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MABC615

Anti-TNFα Receptor Antibody, clone 13F9.1

clone 13F9.1, from mouse

Synonym(e):

Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tumor necrosis factor receptor superfamily member 1A, membrane form, Tumor necrosis f

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Über diesen Artikel

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
13F9.1, monoclonal
Application:
IHC, WB
Citations:
1
Preise und Verfügbarkeit sind derzeit nicht verfügbar.
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Unterstützung erhalten

biological source

mouse

Quality Level

100

conjugate

unconjugated

antibody form

purified antibody

antibody product type

primary antibodies

clone

13F9.1, monoclonal

species reactivity

mouse, human

technique(s)

immunohistochemistry: suitable, western blot: suitable

isotype

IgG1κ

NCBI accession no.

NP_001056

General description

Tumor necrosis factor receptor superfamily member 1A (UniProt P19438; also known as CD120a, p55, p60, TNF-R1, TNF-RI, TNFR-I, Tumor necrosis factor-alpha receptor, Tumor necrosis factor receptor type 1) is encoded by the TNFRSF1A (also known as FPF, MS5, TNFAR, TNFAR55, TNFAR60, TNFR1) gene (Gene ID 7132) in human. It functions as a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. Upon activation, TNFalpha receptor mediates apoptotic, anti-viral, and other cellular signaling events. Binding of TNF-alpha to the extracellular domain of TNF receptor leads to homotrimerization. Proteolytic cleavage results in the relese of Tumor necrosis factor-binding protein 1 (TBP1). Defects in TNF receptor cause tumor necrosis factor receptor-associated periodic syndrome (TRAPS), a hereditary periodic fever syndrome characterized by recurrent fever, abdominal pain, localized tender skin lesions and myalgia.
~50/43 kDa observed. 50.5 kDa (isoform 1/FL-TNFR1 calculated), 38.7 kDa (isoform 2 calculated), 25.6 kDa (isoform 4/Delta6-TNFR1 calculated), 24.2 kDa (isoform 5 calculated).

Immunogen

GST-tagged recombinant protein corresponding to the extracellular domain of human TNFα Receptor.

Application

Anti-TNF apha Receptor Antibody, clone 13F9.1 is a highly specific mouse monoclonal antibody, that targets TNFα Receptor & has been tested in Western Blotting, and Immunohistochemistry.
Western Blotting Analysis: 1.0 µg/mL from a representative lot detected TNFα Receptor in 10 µg of HepG2 and RAW264 cell lysate.
Immunohistochemistry Analysis: A 1:1,000 dilution from a representative lot detected TNFα Receptor in human colon tissue and human colon cancer cells.

Biochem/physiol Actions

Expected to react with spliced isoforms 1/FL-TNFR1, 2, 4/Delta6-TNFR1, and 5, but not isoform 3.

Physical form

Format: Purified

Analysis Note

Evaluated by Western Blotting in Jurkat cell lysate.

Western Blotting Analysis: 1.0 µg/mL of this antibody detected TNFα Receptor in 10 µg of Jurkat cell lysate.

Other Notes

Concentration: Please refer to lot specific datasheet.

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Lagerklasse

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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Die Dokumentenbibliothek aufrufen

Qian Bai et al.
Molecular neurobiology, 56(1), 278-291 (2018-04-27)
Previous studies have shown that tumor necrosis factor alpha (TNFα) is significantly increased in complete Freund's adjuvant (CFA)-treated temporomandibular joint (TMJ) tissues. However, it is unclear whether TNFα in the trigeminal nociceptive system contributes to the development of TMJ pain.

Verwandter Inhalt

Characterization of Estrogen Receptor α Phosphorylation Sites in Breast Cancer Tissue Using the SNAP i.d® 2.0 System

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

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