Human TNF-alpha CLIA Kit | TNF-alpha clia kit

TNF-alpha (Human) LumiAb ELISA Kit

Cat. Num. AAA9510820

• Gene Names: TNF; DIF; TNFA; TNFSF2; TNLG1F; TNF-alpha
• Reactivity: Human
• Synonyms: TNF-alpha; TNF-alpha (Human) LumiAb ELISA Kit; Human TNF-alpha; Tumor necrosis factor; Cachectin; Tumor necrosis factor ligand superfamily member 2; TNFSF2; TNF-alpha clia kit

• Reactivity: Human
• Specificity: The LumiAb Human TIMP-1 ELISA is capable of recognizing both recombinant and naturally produced Human TIMP-1 proteins. The antigens listed below were tested at 50 ng/ml and did not exhibit significant cross reactivity or interference.
• Sequence Length: 233

• Assay Type: Quantitative Sandwich
• Sensitivity: 4 pg/ml.
• Preparation and Storage: Store at 4 degree C for 6 months.

Typical Testing Data/Standard Curve (for reference only)

Related Product Information for TNF-alpha clia kit

Principle of the Assay: The LumiAb Human TIMP-1 Chemiluminescent ELISA Kit contains the components necessary for quantitative determination of natural or recombinant Human TIMP-1 concentrations within any experimental sample including cell lysates, serum and plasma. This particular immunoassay utilizes the quantitative technique of a "Sandwich" Enzyme-Linked Immunosorbent Assay (ELISA) where the target protein (antigen) is bound in a "sandwich" format by the primary capture antibodies coated to each well-bottom and the secondary detection antibodies added subsequently by the investigator. The capture antibodies coated to the bottom of each well are specific for a particular epitope on Human TIMP-1 while the user-added detection antibodies bind to epitopes on the captured target protein. Amid each step of the procedure, a series of wash steps must be performed to ensure the elimination of non-specific binding between proteins to other proteins or to the solid phase. After incubation and "sandwiching" of the target antigen, a peroxidase enzyme is conjugated to the constant heavy chain of the secondary antibody (either covalently or via Avidin/Streptavidin-Biotin interactions), allowing for a sensitive luminescent reaction to ensue upon substrate addition. When the Peroxide Enhancer solution is added, the reaction catalyzed by peroxidase yields light that is representative of the antigen concentration. After a brief incubation, the microplate can be read with a luminometer, allowing for generation of a standard curve and subsequent determination of protein concentration!!Background/Introduction: Human TIMP-1 or Tissue Inhibitor of Metalloproteinases, also known as Fibroblast Collagenase Inhibitor, is a 207 amino acid cytokine protein encoded by the TIMP1 gene located at locus Xp11.3-Xp11.23 on the X chromosome. After initial synthesis, the 23 residue N-terminal signal sequence is removed, allowing for the 184 residue TIMP-1 protein to fold properly. Belonging to the TIMP gene family, the expressed proteins are natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1 complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. In addition to its inhibitory role against most of the known MMPs, the encoded protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. Also, TIMP-1 is known to mediate erythropoiesis in vitro, but unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and mouse erythroid progenitors. It typically acts on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16 but does not act on MMP-14. Lastly, the activity of TIMP-1 is dependent on the presence of disulfide bonds.

Product Categories/Family for TNF-alpha clia kit

Luminometer Sandwich ELISA

NCBI and Uniprot Product Information

• NCBI GI #: 37210
• NCBI GeneID: 7124
• UniProt Accession #: P01375
• NCBI Official Full Name: TNF-alpha
• NCBI Official Synonym Full Names: tumor necrosis factor
• NCBI Official Symbol: TNF
• NCBI Official Synonym Symbols: DIF; TNFA; TNFSF2; TNLG1F; TNF-alpha
• NCBI Protein Information: tumor necrosis factor
• UniProt Protein Name: Tumor necrosis factor
• UniProt Gene Name: TNF
• UniProt Synonym Gene Names: TNFA; TNFSF2; TNF-a; NTF; ICD1; ICD2
• UniProt Entry Name: TNFA_HUMAN

NCBI Description

This gene encodes a multifunctional proinflammatory cytokine that belongs to the tumor necrosis factor (TNF) superfamily. This cytokine is mainly secreted by macrophages. It can bind to, and thus functions through its receptors TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. This cytokine is involved in the regulation of a wide spectrum of biological processes including cell proliferation, differentiation, apoptosis, lipid metabolism, and coagulation. This cytokine has been implicated in a variety of diseases, including autoimmune diseases, insulin resistance, and cancer. Knockout studies in mice also suggested the neuroprotective function of this cytokine. [provided by RefSeq, Jul 2008]

Uniprot Description

TNF-a: 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. Homotrimer. Interacts with SPPL2B. Belongs to the tumor necrosis factor family.

Protein type: Cytokine; Membrane protein, integral; Motility/polarity/chemotaxis; Apoptosis

Chromosomal Location of Human Ortholog: 6p21.3

Cellular Component: extracellular space; recycling endosome; cell surface; integral to plasma membrane; plasma membrane; extracellular region; phagocytic cup; lipid raft; external side of plasma membrane

Molecular Function: identical protein binding; protein binding; protease binding; cytokine activity; tumor necrosis factor receptor binding

Biological Process: positive regulation of JNK activity; extracellular matrix organization and biogenesis; positive regulation of nitric oxide biosynthetic process; positive regulation of NFAT protein import into nucleus; activation of MAPK activity; positive regulation of osteoclast differentiation; positive regulation of apoptosis; positive regulation of transcription, DNA-dependent; response to glucocorticoid stimulus; positive regulation of caspase activity; positive regulation of NF-kappaB import into nucleus; osteoclast differentiation; positive regulation of translational initiation by iron; positive regulation of membrane protein ectodomain proteolysis; activation of NF-kappaB transcription factor; positive regulation of MAP kinase activity; tumor necrosis factor-mediated signaling pathway; positive regulation of phagocytosis; negative regulation of interleukin-6 production; JNK cascade; negative regulation of osteoblast differentiation; positive regulation of action potential; embryonic gut development; regulation of immunoglobulin secretion; negative regulation of protein complex disassembly; response to drug; positive regulation of cytokine production; positive regulation of heterotypic cell-cell adhesion; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of mitosis; response to virus; positive regulation of interleukin-8 biosynthetic process; glucose metabolic process; positive regulation of interleukin-6 production; negative regulation of fat cell differentiation; positive regulation of chemokine production; negative regulation of cytokine secretion during immune response; positive regulation of protein transport; cell activation; detection of mechanical stimulus involved in sensory perception of pain; defense response to Gram-positive bacterium; DNA damage response, signal transduction resulting in induction of apoptosis; induction of apoptosis via death domain receptors; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; response to activity; negative regulation of L-glutamate transport; negative regulation of transcription, DNA-dependent; skeletal muscle contraction; sequestering of triacylglycerol; positive regulation of smooth muscle cell proliferation; negative regulation of transcription from RNA polymerase II promoter; positive regulation of interleukin-18 production; chronic inflammatory response to antigenic stimulus; positive regulation of synaptic transmission; response to salt stress; positive regulation of hair follicle development; negative regulation of cell proliferation; response to radiation; negative regulation of lipid catabolic process; positive regulation of neuron apoptosis; lipopolysaccharide-mediated signaling pathway; protein kinase B signaling cascade; positive regulation of chronic inflammatory response to antigenic stimulus; regulation of I-kappaB kinase/NF-kappaB cascade; inflammatory response; caspase activation; positive regulation of humoral immune response mediated by circulating immunoglobulin; positive regulation of protein complex disassembly; transformed cell apoptosis; calcium-mediated signaling; MAPKKK cascade; positive regulation of peptidyl-serine phosphorylation; humoral immune response; positive regulation of protein kinase B signaling cascade; positive regulation of programmed cell death; positive regulation of interferon-gamma production; negative regulation of glucose import; positive regulation of protein complex assembly; positive regulation of chemokine biosynthetic process; negative regulation of viral genome replication; protein import into nucleus, translocation; positive regulation of protein kinase activity; activation of MAPKKK activity; response to hypoxia; positive regulation of fever; receptor biosynthetic process; positive regulation of protein amino acid phosphorylation; leukocyte tethering or rolling; negative regulation of myoblast differentiation; regulation of insulin secretion; positive regulation of cytokine secretion

Disease: Asthma, Susceptibility To; Migraine With Or Without Aura, Susceptibility To, 1; Malaria, Susceptibility To