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Heparan-sulfate 6-O-sulfotransferase 2 (HS6ST-2) (EC 2.8.2.-)

 H6ST2_HUMAN             Reviewed;         605 AA.
Q96MM7; B9WRT4; B9WRT5; E9PDY5; Q2TB13; Q4VC07; Q6PIC4; Q86SM9;
Q8N3T4; Q8NBN4; Q96SJ4;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 2.
12-SEP-2018, entry version 127.
RecName: Full=Heparan-sulfate 6-O-sulfotransferase 2;
Short=HS6ST-2;
EC=2.8.2.-;
Name=HS6ST2; ORFNames=PSEC0092;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain;
PubMed=12492399; DOI=10.1042/BJ20021259;
Habuchi H., Miyake G., Nogami K., Kuroiwa A., Matsuda Y.,
Kusche-Gullberg M., Habuchi O., Tanaka M., Kimata K.;
"Biosynthesis of heparan sulphate with diverse structures and
functions: two alternatively spliced forms of human heparan sulphate
6-O-sulphotransferase-2 having different expression patterns and
properties.";
Biochem. J. 371:131-142(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 176-605 (ISOFORM 3).
TISSUE=Placenta;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-605.
TISSUE=Teratocarcinoma;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-605.
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
-!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of
sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to
position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan
sulfate.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan
sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan
sulfate]-glucosamine 6-sulfate.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q96MM7-1; Sequence=Displayed;
Name=2; Synonyms=HS6ST-2S;
IsoId=Q96MM7-2; Sequence=VSP_015846;
Name=3; Synonyms=HS6ST-2;
IsoId=Q96MM7-3; Sequence=VSP_015846, VSP_015847;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q96MM7-4; Sequence=VSP_015847;
Note=Gene prediction based on EST data.;
-!- SIMILARITY: Belongs to the sulfotransferase 6 family.
{ECO:0000305}.
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EMBL; AB067776; BAC07183.1; -; mRNA.
EMBL; AB067777; BAC07184.1; -; mRNA.
EMBL; AK027720; BAB55322.1; -; mRNA.
EMBL; AK056706; BAB71260.1; -; mRNA.
EMBL; Z81365; CAX30811.1; -; Genomic_DNA.
EMBL; Z86064; CAX30811.1; JOINED; Genomic_DNA.
EMBL; Z81365; CAX30812.1; -; Genomic_DNA.
EMBL; Z86064; CAX30812.1; JOINED; Genomic_DNA.
EMBL; AL022309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL022159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z82205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z86064; CAI42774.1; -; Genomic_DNA.
EMBL; Z81365; CAI42774.1; JOINED; Genomic_DNA.
EMBL; Z86064; CAI42775.1; -; Genomic_DNA.
EMBL; Z81365; CAI42775.1; JOINED; Genomic_DNA.
EMBL; BC037325; AAH37325.1; -; mRNA.
EMBL; BC094718; AAH94718.1; -; mRNA.
EMBL; BC110620; AAI10621.1; -; mRNA.
EMBL; BC110621; AAI10622.1; -; mRNA.
EMBL; AK075402; BAC11597.1; -; mRNA.
EMBL; AL831923; CAD38583.1; -; mRNA.
CCDS; CCDS48169.1; -. [Q96MM7-1]
CCDS; CCDS48170.1; -. [Q96MM7-4]
RefSeq; NP_001070656.1; NM_001077188.1. [Q96MM7-4]
RefSeq; NP_671704.3; NM_147175.3. [Q96MM7-1]
RefSeq; XP_005262547.1; XM_005262490.3. [Q96MM7-4]
RefSeq; XP_011529708.1; XM_011531406.1. [Q96MM7-3]
RefSeq; XP_016885433.1; XM_017029944.1. [Q96MM7-1]
RefSeq; XP_016885434.1; XM_017029945.1. [Q96MM7-3]
UniGene; Hs.385956; -.
ProteinModelPortal; Q96MM7; -.
SMR; Q96MM7; -.
BioGrid; 124671; 10.
IntAct; Q96MM7; 5.
iPTMnet; Q96MM7; -.
PhosphoSitePlus; Q96MM7; -.
BioMuta; HS6ST2; -.
DMDM; 77416506; -.
MaxQB; Q96MM7; -.
PeptideAtlas; Q96MM7; -.
PRIDE; Q96MM7; -.
ProteomicsDB; 77375; -.
ProteomicsDB; 77376; -. [Q96MM7-2]
ProteomicsDB; 77377; -. [Q96MM7-3]
Ensembl; ENST00000370833; ENSP00000359870; ENSG00000171004. [Q96MM7-4]
Ensembl; ENST00000370836; ENSP00000359873; ENSG00000171004. [Q96MM7-1]
Ensembl; ENST00000406696; ENSP00000384013; ENSG00000171004. [Q96MM7-1]
Ensembl; ENST00000521489; ENSP00000429473; ENSG00000171004. [Q96MM7-4]
GeneID; 90161; -.
KEGG; hsa:90161; -.
UCSC; uc011mvd.2; human. [Q96MM7-1]
CTD; 90161; -.
DisGeNET; 90161; -.
EuPathDB; HostDB:ENSG00000171004.17; -.
GeneCards; HS6ST2; -.
HGNC; HGNC:19133; HS6ST2.
HPA; HPA034625; -.
HPA; HPA034626; -.
MIM; 300545; gene.
neXtProt; NX_Q96MM7; -.
OpenTargets; ENSG00000171004; -.
PharmGKB; PA134950831; -.
GeneTree; ENSGT00390000013468; -.
HOVERGEN; HBG083012; -.
InParanoid; Q96MM7; -.
KO; K08102; -.
OMA; NYYYITI; -.
OrthoDB; EOG091G08UD; -.
PhylomeDB; Q96MM7; -.
TreeFam; TF312835; -.
Reactome; R-HSA-2022928; HS-GAG biosynthesis.
ChiTaRS; HS6ST2; human.
GenomeRNAi; 90161; -.
PRO; PR:Q96MM7; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000171004; Expressed in 164 organ(s), highest expression level in endothelial cell.
CleanEx; HS_HS6ST2; -.
ExpressionAtlas; Q96MM7; baseline and differential.
Genevisible; Q96MM7; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005331; Sulfotransferase.
PANTHER; PTHR12812; PTHR12812; 1.
Pfam; PF03567; Sulfotransfer_2; 1.
SUPFAM; SSF52540; SSF52540; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Glycoprotein; Membrane;
Polymorphism; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 605 Heparan-sulfate 6-O-sulfotransferase 2.
/FTId=PRO_0000190805.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 605 Lumenal. {ECO:0000255}.
REGION 233 241 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 263 264 Substrate binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 457 459 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
REGION 463 464 PAPS binding.
{ECO:0000250|UniProtKB:A0MGZ7}.
ACT_SITE 290 290 Proton acceptor.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 280 280 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 285 285 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 290 290 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 325 325 PAPS. {ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 333 333 PAPS. {ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 337 337 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
BINDING 344 344 Substrate.
{ECO:0000250|UniProtKB:A0MGZ7}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 460 460 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 544 544 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 556 556 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 589 589 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 592 592 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 146 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:12492399,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015846.
VAR_SEQ 315 316 SR -> SRWRIFQILDAASKDKRGSPNTNAGANSPSSTKTR
NTSKSGK (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:12492399,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015847.
VARIANT 127 127 K -> N (in dbSNP:rs7053397).
/FTId=VAR_061828.
CONFLICT 192 192 D -> G (in Ref. 2; BAB71260).
{ECO:0000305}.
CONFLICT 299 299 C -> Y (in Ref. 4; AAH37325).
{ECO:0000305}.
CONFLICT 426 426 K -> R (in Ref. 5; BAC11597).
{ECO:0000305}.
CONFLICT 568 568 S -> N (in Ref. 2; BAB71260).
{ECO:0000305}.
CONFLICT 580 580 Q -> R (in Ref. 5; BAC11597).
{ECO:0000305}.
CONFLICT 585 585 E -> G (in Ref. 5; BAC11597).
{ECO:0000305}.
SEQUENCE 605 AA; 69130 MW; 10528AC424935B13 CRC64;
MALPACAVRE FEPPRQPERG APVRTTCPRR HSRVEAELAA SRPGSVAASV RAGPPRGVSH
GFHTRPLLDK PRKASSSLAG AACAPLFALL SRGRRRRMHV LRRRWDLGSL CRALLTRGLA
ALGHSLKHVL GAIFSKIFGP MASVGNMDEK SNKLLLALVM LFLFAVIVLQ YVCPGTECQL
LRLQAFSSPV PDPYRSEDES SARFVPRYNF TRGDLLRKVD FDIKGDDLIV FLHIQKTGGT
TFGRHLVRNI QLEQPCECRV GQKKCTCHRP GKRETWLFSR FSTGWSCGLH ADWTELTSCV
PSVVDGKRDA RLRPSRNFHY ITILRDPVSR YLSEWRHVQR GATWKASLHV CDGRPPTSEE
LPSCYTGDDW SGCPLKEFMD CPYNLANNRQ VRMLSDLTLV GCYNLSVMPE KQRNKVLLES
AKSNLKHMAF FGLTEFQRKT QYLFEKTFNM NFISPFTQYN TTRASSVEIN EEIQKRIEGL
NFLDMELYSY AKDLFLQRYQ FMRQKEHQEA RRKRQEQRKF LKGRLLQTHF QSQGQGQSQN
PNQNQSQNPN PNANQNLTQN LMQNLTQSLS QKENRESPKQ NSGKEQNDNT SNGTNDYIGS
VEKWR


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E0252h Human ELISA Kit FOR Heparan-sulfate 6-O-sulfotransferase 2 96T
CSB-EL010758MO Mouse Heparan-sulfate 6-O-sulfotransferase 2(HS6ST2) ELISA kit 96T
PTHB1_HUMAN Human ELISA Kit FOR Heparan sulfate glucosamine 3-O-sulfotransferase 4 96T
CSB-EL010746CH Chicken Heparan sulfate 2-O-sulfotransferase 1(HS2ST1) ELISA kit 96T
CSB-EL010756MO Mouse Heparan-sulfate 6-O-sulfotransferase 1(HS6ST1) ELISA kit 96T
CSB-EL010758CH Chicken Heparan-sulfate 6-O-sulfotransferase 2(HS6ST2) ELISA kit 96T
HS3SA_HUMAN Human ELISA Kit FOR Heparan sulfate glucosamine 3-O-sulfotransferase 3A1 96T


 

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