Product: TNF alpha Antibody
Catalog: DF6080
Description: Rabbit polyclonal antibody to TNF alpha
Application: WB IHC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Dog
Mol.Wt.: 26kDa; 26kD(Calculated).
Uniprot: P01375
RRID: AB_2838048

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:1000-1:2000, IHC 1:50-1:100
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Dog(100%)
Clonality:
Polyclonal
Specificity:
TNF alpha Antibody detects endogenous levels of total TNF alpha.
RRID:
AB_2838048
Cite Format: Affinity Biosciences Cat# DF6080, RRID:AB_2838048.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

APC1; APC1 protein; Cachectin; DIF; Differentiation inducing factor; Macrophage cytotoxic factor; Tnf; TNF superfamily, member 2; TNF, macrophage derived; TNF, monocyte derived; TNF-a; TNF-alpha; TNFA; TNFA_HUMAN; TNFSF2; Tumor necrosis factor alpha; Tumor necrosis factor; Tumor necrosis factor ligand superfamily member 2; Tumor Necrosis Factor, Membrane Form; Tumor necrosis factor, soluble form;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Description:
TNF-α, the prototypical member of the TNF protein superfamily, is a homotrimeric type-II membrane protein (1,2). Membrane-bound TNF-α is cleaved by the metalloprotease TACE/ADAM17 to generate a soluble homotrimer (2). Both membrane and soluble forms of TNF-α are biologically active. TNF-α is produced by a variety of immune cells including T cells, B cells, NK cells, and macrophages (1). Cellular response to TNF-α is mediated through interaction with receptors TNF-R1 and TNF-R2 and results in activation of pathways that favor both cell survival and apoptosis depending on the cell type and biological context. Activation of kinase pathways (including JNK, Erk (p44/42), p38 MAPK, and NF-κB) promotes the survival of cells, while TNF-α-mediated activation of caspase-8 leads to programmed cell death (1,2). TNF-α plays a key regulatory role in inflammation and host defense against bacterial infection, notably Mycobacterium tuberculosis (3). The role of TNF-α in autoimmunity is underscored by blocking TNF-α action to treat rheumatoid arthritis and Crohn’s disease (1,2,4).
Sequence:
MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Dog
100
Sheep
75
Horse
0
Bovine
0
Xenopus
0
Zebrafish
0
Chicken
0
Rabbit
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P01375 As Substrate

Site PTM Type Enzyme
S2 Phosphorylation Q8N165 (PDIK1L)
K19 Myristoylation
K20 Myristoylation
S80 O-Glycosylation
S162 Phosphorylation
S171 Phosphorylation

Research Backgrounds

Function:

Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective. Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line. Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity).

The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells.

PTMs:

The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space.

The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.

O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid.

Subcellular Location:

Cell membrane>Single-pass type II membrane protein.

Membrane>Single-pass type II membrane protein.

Secreted.

Secreted.

Secreted.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Homotrimer. Interacts with SPPL2B.

Family&Domains:

Belongs to the tumor necrosis factor family.

Research Fields

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Cellular Processes > Cell growth and death > Necroptosis.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Environmental Information Processing > Signaling molecules and interaction > Cytokine-cytokine receptor interaction.   (View pathway)

· Environmental Information Processing > Signal transduction > NF-kappa B signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Sphingolipid signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > mTOR signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > TGF-beta signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > TNF signaling pathway.   (View pathway)

· Human Diseases > Drug resistance: Antineoplastic > Antifolate resistance.

· Human Diseases > Endocrine and metabolic diseases > Type II diabetes mellitus.

· Human Diseases > Endocrine and metabolic diseases > Insulin resistance.

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Human Diseases > Endocrine and metabolic diseases > Type I diabetes mellitus.

· Human Diseases > Neurodegenerative diseases > Alzheimer's disease.

· Human Diseases > Neurodegenerative diseases > Amyotrophic lateral sclerosis (ALS).

· Human Diseases > Infectious diseases: Bacterial > Pertussis.

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Parasitic > Leishmaniasis.

· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).

· Human Diseases > Infectious diseases: Parasitic > African trypanosomiasis.

· Human Diseases > Infectious diseases: Parasitic > Malaria.

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Hepatitis C.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Immune diseases > Asthma.

· Human Diseases > Immune diseases > Inflammatory bowel disease (IBD).

· Human Diseases > Immune diseases > Systemic lupus erythematosus.

· Human Diseases > Immune diseases > Rheumatoid arthritis.

· Human Diseases > Immune diseases > Allograft rejection.

· Human Diseases > Immune diseases > Graft-versus-host disease.

· Human Diseases > Cardiovascular diseases > Hypertrophic cardiomyopathy (HCM).

· Human Diseases > Cardiovascular diseases > Dilated cardiomyopathy (DCM).

· Organismal Systems > Development > Osteoclast differentiation.   (View pathway)

· Organismal Systems > Immune system > Antigen processing and presentation.   (View pathway)

· Organismal Systems > Immune system > Toll-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > NOD-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > RIG-I-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Hematopoietic cell lineage.   (View pathway)

· Organismal Systems > Immune system > Natural killer cell mediated cytotoxicity.   (View pathway)

· Organismal Systems > Immune system > IL-17 signaling pathway.   (View pathway)

· Organismal Systems > Immune system > T cell receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Fc epsilon RI signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Adipocytokine signaling pathway.

References

1). Stress-induced phosphoprotein 1 restrains spinal cord ischaemia-reperfusion injury by modulating NF-κB signalling. Journal of Cellular and Molecular Medicine (PubMed: 34734476) [IF=5.3]

Application: WB    Species: Mouse    Sample: BV2 cells

FIGURE 4 STIP1 restrains OGD-induced inflammation in microglial cells. A, BV2 cell treatments; B, Western blotting determines STIP1 expression in BV2 cells after OGD treatment, C, Immunoprecipitation detects the binding between STIP1 and HSPA8 in BV2 cells; D, Western blotting determines STIP1 expression after STIP1 overexpression; E, Immunoprecipitation detects the interaction between HSPA8 and IκBβ in BV2 cells; F, Western blotting detects IκBβ expression in BV2 cells; G, Western blotting detects cytoplasmic and nuclear NF-κB p65 levels in BV2 cells; H, Immunofluorescent staining detects the location of NF-κB p65. Scale bar =50 μm; I, Immunofluorescent staining detects the expression of the microglia marker Iba-1. Scale bar =50 μm; J, ELISA detects the secretion of inflammatory factors TNF-α and IL-6 in the cell culture supernatant; K, Western blotting determines TNF-α and IL-6 expression in BV2 cells after OGD treatment and STIP1 overexpression. NF-κB, nuclear factor kappa B; OGD, oxygen and glucose deprivation; SCII, spinal cord ischaemia-reperfusion injury; STIP1, stress-induced phosphoprotein 1; TNF, tumour necrosis factor. **p < 0.01, ***p < 0.001 versus the Sham group, #p < 0.05, ##p < 0.01, ###p < 0.001 versus the SCII + LV group

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