Positive control:
Lane 1: Jurkat cell lysate
Lane 2: PC-12 cell lysate
Applications
-
WB
-
ICC
-
IHC-P
REACTIVITY
-
Human
-
Mouse
-
Rat
SPECIFICATIONS
Product Type
Recombinant Rabbit monoclonal primary
Product Name
Recombinant RPS3 Monoclonal Antibody (ET1601-27)
Immunogen
Synthetic peptide within human rps3 aa 130-160.
Host
Rabbit
Positive Control
Jurkat cell lysate, PC-12 cell lysate, N2A, SH-SY5Y, human kidney tissue, mouse lung tissue.
Conjugation
Unconjugated
Clonality
Monoclonal
Clone Number
SA46-08
PROPERTIES
Form
Liquid
Storage Condition
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
Storage Buffer
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Concentration
1 ug/ul
PURIFICATION
Protein A affinity purified.
MOLECULAR WEIGHT
27 kDa
Isotype
IgG
APPLICATION DILUTION
-
WB
-
1:500-1:1,000
-
ICC
-
1:50-1:200
-
IHC-P
-
1:50-1:200
TARGET
UNIPROT #
PROTEIN NAME
RPS3
SYNONYMS
40S ribosomal protein S3 antibody; fb13d09 antibody; FLJ26283 antibody; FLJ27450 antibody; IMR 90 ribosomal protein S3 antibody; MGC56088 antibody; MGC87870 antibody; OTTHUMP00000229804 antibody; OTTHUMP00000229805 antibody; OTTHUMP00000229874 antibody; OTTHUMP00000229877 antibody; OTTHUMP00000229878 antibody; OTTHUMP00000229879 antibody; OTTHUMP00000229880 antibody; OTTHUMP00000229882 antibody; OTTHUMP00000229883 antibody; OTTHUMP00000229886 antibody; Ribosomal protein S3 antibody; rps3 antibody; RS3_HUMAN antibody; S3 antibody; wu:fb13d09 antibody; zgc:56088 antibody
SEQUENCE SIMILARITIES
Belongs to the universal ribosomal protein uS3 family.
POST-TRANSLATIONAL MODIFICATION
Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly.; Sumoylation by SUMO1 enhances protein stability through increased resistance to proteolysis. Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.; Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase. Phosphorylation by PRKCD occurs on a non-ribosomal-associated form which results in translocation of RPS3 to the nucleus and enhances its endonuclease activity. Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3. Phosphorylation by MAPK is required for translocation to the nucleus following exposure of cells to DNA damaging agents such as hydrogen peroxide. Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation, enhances RPS3 endonuclease activity and suppresses RPS3-induced neuronal apoptosis.; Ubiquitinated. This is prevented by interaction with HSP90 which stabilizes the protein. Monoubiquitinated at Lys-214 by ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide.
SUBCELLULAR LOCATION
Cytoplasm, Nucleus, Mitochondrion inner membrane
FUNCTION
Ribosomal subunits are synthesized in the nucleus, and mature 40S and 60S subunits are exported stoichiometrically into the cytoplasm. Both 40S and 60S subunits are composed of four RNA species and approximately 80 structurally distinct proteins. Mitochondrial ribosomes consist of a small 28S subunit and a large 39S subunit. Ribosomal proteins have the ability to pass through the nuclear envelope in the native state, making them the largest of the structures accommodated by the nuclear pore complexes. The nuclear export of ribosomal subunits is a unidirectional, saturable and energy-dependent process. Ribosomal Protein S3 a member of the 40S subunit and plays a role in translation and ribosome maturation. Specifically, Ribosomal Protein S3 mediates the formation of the mRNA binding site 3’ of the codon in the decoding site. In addition, Ribosomal Protein S3 is involved in DNA damage recognition as shown by its affinity for abasic sites and 7,8-dihydro-8-oxoguanine residues and its interaction with human base excision repair (BER) proteins OGG1 and Ref-1.