Human Non POU Domain Containing Octamer Binding Protein (NONO) ELISA Kit (96T)

Human Non POU Domain Containing Octamer Binding Protein (NONO) ELISA Kit (96T)

Catalog #: TD3945
Availability: In Stock
¥649.00
Detection range: 0.312-20ng/mL    
Sensitivity: 0.126ng/mL    
Type: Traditional NONO ELISA kit    
Synonyms: P54; NMT55; NRB54; P54NRB; Nuclear RNA-Binding Protein 54-kD; 54 kDa nuclear RNA- and DNA-binding protein; DNA-binding p52/p100 complex, 52 kDa subunit
Species: Human
Sample type: tissue homogenates, cell lysates or other biological fluids.
Experimental method: Sandwich
Shelf life: 12 months
Gene ID: 4841
UniProt ID: Q15233
Components: 1. Pre-coated, ready to use 96-well strip plate 1
2. Plate sealer for 96 wells 2
3. Standard 2
4. Diluents buffer: 1×45 mL
5. Detection Reagent A: 1×120 μL
6. Detection Reagent B: 1×120 μL
7. TMB Substrate: 1×9 mL
8. Stop Solution: 1×6 mL
9. Wash Buffer (30× concentrate): 1×20 mL




Background

The secreted polypeptide, encoded by this gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, this protein may have a principal role in creating morphogenic gradients. The protein appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of the ortholog suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as this gene. All of these mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of this human gene is highly homologous to that of Xenopus, rat and mouse.

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