|Tested species reactivity||Human, Mouse|
|Published species reactivity||Human, Not Applicable|
|Host / Isotype||Mouse / IgG2b, kappa|
|Immunogen||Synthetic peptide derived from the internal region of the human nucleolin protein|
|Storage buffer||PBS, pH 7.4|
|Contains||0.1% sodium azide|
|Tested Applications||Dilution *|
|ELISA (ELISA)||0.1-1.0 ug/ml|
|Flow Cytometry (Flow)||3-5 µg/10^6 cells|
|Immunocytochemistry (ICC)||5-10 µg/ml|
|Immunofluorescence (IF)||5-10 ug/ml|
|Western Blot (WB)||1-3 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Nucleolin, which is identical to human DNA helicase IV, is a major nucleolar phosphoprotein which is associated with preribosomal RNA and is implicated in the early stage of preribosomal RNP assembly and processing. This 100 kDa protein has three major domains: a N-terminal domain comprised of long acidic stretches interspersed with basic repeats, similar to the structure of a high mobility group-type protein, a central domain that contains four RNA binding elements, a C-terminal domain approximately 85 amino acids long that is rich in glycine, arginine, and phenylalanine residues. Nucleolin fluctuates in parallel to DNA synthesis; intact 100 kDa protein is the major species in actively dividing cells, whereas the degraded forms are relativley abundant in nondividing cells. Nucleolin can unwind RNA-RNA duplexes, as well as DNA-DNA and DNA-RNA duplexes. Nucleolin also interacts directly with DNA topoisomerase I. It is located mainly in dense fibrillar regions of the nucleolus. Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and preribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. It interacts with APTX and contains 4 RNA recognition motif (RRM) domains.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
|Not Applicable||Not Cited||
Morphological, Biochemical, and Functional Study of Viral Replication Compartments Isolated from Adenovirus-Infected Cells.
39-6400 was used in immunocytochemistry and western blot to characterize viral replication compartments isolated from adenovirus-infected cells for biochemical, morphological, and functional properties
|Hidalgo P,Anzures L,Hernández-Mendoza A,Guerrero A,Wood CD,Valdés M,Dobner T,Gonzalez RA||Journal of virology (90:3411)||2016|
Molecular evolution and in vitro characterization of Botryllus histocompatibility factor.
39-6400 was used in immunocytochemistry to study allorecognition using Botryllus schlosseri.
|Taketa DA,Nydam ML,Langenbacher AD,Rodriguez D,Sanders E,De Tomaso AW||Immunogenetics (67:605)||2015|
Nucleophosmin delocalization in thyroid tumour cells.
39-6400 was used in immunocytochemistry to examine the localization of nucleophosmin in thyroid tumors.
|Pianta A,Puppin C,Passon N,Franzoni A,Romanello M,Tell G,Di Loreto C,Bulotta S,Russo D,Damante G||Endocrine pathology (22:18)||2011|
Two novel NPM1 mutations in a therapy-responder AML patient.
39-6400 was used in immunocytochemistry to describe a case of a therapy-responder acute myeloid leukemia patient bearing two novel NPM1 mutations
|Pianta A,Fabbro D,Damiani D,Tiribelli M,Fanin R,Franzoni A,Romanello M,Tell G,Di Loreto C,Damante G||Hematological oncology (28:151)||2010|
||Nucleolar accumulation of APE1 depends on charged lysine residues that undergo acetylation upon genotoxic stress and modulate its BER activity in cells.||Lirussi L,Antoniali G,Vascotto C,D'Ambrosio C,Poletto M,Romanello M,Marasco D,Leone M,Quadrifoglio F,Bhakat KK,Scaloni A,Tell G||Molecular biology of the cell (23:4079)||2012|
|Human||Not Cited||Secretome-based identification and characterization of potential biomarkers in thyroid cancer.||Kashat L,So AK,Masui O,Wang XS,Cao J,Meng X,Macmillan C,Ailles LE,Siu KW,Ralhan R,Walfish PG||Journal of proteome research (9:5757)||2010|
|Human||Not Cited||Nucleolar accumulation of APE1 depends on charged lysine residues that undergo acetylation upon genotoxic stress and modulate its BER activity in cells.||Lirussi L,Antoniali G,Vascotto C,D'Ambrosio C,Poletto M,Romanello M,Marasco D,Leone M,Quadrifoglio F,Bhakat KK,Scaloni A,Tell G||Molecular biology of the cell (23:4079)||2012|