|Antigen||Non-Metastatic Cells 1, Protein (NM23A) Expressed in (NME1) Antibodies|
|Epitope||AA 44-152 Alternatives|
|Reactivity||Chicken, Human, Mouse (Murine), Rat (Rattus) Alternatives|
|Conjugate||This NME1 antibody is un-conjugated Alternatives|
Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
|3 references available|
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Product Details anti-NME1 AntibodyTarget Details NME1 Application Details Handling References for anti-NME1 antibody (ABIN967854) Images
|Cross-Reactivity||Mouse (Murine), Rat (Rattus), Chicken|
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
|Purification||The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.|
|Immunogen||Human Nm23 aa. 44-152|
Target Details NME1Product Details anti-NME1 Antibody Application Details Handling References for anti-NME1 antibody (ABIN967854) Images back to top
|Alternative Name||Nm23 (NME1 Antibody Abstract)|
|Background||Nm23 is a potential metastasis suppressor protein whose expression is either reduced, altered (by mutation), or amplified in various types of metastatic carcinomas. Two human gene homologues, nm23-H1 and nm23-H2, encode 17 kDa proteins that are 90% identical. Nm23 proteins possess a nucleoside diphosphate kinase (NDPK) activity. This enzymatic activity catalyzes the synthesis of non-adenine-containing nucleoside triphosphates from nucleoside diphosphates via a phosphorylated enzyme intermediate. In addition, Nm23 inhibits differentiation, interacts with GTP-binding (GAP) proteins, autophosphorylates serine residues, and binds to DNA. The biochemical mechanisms by which Nm23 affects tumor metastatic potential have yet to be determined. In murine melanoma cell lines, serine 44 is the major site of autophosphorylation on Nm23-1. This acid-stable phosphorylation of Nm23 is inhibited in vitro by cAMP and in vivo by forskolin. These data indicate that this serine phosphorylation is regulated via some cAMP-dependent event in signal transduction. In addition, it has been shown that the Nm23-H2 protein is identical to the c-myc transcription factor PuF. This suggests that some of the cellular effects of Nm23 are mediated by its transcriptional regulatory function, while others are mediated by its NDPK activity.|
|Molecular Weight||17 kDa|
|Pathways||Apoptosis, Nucleotide Phosphorylation, Carbohydrate Homeostasis, Ribonucleoside Biosynthetic Process|
Application DetailsProduct Details anti-NME1 Antibody Target Details NME1 Handling References for anti-NME1 antibody (ABIN967854) Images back to top
Related Products: ABIN968535, ABIN967389
|Restrictions||For Research Use only|
HandlingProduct Details anti-NME1 Antibody Target Details NME1 Application Details References for anti-NME1 antibody (ABIN967854) Images back to top
|Buffer||Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.|
|Precaution of Use||This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.|
|Storage Comment||Store undiluted at -20° C.|
References for anti-NME1 antibody (ABIN967854)Product Details anti-NME1 Antibody Target Details NME1 Application Details Handling Images back to top
|Product cited in:||
MacDonald, De la Rosa, Benedict, Freije, Krutsch, Steeg: "A serine phosphorylation of Nm23, and not its nucleoside diphosphate kinase activity, correlates with suppression of tumor metastatic potential." in: The Journal of biological chemistry, Vol. 268, Issue 34, pp. 25780-9, 1994
Postel, Ferrone: "Nucleoside diphosphate kinase enzyme activity of NM23-H2/PuF is not required for its DNA binding and in vitro transcriptional functions." in: The Journal of biological chemistry, Vol. 269, Issue 12, pp. 8627-30, 1994
Rosengard, Krutzsch, Shearn, Biggs, Barker, Margulies, King, Liotta, Steeg: "Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development." in: Nature, Vol. 342, Issue 6246, pp. 177-80, 1989
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