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ELK Biotechnology

SKU:EA023

COX1/Cyclooxygenase 1  Rabbit Polyclonal Antibody

COX1/Cyclooxygenase 1  Rabbit Polyclonal Antibody

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COX1/Cyclooxygenase 1  Rabbit Polyclonal Antibody

Overview

Product name: COX1/Cyclooxygenase 1 Rabbit pAb
Reactivity: Human
Alternative Names: N/A
Source: Rabbit
Applications: WB, IHC
Species: Human
Recommended dilutions: WB 1:1,000 IHC 1:100
Immunogen: Synthetic Peptide
Storage: PBS with 0.02% sodium azide and 50% glycerol pH 7.4. Store at -20°C. Avoid repeated freeze-thaw cycles.
Clonality: Polyclonal
Isotype: IgG
Concentration: 1mg/ml
Observed band: 70kDa
GeneID(Human): 5742
Human Swiss-Prot No: P23219
Cellular localization: Endoplasmic reticulum, Membrane, Microsome
Background: Cyclooxygenase-1 (COX-1), also known as prostaglandin G/H synthase 1, prostaglandin-endoperoxide synthase 1 or prostaglandin H2 synthase 1, is an enzyme that in humans is encoded by the PTGS1 gene. There are two isozymes of COX encoded by distinct gene products: a constitutive COX-1 (this enzyme) and an inducible COX-2, which differ in their regulation of expression and tissue distribution. The expression of these two transcripts is differentially regulated by relevant cytokines and growth factors. A splice variant of COX-1 termed COX-3 was identified in the CNS of dogs, but does not result in a functional protein in humans. Two smaller COX-1-derived proteins (the partial COX-1 proteins PCOX-1A and PCOX-1B) have also been discovered, but their precise roles are yet to be describedGalectin 3 is one of the more extensively studied members of this family and is a 30 kDa protein. Due to a C-terminal carbohydrate binding site, Galectin 3 is capable of binding IgE and mammalian cell surfaces only when homodimerized or homooligomerized. Galectin 3 is normally distributed in epithelia of many organs, in various inflammatory cells, including macrophages, as well as dendritic cells and Kupffer cells. The expression of this lectin is up-regulated during inflammation, cell proliferation, cell differentiation and through trans-activation by viral proteins. 
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