Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

L-lactate dehydrogenase B chain (LDH-B) (EC 1.1.1.27) (LDH heart subunit) (LDH-H) (Renal carcinoma antigen NY-REN-46)

 LDHB_HUMAN              Reviewed;         334 AA.
P07195;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 221.
RecName: Full=L-lactate dehydrogenase B chain;
Short=LDH-B;
EC=1.1.1.27;
AltName: Full=LDH heart subunit;
Short=LDH-H;
AltName: Full=Renal carcinoma antigen NY-REN-46;
Name=LDHB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2930497; DOI=10.1042/bj2570921;
Takeno T., Li S.S.-L.;
"Structure of the human lactate dehydrogenase B gene.";
Biochem. J. 257:921-924(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell;
PubMed=3435492; DOI=10.1042/bj2480933;
Sakai I., Sharief F.S., Pan Y.-C.E., Li S.S.-L.;
"The cDNA and protein sequences of human lactate dehydrogenase B.";
Biochem. J. 248:933-936(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-23; 44-58; 78-100; 108-113; 120-127; 159-170;
234-244; 271-279 AND 300-329, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAY-2005) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 8-23; 44-58; 78-91; 108-113; 120-127; 159-170;
234-244; 280-299 AND 300-318, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[6]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND TYR-240, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-58; LYS-119 AND
LYS-329, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADH AND
SUBSTRATE ANALOG, AND HOMOTETRAMERIZATION.
PubMed=11276087;
DOI=10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#;
Read J.A., Winter V.J., Eszes C.M., Sessions R.B., Brady R.L.;
"Structural basis for altered activity of M- and H-isozyme forms of
human lactate dehydrogenase.";
Proteins 43:175-185(2001).
[16]
VARIANT LDHBD GLU-7.
PubMed=8314553; DOI=10.1007/BF00217765;
Maekawa M., Sudo K., Kitajima M., Matsuura Y., Li S.S.-L., Kanno T.;
"Analysis of a genetic mutation in an electrophoretic variant of the
human lactate dehydrogenase-B(H) subunit.";
Hum. Genet. 91:423-426(1993).
[17]
VARIANTS LDHBD GLU-35; VAL-171 AND LEU-175.
PubMed=8462975; DOI=10.1007/BF00222718;
Maekawa M., Sudo K., Kitajima M., Matsuura Y., Li S.S.-L., Kanno T.;
"Detection and characterization of new genetic mutations in
individuals heterozygous for lactate dehydrogenase-B(H) deficiency
using DNA conformation polymorphism analysis and silver staining.";
Hum. Genet. 91:163-168(1993).
[18]
VARIANTS LDHBD ARG-129 AND HIS-172.
PubMed=1587525; DOI=10.1007/BF00217116;
Sudo K., Maekawa M., Tomonaga A., Tsukada T., Nakayama T.,
Kitamura M., Li S.S.-L., Kanno T., Toriumi J.;
"Molecular characterization of genetic mutations in human lactate
dehydrogenase (LDH) B (H) variant.";
Hum. Genet. 89:158-162(1992).
[19]
VARIANT LDHBD HIS-172.
PubMed=2334429; DOI=10.1016/0006-291X(90)92373-8;
Sudo K., Maekawa M., Ikawa S., Machida K., Kitamura M., Li S.S.-L.;
"A missense mutation found in human lactate dehydrogenase-B (H)
variant gene.";
Biochem. Biophys. Res. Commun. 168:672-676(1990).
[20]
VARIANT LDHBD VAL-322.
Maekawa M., Sudo K., Fujita K., Yoshioka N., Sakurabayashi I.,
Li S.S.-L., Kanno T.;
"DNA analysis of slow type of electrophoretic lactate dehydrogenase
B(H) variant.";
Seibutsu Butsuri Kagaku 38:25-29(1994).
[21]
VARIANT LDHBD TRP-107.
PubMed=8611651; DOI=10.1016/0925-4439(95)00089-5;
Shonnard G.C., Hud N.V., Mohrenweiser H.W.;
"Arginine to tryptophan substitution in the active site of a human
lactate dehydrogenase variant -- LDHB GUA1: postulated effects on
subunit structure and catalysis.";
Biochim. Biophys. Acta 1315:9-14(1996).
[22]
VARIANT LDHBD ASN-223 DEL.
PubMed=10211631; DOI=10.1016/S0009-9120(98)00097-6;
Sudo K., Maekawa M., Houki N., Okuda T., Akizuki S., Magara T.,
Kawano K.;
"A novel in-frame deletion mutation in a case of lactate dehydrogenase
(LD) H subunit deficiency showing an atypical LD isoenzyme pattern in
serum and erythrocytes.";
Clin. Biochem. 32:137-141(1999).
[23]
VARIANT LDHBD PRO-172.
PubMed=9929983; DOI=10.1007/s100380050111;
Hidaka K., Ueda N., Hirata I., Watanabe Y., Minatogawa Y., Iuchi I.;
"First case of missense mutation (LDH-H:R171P) in exon 4 of the
lactate dehydrogenase gene detected in a Japanese patient.";
J. Hum. Genet. 44:69-72(1999).
[24]
VARIANT LDHBD GLU-69.
PubMed=11509017; DOI=10.1006/mgme.2001.3203;
Takatani T., Takaoka N., Tatsumi M., Kawamoto H., Okuno Y., Morita K.,
Masutani T., Murakawa K., Okamoto Y.;
"A novel missense mutation in human lactate dehydrogenase b-subunit
gene.";
Mol. Genet. Metab. 73:344-348(2001).
-!- CATALYTIC ACTIVITY:
Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
EC=1.1.1.27;
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11276087}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-358748, EBI-358748;
Q93050:ATP6V0A1; NbExp=2; IntAct=EBI-358748, EBI-2891238;
P00338-3:LDHA; NbExp=8; IntAct=EBI-358748, EBI-10195200;
Q5S007:LRRK2; NbExp=2; IntAct=EBI-358748, EBI-5323863;
P50542:PEX5; NbExp=3; IntAct=EBI-358748, EBI-597835;
P54274:TERF1; NbExp=2; IntAct=EBI-358748, EBI-710997;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DISEASE: Lactate dehydrogenase B deficiency (LDHBD) [MIM:614128]:
A condition with no deleterious effects on health. LDHBD is of
interest to laboratory medicine mainly because it can cause
misdiagnosis in those disorders in which elevation of serum LDH is
expected. {ECO:0000269|PubMed:10211631,
ECO:0000269|PubMed:11509017, ECO:0000269|PubMed:1587525,
ECO:0000269|PubMed:2334429, ECO:0000269|PubMed:8314553,
ECO:0000269|PubMed:8462975, ECO:0000269|PubMed:8611651,
ECO:0000269|PubMed:9929983, ECO:0000269|Ref.20}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Lactate dehydrogenase entry;
URL="https://en.wikipedia.org/wiki/Lactate_dehydrogenase";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Another dark horse
- Issue 109 of September 2009;
URL="https://web.expasy.org/spotlight/back_issues/109";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X13794; CAA32033.1; -; Genomic_DNA.
EMBL; X13795; CAA32033.1; JOINED; Genomic_DNA.
EMBL; X13796; CAA32033.1; JOINED; Genomic_DNA.
EMBL; X13797; CAA32033.1; JOINED; Genomic_DNA.
EMBL; X13798; CAA32033.1; JOINED; Genomic_DNA.
EMBL; X13799; CAA32033.1; JOINED; Genomic_DNA.
EMBL; X13800; CAA32033.1; JOINED; Genomic_DNA.
EMBL; Y00711; CAA68701.1; -; mRNA.
EMBL; BC002362; AAH02362.1; -; mRNA.
EMBL; BC015122; AAH15122.1; -; mRNA.
EMBL; BC071860; AAH71860.1; -; mRNA.
CCDS; CCDS8691.1; -.
PIR; S02795; DEHULH.
RefSeq; NP_001167568.1; NM_001174097.2.
RefSeq; NP_001302466.1; NM_001315537.1.
RefSeq; NP_002291.1; NM_002300.7.
UniGene; Hs.446149; -.
PDB; 1I0Z; X-ray; 2.10 A; A/B=2-334.
PDB; 1T2F; X-ray; 3.00 A; A/B/C/D=2-332.
PDBsum; 1I0Z; -.
PDBsum; 1T2F; -.
ProteinModelPortal; P07195; -.
SMR; P07195; -.
BioGrid; 110137; 148.
IntAct; P07195; 40.
MINT; P07195; -.
STRING; 9606.ENSP00000229319; -.
BindingDB; P07195; -.
ChEMBL; CHEMBL4940; -.
DrugBank; DB00157; NADH.
DrugBank; DB03940; Oxamic Acid.
iPTMnet; P07195; -.
PhosphoSitePlus; P07195; -.
SwissPalm; P07195; -.
BioMuta; LDHB; -.
DMDM; 126041; -.
DOSAC-COBS-2DPAGE; P07195; -.
OGP; P07195; -.
REPRODUCTION-2DPAGE; IPI00219217; -.
SWISS-2DPAGE; P07195; -.
UCD-2DPAGE; P07195; -.
EPD; P07195; -.
PaxDb; P07195; -.
PeptideAtlas; P07195; -.
PRIDE; P07195; -.
ProteomicsDB; 51960; -.
TopDownProteomics; P07195; -.
DNASU; 3945; -.
Ensembl; ENST00000350669; ENSP00000229319; ENSG00000111716.
Ensembl; ENST00000396076; ENSP00000379386; ENSG00000111716.
GeneID; 3945; -.
KEGG; hsa:3945; -.
CTD; 3945; -.
DisGeNET; 3945; -.
EuPathDB; HostDB:ENSG00000111716.12; -.
GeneCards; LDHB; -.
HGNC; HGNC:6541; LDHB.
HPA; CAB004641; -.
HPA; HPA019007; -.
MalaCards; LDHB; -.
MIM; 150100; gene.
MIM; 614128; phenotype.
neXtProt; NX_P07195; -.
OpenTargets; ENSG00000111716; -.
Orphanet; 284435; Glycogen storage disease due to lactate dehydrogenase H-subunit deficiency.
PharmGKB; PA30325; -.
eggNOG; KOG1495; Eukaryota.
eggNOG; COG0039; LUCA.
GeneTree; ENSGT00940000153525; -.
HOGENOM; HOG000213793; -.
HOVERGEN; HBG000462; -.
InParanoid; P07195; -.
KO; K00016; -.
OMA; RQPGQTR; -.
OrthoDB; EOG091G0HME; -.
PhylomeDB; P07195; -.
TreeFam; TF314963; -.
BRENDA; 1.1.1.27; 2681.
Reactome; R-HSA-70268; Pyruvate metabolism.
SABIO-RK; P07195; -.
UniPathway; UPA00554; UER00611.
ChiTaRS; LDHB; human.
EvolutionaryTrace; P07195; -.
GenomeRNAi; 3945; -.
PRO; PR:P07195; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111716; Expressed in 233 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_LDHB; -.
ExpressionAtlas; P07195; baseline and differential.
Genevisible; P07195; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004459; F:L-lactate dehydrogenase activity; EXP:Reactome.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
Gene3D; 3.90.110.10; -; 1.
HAMAP; MF_00488; Lactate_dehydrog; 1.
InterPro; IPR001557; L-lactate/malate_DH.
InterPro; IPR011304; L-lactate_DH.
InterPro; IPR018177; L-lactate_DH_AS.
InterPro; IPR022383; Lactate/malate_DH_C.
InterPro; IPR001236; Lactate/malate_DH_N.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF02866; Ldh_1_C; 1.
Pfam; PF00056; Ldh_1_N; 1.
PIRSF; PIRSF000102; Lac_mal_DH; 1.
PRINTS; PR00086; LLDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
PROSITE; PS00064; L_LDH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; NAD; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.4}.
CHAIN 2 334 L-lactate dehydrogenase B chain.
/FTId=PRO_0000168459.
NP_BIND 31 53 NAD. {ECO:0000250}.
ACT_SITE 194 194 Proton acceptor.
BINDING 100 100 NAD. {ECO:0000269|PubMed:11276087}.
BINDING 107 107 Substrate.
BINDING 139 139 NAD or substrate.
{ECO:0000269|PubMed:11276087}.
BINDING 170 170 Substrate.
BINDING 249 249 Substrate.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.4}.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 58 58 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 119 119 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 240 240 Phosphotyrosine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 329 329 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 7 7 K -> E (in LDHBD; slightly decreased
activity; dbSNP:rs118203897).
{ECO:0000269|PubMed:8314553}.
/FTId=VAR_004173.
VARIANT 35 35 A -> E (in LDHBD).
{ECO:0000269|PubMed:8462975}.
/FTId=VAR_004174.
VARIANT 69 69 G -> E (in LDHBD).
{ECO:0000269|PubMed:11509017}.
/FTId=VAR_011634.
VARIANT 107 107 R -> W (in LDHBD; inactive;
dbSNP:rs777954556).
{ECO:0000269|PubMed:8611651}.
/FTId=VAR_011635.
VARIANT 129 129 S -> R (in LDHBD; dbSNP:rs118203896).
{ECO:0000269|PubMed:1587525}.
/FTId=VAR_004175.
VARIANT 171 171 F -> V (in LDHBD).
{ECO:0000269|PubMed:8462975}.
/FTId=VAR_004176.
VARIANT 172 172 R -> H (in LDHBD; dbSNP:rs118203895).
{ECO:0000269|PubMed:1587525,
ECO:0000269|PubMed:2334429}.
/FTId=VAR_004177.
VARIANT 172 172 R -> P (in LDHBD).
{ECO:0000269|PubMed:9929983}.
/FTId=VAR_011636.
VARIANT 175 175 M -> L (in LDHBD).
{ECO:0000269|PubMed:8462975}.
/FTId=VAR_004178.
VARIANT 175 175 M -> V (in dbSNP:rs7966339).
/FTId=VAR_049758.
VARIANT 223 223 Missing (in LDHBD).
{ECO:0000269|PubMed:10211631}.
/FTId=VAR_011637.
VARIANT 322 322 D -> V (in LDHBD). {ECO:0000269|Ref.20}.
/FTId=VAR_004179.
VARIANT 325 325 W -> R (in LDHBD; dbSNP:rs267607212).
/FTId=VAR_011638.
HELIX 4 8 {ECO:0000244|PDB:1I0Z}.
STRAND 9 13 {ECO:0000244|PDB:1T2F}.
STRAND 21 27 {ECO:0000244|PDB:1I0Z}.
HELIX 31 42 {ECO:0000244|PDB:1I0Z}.
STRAND 47 52 {ECO:0000244|PDB:1I0Z}.
HELIX 56 68 {ECO:0000244|PDB:1I0Z}.
HELIX 69 72 {ECO:0000244|PDB:1I0Z}.
STRAND 76 80 {ECO:0000244|PDB:1I0Z}.
HELIX 84 87 {ECO:0000244|PDB:1I0Z}.
STRAND 91 95 {ECO:0000244|PDB:1I0Z}.
HELIX 107 110 {ECO:0000244|PDB:1I0Z}.
HELIX 111 128 {ECO:0000244|PDB:1I0Z}.
STRAND 133 136 {ECO:0000244|PDB:1I0Z}.
STRAND 138 140 {ECO:0000244|PDB:1I0Z}.
HELIX 141 152 {ECO:0000244|PDB:1I0Z}.
HELIX 156 158 {ECO:0000244|PDB:1I0Z}.
STRAND 159 161 {ECO:0000244|PDB:1I0Z}.
HELIX 165 179 {ECO:0000244|PDB:1I0Z}.
HELIX 183 185 {ECO:0000244|PDB:1I0Z}.
STRAND 190 192 {ECO:0000244|PDB:1I0Z}.
HELIX 202 204 {ECO:0000244|PDB:1I0Z}.
HELIX 212 215 {ECO:0000244|PDB:1I0Z}.
TURN 217 220 {ECO:0000244|PDB:1I0Z}.
STRAND 221 223 {ECO:0000244|PDB:1I0Z}.
STRAND 225 227 {ECO:0000244|PDB:1T2F}.
HELIX 229 246 {ECO:0000244|PDB:1I0Z}.
HELIX 251 265 {ECO:0000244|PDB:1I0Z}.
STRAND 270 277 {ECO:0000244|PDB:1I0Z}.
TURN 279 282 {ECO:0000244|PDB:1T2F}.
STRAND 289 297 {ECO:0000244|PDB:1I0Z}.
STRAND 300 304 {ECO:0000244|PDB:1I0Z}.
HELIX 311 328 {ECO:0000244|PDB:1I0Z}.
SEQUENCE 334 AA; 36638 MW; 3AD605DEED0D54A2 CRC64;
MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK
GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF
IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG
IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY
EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG
LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL


Related products :

Catalog number Product name Quantity
E2196h Homo sapiens,Human,LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Renal carcinoma antigen NY-REN-46
U2196h CLIA Homo sapiens,Human,LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Renal carcinoma antigen NY-REN-46 96T
E2196h ELISA Homo sapiens,Human,LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Renal carcinoma antigen NY-REN-46 96T
E2196h ELISA kit Homo sapiens,Human,LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Renal carcinoma antigen NY-REN-46 96T
U2196h CLIA kit Homo sapiens,Human,LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Renal carcinoma antigen NY-REN-46 96T
E2195h Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59
U2195h CLIA kit Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59 96T
E2195h ELISA Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59 96T
U2195h CLIA Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59 96T
E2195h ELISA kit Cell proliferation-inducing gene 19 protein,Homo sapiens,Human,LDH muscle subunit,LDHA,LDH-A,LDH-M,L-lactate dehydrogenase A chain,PIG19,Renal carcinoma antigen NY-REN-59 96T
E2196p LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Pig,Sus scrofa
E2196p ELISA kit LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Pig,Sus scrofa 96T
U2196p CLIA kit LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Pig,Sus scrofa 96T
U2196p CLIA LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Pig,Sus scrofa 96T
E2196p ELISA LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Pig,Sus scrofa 96T
E2196m LDH heart subunit,Ldh2,Ldh-2,Ldhb,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Mouse,Mus musculus
E2196Rb LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Oryctolagus cuniculus,Rabbit
E2196r LDH heart subunit,Ldh2,Ldh-2,Ldhb,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Rat,Rattus norvegicus
E2196m ELISA LDH heart subunit,Ldh2,Ldh-2,Ldhb,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Mouse,Mus musculus 96T
U2196Rb CLIA LDH heart subunit,LDHB,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Oryctolagus cuniculus,Rabbit 96T
E2196m ELISA kit LDH heart subunit,Ldh2,Ldh-2,Ldhb,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Mouse,Mus musculus 96T
U2196m CLIA LDH heart subunit,Ldh2,Ldh-2,Ldhb,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Mouse,Mus musculus 96T
U2196r CLIA kit LDH heart subunit,Ldh2,Ldh-2,Ldhb,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Rat,Rattus norvegicus 96T
U2196m CLIA kit LDH heart subunit,Ldh2,Ldh-2,Ldhb,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Mouse,Mus musculus 96T
U2196r CLIA LDH heart subunit,Ldh2,Ldh-2,Ldhb,LDH-B,LDH-H,L-lactate dehydrogenase B chain,Rat,Rattus norvegicus 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur