produced in response to immunological challenges such as bacteria (lipopolysaccharides), parasites, mitogens, viruses and other cytokines. It has essential roles in antitumor activity, inflammation, septic shock, immune modulation, anorexia, cachexia, hematopoiesis and viral replication. It also facilitates the growth of human fibroblasts, collagenase production as well as can activates polymorphonuclear neutrophils and osteoclasts. Anti-Tumor Necrosis Factor-α antibody can be used in neutralization and immunoblotting (working concentration-0.1-0.2 μg/ml) for detecting porcine TNF-α. Goat anti-Tumor Necrosis Factor-α antibody reacts specifically with recombinant porcine tumor necrosis factor α.
Specificity
The antibody neutralizes the biological activity of recombinant porcine TNF-α.
Immunogen
recombinant porcine TNF-α expressed in Escherichia coli.
Application
Anti-Tumor Necrosis Factor-α antibody can be used in immunohistochemistry and indirect ELISA.
Physical form
Lyophilized from a 0.2 μm filtered solution of phosphate buffered saline.
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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Storage Class
10 - Combustible liquids
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D R Bertolini et al.
Nature, 319(6053), 516-518 (1986-02-06)
When leukocytes are exposed to mitogens or antigens in vitro, they release bone-resorbing activity into the culture supernatants which can be detected by bioassay. Like many lymphocyte-monocyte products, this activity has been difficult to purify because of its low abundance
J M Dayer et al.
The Journal of experimental medicine, 162(6), 2163-2168 (1985-12-01)
Cachectin/TNF (tumor necrosis factor), an endotoxin-induced murine macrophage hormone implicated in the pathogenesis of cachexia and shock, has been found capable of stimulating collagenase and prostaglandin E2 (PGE2) production by isolated human synovial cells and dermal fibroblasts. This bioactivity associated
B J Sugarman et al.
Science (New York, N.Y.), 230(4728), 943-945 (1985-11-22)
Modulation of the growth of human and murine cell lines in vitro by recombinant human tumor necrosis factor-alpha (rTNF-alpha) and recombinant human interferon-gamma (rIFN-gamma) was investigated. rTNF-alpha had cytostatic or cytolytic effects on only some tumor cell lines. When administered
K M Reich et al.
Alimentary pharmacology & therapeutics, 40(6), 629-638 (2014-07-22)
Medical therapy is standard treatment for ulcerative colitis with colectomy reserved for medically refractory disease or malignancy. The introductions of ciclosporin in 1994 and anti-TNF therapy in 2005 have extended medical management options. To determine whether the colectomy incidence rate
Anca Dorhoi et al.
European journal of immunology, 44(8), 2380-2393 (2014-05-02)
General interest in the biological functions of IFN type I in Mycobacterium tuberculosis (Mtb) infection increased after the recent identification of a distinct IFN gene expression signature in tuberculosis (TB) patients. Here, we demonstrate that TB-susceptible mice lacking the receptor
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