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Small ribosomal subunit biogenesis GTPase RsgA (EC 3.6.1.-)

 RSGA_ECOLI              Reviewed;         350 AA.
P39286; Q2M6E1;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
28-MAR-2018, entry version 151.
RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000255|HAMAP-Rule:MF_01820};
EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820};
Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820,
ECO:0000303|PubMed:15466596}; Synonyms=engC, yjeQ;
OrderedLocusNames=b4161, JW4122;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7610040; DOI=10.1093/nar/23.12.2105;
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the
region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
IDENTIFICATION.
PubMed=9743119; DOI=10.1038/nbt0998-851;
Arigoni F., Talabot F., Peitsch M.C., Edgerton M.D., Meldrum E.,
Allet E., Fish R., Jamotte T., Curchod M.-L., Loferer H.;
"A genome-based approach for the identification of essential bacterial
genes.";
Nat. Biotechnol. 16:851-856(1998).
[5]
PARTIAL PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
SUBUNIT, MASS SPECTROMETRY, MUTAGENESIS OF LYS-220 AND SER-221, AND
GDP-BINDING.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=12220175; DOI=10.1021/bi020355q;
Daigle D.M., Rossi L., Berghuis A.M., Aravind L., Koonin E.V.,
Brown E.D.;
"YjeQ, an essential, conserved, uncharacterized protein from
Escherichia coli, is an unusual GTPase with circularly permuted G-
motifs and marked burst kinetics.";
Biochemistry 41:11109-11117(2002).
[6]
FUNCTION, ASSOCIATION WITH 30S RIBOSOMAL SUBUNIT, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 1-MET--ARG-20 AND SER-221.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=14973029; DOI=10.1128/JB.186.5.1381-1387.2004;
Daigle D.M., Brown E.D.;
"Studies of the interaction of Escherichia coli YjeQ with the ribosome
in vitro.";
J. Bacteriol. 186:1381-1387(2004).
[7]
FUNCTION, ASSOCIATION WITH 30S RIBOSOMAL SUBUNIT, DISRUPTION
PHENOTYPE, AND EFFECT OF ANTIBIOTICS ON GTPASE.
STRAIN=K12;
PubMed=15466596; DOI=10.1093/nar/gkh861;
Himeno H., Hanawa-Suetsugu K., Kimura T., Takagi K., Sugiyama W.,
Shirata S., Mikami T., Odagiri F., Osanai Y., Watanabe D., Goto S.,
Kalachnyuk L., Ushida C., Muto A.;
"A novel GTPase activated by the small subunit of ribosome.";
Nucleic Acids Res. 32:5303-5309(2004).
[8]
FUNCTION, AND EFFECT OF ANTIBIOTICS ON GTPASE ACTIVITY.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15828870; DOI=10.1042/BJ20041873;
Campbell T.L., Daigle D.M., Brown E.D.;
"Characterization of the Bacillus subtilis GTPase YloQ and its role in
ribosome function.";
Biochem. J. 389:843-852(2005).
[9]
FUNCTION, AND GENETIC INTERACTION.
STRAIN=K12;
PubMed=18223068; DOI=10.1128/JB.01744-07;
Campbell T.L., Brown E.D.;
"Genetic interaction screens with ordered overexpression and deletion
clone sets implicate the Escherichia coli GTPase YjeQ in late ribosome
biogenesis.";
J. Bacteriol. 190:2537-2545(2008).
[10]
FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-250.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=21102555; DOI=10.1038/emboj.2010.291;
Goto S., Kato S., Kimura T., Muto A., Himeno H.;
"RsgA releases RbfA from 30S ribosome during a late stage of ribosome
biosynthesis.";
EMBO J. 30:104-114(2011).
[11]
FUNCTION, STRUCTURE BY ELECTRON MICROSCOPY (11.6 ANGSTROMS), AND
DISRUPTION PHENOTYPE.
STRAIN=EB334;
PubMed=21303937; DOI=10.1261/rna.2509811;
Jomaa A., Stewart G., Martin-Benito J., Zielke R., Campbell T.L.,
Maddock J.R., Brown E.D., Ortega J.;
"Understanding ribosome assembly: the structure of in vivo assembled
immature 30S subunits revealed by cryo-electron microscopy.";
RNA 17:697-709(2011).
[12]
FUNCTION, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
298-LYS--ARG-300 AND 320-LYS--ASP-350.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=25904134; DOI=10.1261/rna.049171.114;
Jeganathan A., Razi A., Thurlow B., Ortega J.;
"The C-terminal helix in the YjeQ zinc-finger domain catalyzes the
release of RbfA during 30S ribosome subunit assembly.";
RNA 21:1203-1216(2015).
[13]
FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / BW25113;
PubMed=27382067; DOI=10.1093/nar/gkw613;
Thurlow B., Davis J.H., Leong V., Moraes T.F., Williamson J.R.,
Ortega J.;
"Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly
intermediates of the 30S subunit.";
Nucleic Acids Res. 44:9918-9932(2016).
[14] {ECO:0000244|PDB:2YKR}
STRUCTURE BY ELECTRON MICROSCOPY (9.80 ANGSTROMS) IN GMP-PNP-BOUND
FORM ON THE 30S RIBOSOME, SUBUNIT, AND RRNA-BINDING.
STRAIN=K12 / DH5-alpha;
PubMed=21788480; DOI=10.1073/pnas.1104645108;
Guo Q., Yuan Y., Xu Y., Feng B., Liu L., Chen K., Sun M., Yang Z.,
Lei J., Gao N.;
"Structural basis for the function of a small GTPase RsgA on the 30S
ribosomal subunit maturation revealed by cryoelectron microscopy.";
Proc. Natl. Acad. Sci. U.S.A. 108:13100-13105(2011).
[15] {ECO:0000244|PDB:4A2I}
STRUCTURE BY ELECTRON MICROSCOPY (16.50 ANGSTROMS) OF 35-337 IN
GMP-PNP-BOUND FORM ON THE 30S RIBOSOME, SUBUNIT, AND RRNA-BINDING.
STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
PubMed=21960487; DOI=10.1261/rna.2922311;
Jomaa A., Stewart G., Mears J.A., Kireeva I., Brown E.D., Ortega J.;
"Cryo-electron microscopy structure of the 30S subunit in complex with
the YjeQ biogenesis factor.";
RNA 17:2026-2038(2011).
-!- FUNCTION: One of at least 4 proteins (Era, RbfA, RimM and
RsgA/YjeQ) that assist in the late maturation steps of the
functional core of the 30S ribosomal subunit (PubMed:18223068,
PubMed:21102555, PubMed:21303937, PubMed:25904134,
PubMed:27382067). Binds the 30S subunit contacting the head,
platform, and rRNA helix 44, which may assist the last maturation
stages (PubMed:21788480, PubMed:21960487). Removes RbfA from
mature, but not immature 30S ribosomes in a GTP-dependent manner;
95% removal in the presence of GTP, 90% removal in GMP-PNP and 65%
removal in the presence of GDP (PubMed:21102555, PubMed:25904134).
Circulary permuted GTPase that catalyzes rapid hydrolysis of GTP
with a slow catalytic turnover (PubMed:12220175). Dispensible for
viability, but important for overall fitness. The intrinsic GTPase
activity is stimulated by the presence of 30S (160-fold increase
in kcat) or 70S (96-fold increase in kcat) ribosomes
(PubMed:14973029). Mature 30S ribosomes stimulate intrinsic GTPase
more than do immature 30S ribosomes (PubMed:25904134). Ribosome-
associated GTPase activity is stimulated by RbfA
(PubMed:21102555). The GTPase is inhibited by aminoglycoside
antibiotics such as neomycin and paromycin (PubMed:15466596)
streptomycin and spectinomycin (PubMed:15828870). This inhibition
is not due to competition for binding sites on the 30S or 70S
ribosome (PubMed:15828870). {ECO:0000269|PubMed:12220175,
ECO:0000269|PubMed:14973029, ECO:0000269|PubMed:15466596,
ECO:0000269|PubMed:15828870, ECO:0000269|PubMed:21102555,
ECO:0000269|PubMed:25904134, ECO:0000305|PubMed:18223068,
ECO:0000305|PubMed:27382067}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_01820};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_01820};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.41 mM for GTP {ECO:0000269|PubMed:12220175};
KM=1.0 mM for dATP {ECO:0000269|PubMed:12220175};
KM=1.2 mM for ATP {ECO:0000269|PubMed:12220175};
KM=1.3 mM for ITP {ECO:0000269|PubMed:12220175};
KM=1.6 mM for dGTP {ECO:0000269|PubMed:12220175};
KM=2.4 mM for CTP {ECO:0000269|PubMed:12220175};
Note=Measured in the absence of 30S ribosomes, kcat is 8.1
hour(-1) for GTP, 5.2 for dATP, 3.5 for ATP, 4.5 for ITP, 7.1
for dGTP, 2.1 for CTP. {ECO:0000269|PubMed:12220175};
-!- SUBUNIT: Monomer (Probable). All of the protein is associated with
ribosomes; the ratio is substoichiometric at 1:200 RsgA/ribosome
(PubMed:14973029). Association is tightest with the 30S subunit in
the presence of the non-hydrolyzable GTP analog GMP-PNP
(PubMed:14973029, PubMed:15466596). 2 cryoelectron microscopy
(cryo-EM) structures in complex with 30S ribosomes have been
resolved; the protein is determined to bind to different but
partially overlapping regions of the 30S ribosomal subunit
(PubMed:21788480, PubMed:21960487). One cryo-EM study suggests it
contacts ribosomal proteins S3, S12 and S13 as well as 16S rRNA
(PubMed:21788480). Another cryo-EM study shows it to bind 16S
rRNA, no ribosomal proteins, and to cover the sites of
intersubunit bridges B2a, B3 and B7a (PubMed:21960487). Has a
significant preference for mature versus immature 30S ribosomes in
the presence of GMP-PNP (PubMed:21102555, PubMed:27382067).
Another study shows it binds equally well to mature and immature
30S ribosomal subunits in the presence of GMP-PNP
(PubMed:25904134). {ECO:0000269|PubMed:14973029,
ECO:0000269|PubMed:15466596, ECO:0000269|PubMed:21102555,
ECO:0000269|PubMed:21788480, ECO:0000269|PubMed:21960487,
ECO:0000269|PubMed:25904134, ECO:0000269|PubMed:27382067,
ECO:0000305|PubMed:12220175}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01820,
ECO:0000269|PubMed:14973029}. Note=Associates with 30S ribosomes
(PubMed:14973029). {ECO:0000269|PubMed:14973029}.
-!- DOMAIN: Has 3 domains; an N-terminal OB-like domain (about
residues 1-100), a central, circularly permutated GTPase module
(residues 104-270) and the C-terminal zinc-finger domain (residues
280 to 350) (PubMed:25904134). The C-terminal domain has 2
regions; the zinc-binding domain (residues 287-319) is required
for binding to 30S ribosomes while the extreme C-terminus
(residues 320-350) helps remove RbfA from the mature 30S subunit.
{ECO:0000305|PubMed:25904134}.
-!- MASS SPECTROMETRY: Mass=36830; Method=Electrospray; Range=21-350;
Note=Overexpressed protein is missing the first 20 residues.;
Evidence={ECO:0000269|PubMed:12220175};
-!- DISRUPTION PHENOTYPE: Reduced growth rate, reduced 70S ribosomes,
accumulation of 17S rRNA (the precursor of 16S rRNA)
(PubMed:15466596, PubMed:21303937, PubMed:25904134,
PubMed:27382067). Ribosomal proteins S2 and S21 not found in 30S
subunits, decreased S3 and RbfA in 30S subunits, distortion of
rRNA helix 44 near the decoding center (PubMed:21303937,
PubMed:27382067). The phenotype is partially suppressed by
overexpression of a number of genes involved in ribosome function,
including infB, era and ksgA (PubMed:15466596). Double rbfA-rsgA
deletion mutants have the same phenotype as single mutants
(PubMed:21102555). Single rgsA deletion is suppressed by a number
of mutants in RbfA but not by wild-type RbfA; in all the RbfA
mutants less RbfA is found bound to the 30S ribosome
(PubMed:21102555). {ECO:0000269|PubMed:15466596,
ECO:0000269|PubMed:21102555, ECO:0000269|PubMed:21303937,
ECO:0000269|PubMed:25904134, ECO:0000269|PubMed:27382067}.
-!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
RsgA subfamily. {ECO:0000255|HAMAP-Rule:MF_01820}.
-!- CAUTION: Was initially characterized with a propeptide of 20
residues; this is now thought to be the result of in vitro
proteolysis when the protein is overexpressed (PubMed:12220175,
PubMed:14973029). {ECO:0000305|PubMed:12220175,
ECO:0000305|PubMed:14973029}.
-!- SEQUENCE CAUTION:
Sequence=AAA97060.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U14003; AAA97060.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC77121.2; -; Genomic_DNA.
EMBL; AP009048; BAE78165.1; -; Genomic_DNA.
PIR; S56389; S56389.
RefSeq; NP_418585.4; NC_000913.3.
RefSeq; WP_000041964.1; NZ_LN832404.1.
PDB; 2YKR; EM; 9.80 A; W=1-350.
PDB; 4A2I; EM; 16.50 A; V=35-337.
PDB; 5NO2; EM; 5.16 A; Z=34-346.
PDB; 5NO3; EM; 5.16 A; Z=34-346.
PDB; 5NO4; EM; 5.16 A; Z=34-346.
PDB; 5UZ4; EM; 5.80 A; Z=6-339.
PDBsum; 2YKR; -.
PDBsum; 4A2I; -.
PDBsum; 5NO2; -.
PDBsum; 5NO3; -.
PDBsum; 5NO4; -.
PDBsum; 5UZ4; -.
ProteinModelPortal; P39286; -.
SMR; P39286; -.
BioGrid; 4261080; 609.
DIP; DIP-12581N; -.
IntAct; P39286; 33.
MINT; P39286; -.
STRING; 316385.ECDH10B_4356; -.
EPD; P39286; -.
PaxDb; P39286; -.
PRIDE; P39286; -.
EnsemblBacteria; AAC77121; AAC77121; b4161.
EnsemblBacteria; BAE78165; BAE78165; BAE78165.
GeneID; 948674; -.
KEGG; ecj:JW4122; -.
KEGG; eco:b4161; -.
PATRIC; fig|1411691.4.peg.2537; -.
EchoBASE; EB2372; -.
EcoGene; EG12479; rsgA.
eggNOG; ENOG4105E06; Bacteria.
eggNOG; COG1162; LUCA.
HOGENOM; HOG000006957; -.
InParanoid; P39286; -.
KO; K06949; -.
OMA; FRDCKHL; -.
PhylomeDB; P39286; -.
BioCyc; EcoCyc:G7841-MONOMER; -.
BioCyc; MetaCyc:G7841-MONOMER; -.
SABIO-RK; P39286; -.
EvolutionaryTrace; P39286; -.
PRO; PR:P39286; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0019003; F:GDP binding; IDA:EcoCyc.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:EcoCyc.
CDD; cd01854; YjeQ_EngC; 1.
HAMAP; MF_01820; GTPase_RsgA; 1.
InterPro; IPR030378; G_CP_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
InterPro; IPR010914; RsgA_GTPase_dom.
PANTHER; PTHR32120; PTHR32120; 1.
Pfam; PF03193; RsgA_GTPase; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00157; TIGR00157; 1.
PROSITE; PS50936; ENGC_GTPASE; 1.
PROSITE; PS51721; G_CP; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding;
Zinc.
CHAIN 1 350 Small ribosomal subunit biogenesis GTPase
RsgA.
/FTId=PRO_0000008149.
DOMAIN 104 273 CP-type G.
NP_BIND 160 163 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}.
NP_BIND 214 222 GTP. {ECO:0000255|HAMAP-Rule:MF_01820}.
REGION 1 113 Necessary for association with the
ribosome and for stimulation of GTPase
activity by 30S ribosomes.
{ECO:0000269|PubMed:14973029}.
REGION 1 20 Necessary for GMP-PNP-dependent
association with the 30S ribosomal
subunit. {ECO:0000269|PubMed:14973029,
ECO:0000305|PubMed:12220175,
ECO:0000305|PubMed:21788480}.
REGION 287 319 Required for binding to mature and
immature 30S ribosomes.
{ECO:0000269|PubMed:25904134}.
REGION 320 350 Required to remove RbfA from mature 30S
ribosomes. {ECO:0000269|PubMed:25904134}.
METAL 297 297 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}.
METAL 302 302 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}.
METAL 304 304 Zinc; via pros nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01820}.
METAL 310 310 Zinc. {ECO:0000255|HAMAP-Rule:MF_01820}.
MUTAGEN 1 20 Missing: Loss of GMP-PNP-dependent
association with 30S ribosomal subunit,
increased association with 50S and 70S
ribosomes. {ECO:0000269|PubMed:14973029}.
MUTAGEN 220 220 K->A: Reduction in GTPase activity, 38%
of wild-type kcat for GTP. Strong
reduction, 5.2% of wild-type kcat for
GTP; when associated with A-221.
{ECO:0000269|PubMed:12220175}.
MUTAGEN 221 221 S->A: Reduction in GTPase activity, 22%
of wild-type kcat for GTP. GTPase
activity not stimulated by 30S ribosomes
(PubMed:14973029). Strong reduction, 5.2%
of wild-type kcat for GTP; when
associated with A-220.
{ECO:0000269|PubMed:12220175,
ECO:0000269|PubMed:14973029}.
MUTAGEN 250 250 T->A: Loss of GTPase activity, does not
dissociate RbfA.
{ECO:0000269|PubMed:21102555}.
MUTAGEN 298 300 KYR->AYA: About 2-fold decreased binding
to mature and immature 30S ribosomes,
GTPase activity stimulated by ribosomes.
{ECO:0000269|PubMed:25904134}.
MUTAGEN 320 350 Missing: Slightly increased specific
binding to mature and immature 30S
ribosomes, GTPase activity not stimulated
by ribosomes. No longer removes RbfA from
mature 30S ribosomes, increases RbfA-
binding about 5-fold. Does not complement
a deletion mutant in vivo, fewer 70S
ribosomes, slower growth than deletion
mutant. {ECO:0000269|PubMed:25904134}.
SEQUENCE 350 AA; 39193 MW; DEB14E36D2F0F378 CRC64;
MSKNKLSKGQ QRRVNANHQR RLKTSKEKPD YDDNLFGEPD EGIVISRFGM HADVESADGD
VHRCNIRRTI RSLVTGDRVV WRPGKPAAEG VNVKGIVEAV HERTSVLTRP DFYDGVKPIA
ANIDQIVIVS AILPELSLNI IDRYLVACET LQIEPIIVLN KIDLLDDEGM AFVNEQMDIY
RNIGYRVLMV SSHTQDGLKP LEEALTGRIS IFAGQSGVGK SSLLNALLGL QKEILTNDIS
DNSGLGQHTT TAARLYHFPH GGDVIDSPGV REFGLWHLEP EQITQGFVEF HDYLGLCKYR
DCKHDTDPGC AIREAVEEGK IAETRFENYH RILESMAQVK TRKNFSDTDD


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CSB-EL007636MO Mouse Ribosomal RNA small subunit methyltransferase NEP1(EMG1) ELISA kit 96T
CSB-EL007636HU Human Ribosomal RNA small subunit methyltransferase NEP1(EMG1) ELISA kit 96T
CSB-EL007636MO Mouse Ribosomal RNA small subunit methyltransferase NEP1(EMG1) ELISA kit SpeciesMouse 96T
CSB-EL007636HU Human Ribosomal RNA small subunit methyltransferase NEP1(EMG1) ELISA kit SpeciesHuman 96T
NEP1_MOUSE ELISA Kit FOR Ribosomal RNA small subunit methyltransferase NEP1; organism: Mouse; gene name: Emg1 96T
201-20-5046 RRP9{ribosomal RNA processing 9, small subunit (SSU) processome component, homolog (yeast)}rabbit.pAb 0.2ml
EIAAB35182 Mouse,Mus musculus,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,Rsl24d1
EIAAB35181 C15orf15,Homo sapiens,Human,My024,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,RPL24L,RSL24D1


 

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