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- goat polyclonal IgG, 200 µg/ml
- epitope mapping at the N-terminus of OCM of human origin
- recommended for detection of Oncomodulin of mouse, rat and human origin and Oncomodulin-like of human origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, canine and porcine
- blocking peptide, sc-7446 P
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OCM Background Information The family of EF-hand type Ca2+-binding proteins includes calbindin (previously designated vitamin D-dependent Ca2+-binding protein), S-100å and ∫, calgranulins A (also designated MRP8), B (also designated MRP14) and C (S-100 like proteins) and the parvalbumin family members, including parvalbumin å and parvalbumin ∫ , also designated oncomodulin (OCM). Structurally and evolutionarily conserved, parvalbumin å and OCM proteins are distinct in expression and function. Parvalbumin å, also designated parvalbumin (PV), is most abundantly expressed in fast-contracting muscles, with lower expression levels in brain and some endocrine tissues, including kidney and parathyroid. Research indicates that parvalbumin å plays a significant role in muscle relaxation. OCM was originally thought to have expression restricted to neoplastic tissues, early embryonic cells and certain tumor cell lines. Recent research shows that OCM is also expressed and secreted by macrophages where, in the retina it binds to retinal ganglion cells (RGCs) and functions to promote axon regeneration. OCM has also been detected in the auditory sensory cells of the organ of Corti in mammals. In humans, two different loci on chromosome 7 have been identified as OCM and OCML. These genes encode proteins 109 amino acids in length which share 99% sequence identity.
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OCM (N-19)
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OCM (N-19): sc-7446. Immunofluorescence staining of methanol-fixed ZR-75-1 cells showing cytoplasmic localization.
OCM (N-19): sc-7446. Western blot analysis of OCML expression in non-transfected: sc-117752 (A) and human OCML transfected: sc-372089 (B) 293T whole cell lysates.
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