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Polypeptide N-acetylgalactosaminyltransferase 12 (EC 2.4.1.41) (Polypeptide GalNAc transferase 12) (GalNAc-T12) (pp-GaNTase 12) (Protein-UDP acetylgalactosaminyltransferase 12) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12)

 GLT12_HUMAN             Reviewed;         581 AA.
Q8IXK2; Q5TCF7; Q8NG54; Q96CT9; Q9H771;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 3.
30-AUG-2017, entry version 145.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 12;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 12;
Short=GalNAc-T12;
Short=pp-GaNTase 12;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 12;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12;
Name=GALNT12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE
SPECIFICITY, AND VARIANT VAL-119.
TISSUE=Lung;
PubMed=12135769; DOI=10.1016/S0014-5793(02)03007-7;
Guo J.-M., Zhang Y., Cheng L., Iwasaki H., Wang H., Kubota T.,
Tachibana K., Narimatsu H.;
"Molecular cloning and characterization of a novel member of the UDP-
GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-
GalNAc-T12(1).";
FEBS Lett. 524:211-218(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Bennett E.P.;
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Bone marrow;
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 144-581 (ISOFORM 1).
TISSUE=Colon;
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).
[6]
VARIANTS CRCS1 TRP-297; ASN-303; ASP-341; HIS-373; HIS-382; PHE-479
AND MET-491, CHARACTERIZATION OF VARIANTS CRCS1 TRP-297; ASN-303;
ASP-341; HIS-373; HIS-382; PHE-479 AND MET-491, AND VARIANTS GLU-3;
ARG-46; VAL-119; ASN-261; ARG-272 AND LYS-552.
PubMed=19617566; DOI=10.1073/pnas.0901454106;
Guda K., Moinova H., He J., Jamison O., Ravi L., Natale L.,
Lutterbaugh J., Lawrence E., Lewis S., Willson J.K., Lowe J.B.,
Wiesner G.L., Parmigiani G., Barnholtz-Sloan J., Dawson D.W.,
Velculescu V.E., Kinzler K.W., Papadopoulos N., Vogelstein B.,
Willis J., Gerken T.A., Markowitz S.D.;
"Inactivating germ-line and somatic mutations in polypeptide N-
acetylgalactosaminyltransferase 12 in human colon cancers.";
Proc. Natl. Acad. Sci. U.S.A. 106:12921-12925(2009).
[7]
VARIANTS CRCS1 ASN-303 AND CYS-396.
PubMed=22461326; DOI=10.1002/humu.22088;
Clarke E., Green R.C., Green J.S., Mahoney K., Parfrey P.S.,
Younghusband H.B., Woods M.O.;
"Inherited deleterious variants in GALNT12 are associated with CRC
susceptibility.";
Hum. Mutat. 33:1056-1058(2012).
[8]
INVOLVEMENT IN CRCS1.
PubMed=24115450; DOI=10.1002/humu.22454;
Segui N., Pineda M., Navarro M., Lazaro C., Brunet J., Infante M.,
Duran M., Soto J.L., Blanco I., Capella G., Valle L.;
"GALNT12 is not a major contributor of familial colorectal cancer type
X.";
Hum. Mutat. 35:50-52(2014).
-!- FUNCTION: Catalyzes the initial reaction in O-linked
oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
galactosamine residue to a serine or threonine residue on the
protein receptor. Has activity toward non-glycosylated peptides
such as Muc5AC, Muc1a and EA2, and no detectable activity with
Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc-
Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-
glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role
in the initial step of mucin-type oligosaccharide biosynthesis in
digestive organs.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
{ECO:0000269|PubMed:12135769}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IXK2-1; Sequence=Displayed;
Name=2;
IsoId=Q8IXK2-2; Sequence=VSP_011217;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed at different levels of
expression. Highly expressed in digestive organs such as small
intestine, stomach, pancreas and colon. Expressed at intermediate
level in testis, thyroid gland and spleen. Weakly expressed in
whole brain, cerebral cortex, cerebellum, fetal brain, bone
marrow, thymus, leukocytes, heart, skeletal muscle, liver, lung,
esophagus, kidney, adrenal gland, mammary gland, uterus, placenta,
ovary and prostate. {ECO:0000269|PubMed:12135769}.
-!- DOMAIN: There are two conserved domains in the glycosyltransferase
region: the N-terminal domain (domain A, also called GT1 motif),
which is probably involved in manganese coordination and substrate
binding and the C-terminal domain (domain B, also called
Gal/GalNAc-T motif), which is probably involved in catalytic
reaction and UDP-Gal binding. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- DISEASE: Colorectal cancer 1 (CRCS1) [MIM:608812]: A complex
disease characterized by malignant lesions arising from the inner
wall of the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
{ECO:0000269|PubMed:19617566, ECO:0000269|PubMed:22461326,
ECO:0000269|PubMed:24115450}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. The role of GALNT12 in colon cancer susceptibility is
however subject to discussion: studies on 103 probants with
colorectal cancer 1 (CRCS1) suggest that it does not act as a
major contributor of CRCS1 (PubMed:24115450).
{ECO:0000269|PubMed:24115450}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Polypeptide N-acetylgalactosaminyltransferase 12;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_495";
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EMBL; AB078146; BAC07181.1; -; mRNA.
EMBL; AJ132365; CAC80100.2; -; mRNA.
EMBL; AL136084; CAI17042.1; -; Genomic_DNA.
EMBL; BC013945; AAH13945.1; -; mRNA.
EMBL; AK024865; BAB15027.1; ALT_INIT; mRNA.
CCDS; CCDS6737.1; -. [Q8IXK2-1]
RefSeq; NP_078918.3; NM_024642.4. [Q8IXK2-1]
RefSeq; XP_006717350.1; XM_006717287.1.
UniGene; Hs.47099; -.
ProteinModelPortal; Q8IXK2; -.
SMR; Q8IXK2; -.
BioGrid; 122816; 32.
IntAct; Q8IXK2; 11.
STRING; 9606.ENSP00000364150; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q8IXK2; -.
PhosphoSitePlus; Q8IXK2; -.
SwissPalm; Q8IXK2; -.
BioMuta; GALNT12; -.
DMDM; 84028209; -.
EPD; Q8IXK2; -.
MaxQB; Q8IXK2; -.
PaxDb; Q8IXK2; -.
PeptideAtlas; Q8IXK2; -.
PRIDE; Q8IXK2; -.
DNASU; 79695; -.
Ensembl; ENST00000375011; ENSP00000364150; ENSG00000119514. [Q8IXK2-1]
GeneID; 79695; -.
KEGG; hsa:79695; -.
UCSC; uc004ayz.3; human. [Q8IXK2-1]
CTD; 79695; -.
DisGeNET; 79695; -.
GeneCards; GALNT12; -.
H-InvDB; HIX0008226; -.
HGNC; HGNC:19877; GALNT12.
HPA; HPA048292; -.
MalaCards; GALNT12; -.
MIM; 608812; phenotype.
MIM; 610290; gene.
neXtProt; NX_Q8IXK2; -.
OpenTargets; ENSG00000119514; -.
PharmGKB; PA134929192; -.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q8IXK2; -.
KO; K00710; -.
OMA; ERWNPLC; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q8IXK2; -.
TreeFam; TF352660; -.
BRENDA; 2.4.1.41; 2681.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
GenomeRNAi; 79695; -.
PRO; PR:Q8IXK2; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000119514; -.
CleanEx; HS_GALNT12; -.
ExpressionAtlas; Q8IXK2; baseline and differential.
Genevisible; Q8IXK2; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; TAS:Reactome.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Disulfide bond; Glycosyltransferase; Golgi apparatus; Lectin;
Manganese; Membrane; Metal-binding; Polymorphism; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 581 Polypeptide N-
acetylgalactosaminyltransferase 12.
/FTId=PRO_0000059128.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 37 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 38 581 Lumenal. {ECO:0000255}.
DOMAIN 445 577 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 135 244 Catalytic subdomain A.
REGION 304 366 Catalytic subdomain B.
METAL 228 228 Manganese. {ECO:0000250}.
METAL 230 230 Manganese. {ECO:0000250}.
METAL 363 363 Manganese. {ECO:0000250}.
BINDING 176 176 Substrate. {ECO:0000250}.
BINDING 205 205 Substrate. {ECO:0000250}.
BINDING 335 335 Substrate. {ECO:0000250}.
BINDING 371 371 Substrate. {ECO:0000250}.
DISULFID 125 358 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 349 422 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 458 479 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 506 521 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 547 566 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 1 309 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011217.
VARIANT 3 3 G -> E. {ECO:0000269|PubMed:19617566}.
/FTId=VAR_064352.
VARIANT 46 46 G -> R (in dbSNP:rs10987768).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064353.
VARIANT 119 119 E -> V (in dbSNP:rs1137654).
{ECO:0000269|PubMed:12135769,
ECO:0000269|PubMed:19617566}.
/FTId=VAR_064354.
VARIANT 261 261 D -> N (in dbSNP:rs41306504).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064355.
VARIANT 272 272 G -> R (in dbSNP:rs367645298).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064356.
VARIANT 297 297 R -> W (in CRCS1; germline mutation;
partial loss of activity;
dbSNP:rs149726976).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064357.
VARIANT 303 303 D -> N (in CRCS1; germline mutation;
reduction of activity;
dbSNP:rs145236923).
{ECO:0000269|PubMed:19617566,
ECO:0000269|PubMed:22461326}.
/FTId=VAR_064358.
VARIANT 341 341 E -> D (in CRCS1; somatic mutation; loss
of activity).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064359.
VARIANT 373 373 R -> H (in CRCS1; germline mutation;
partial loss of activity).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064360.
VARIANT 382 382 R -> H (in CRCS1; germline mutation; loss
of activity; dbSNP:rs868590153).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064361.
VARIANT 396 396 Y -> C (in CRCS1).
{ECO:0000269|PubMed:22461326}.
/FTId=VAR_068509.
VARIANT 479 479 C -> F (in CRCS1; somatic mutation; loss
of activity).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064362.
VARIANT 491 491 T -> M (in CRCS1; germline mutation; loss
of activity; dbSNP:rs267606840).
{ECO:0000269|PubMed:19617566}.
/FTId=VAR_064363.
VARIANT 552 552 R -> K. {ECO:0000269|PubMed:19617566}.
/FTId=VAR_064364.
SEQUENCE 581 AA; 66938 MW; 8C001D58E103A523 CRC64;
MWGRTARRRC PRELRRGREA LLVLLALLAL AGLGSVLRAQ RGAGAGAAEP GPPRTPRPGR
REPVMPRPPV PANALGARGE AVRLQLQGEE LRLQEESVRL HQINIYLSDR ISLHRRLPER
WNPLCKEKKY DYDNLPRTSV IIAFYNEAWS TLLRTVYSVL ETSPDILLEE VILVDDYSDR
EHLKERLANE LSGLPKVRLI RANKREGLVR ARLLGASAAR GDVLTFLDCH CECHEGWLEP
LLQRIHEEES AVVCPVIDVI DWNTFEYLGN SGEPQIGGFD WRLVFTWHTV PERERIRMQS
PVDVIRSPTM AGGLFAVSKK YFEYLGSYDT GMEVWGGENL EFSFRIWQCG GVLETHPCSH
VGHVFPKQAP YSRNKALANS VRAAEVWMDE FKELYYHRNP RARLEPFGDV TERKQLRDKL
QCKDFKWFLE TVYPELHVPE DRPGFFGMLQ NKGLTDYCFD YNPPDENQIV GHQVILYLCH
GMGQNQFFEY TSQKEIRYNT HQPEGCIAVE AGMDTLIMHL CEETAPENQK FILQEDGSLF
HEQSKKCVQA ARKESSDSFV PLLRDCTNSD HQKWFFKERM L


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201-20-2176 GALNT14{UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 14 (GalNAc-T14)}rabbit.pAb 0.2ml
201-20-2177 GALNT4{UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 4 (GalNAc-T4)}rabbit.pAb 0.2ml
201-20-2178 GALNT7{UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7)}rabbit.pAb 0.2ml
GALNT8 GALNT6 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6)
CSB-EL009203PI Pig UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) (GALNT1) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL009212RA Rat UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5) (GALNT5) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL009214RA Rat UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7) (GALNT7) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL009207RA Rat UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 13 (GalNAc-T13) (GALNT13) ELISA kit, Species Rat, Sample Type serum, plasma 96T


 

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