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Immunoglobulin superfamily member 10 (IgSF10) (Calvaria mechanical force protein 608) (CMF608)

 IGS10_HUMAN             Reviewed;        2623 AA.
Q6WRI0; Q86YJ9; Q8N772; Q8NA84;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-MAY-2022, entry version 149.
RecName: Full=Immunoglobulin superfamily member 10;
Short=IgSF10;
AltName: Full=Calvaria mechanical force protein 608;
Short=CMF608;
Flags: Precursor;
Name=IGSF10; Synonyms=CMF608;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14962803; DOI=10.1016/j.bone.2003.10.003;
Segev O., Samach A., Faerman A., Kalinski H., Beiman M., Gelfand A.,
Turam H., Boguslavsky S., Moshayov A., Gottlieb H., Kazanov E., Nevo Z.,
Robinson D., Skaliter R., Einat P., Binderman I., Feinstein E.;
"CMF608 -- a novel mechanical strain-induced bone-specific protein
expressed in early osteochondroprogenitor cells.";
Bone 34:246-260(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 2187-2623 (ISOFORM 1).
TISSUE=Testis;
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 MRNA] (ISOFORM 3).
TISSUE=Testis;
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]
SUBCELLULAR LOCATION, PROBABLE INVOLVEMENT IN SELF-LIMITED DELAYED PUBERTY,
VARIANTS LEU-156; LYS-161; GLY-2264 AND ASN-2614, AND CHARACTERIZATION OF
VARIANTS LEU-156 AND LYS-161.
PubMed=27137492; DOI=10.15252/emmm.201606250;
Howard S.R., Guasti L., Ruiz-Babot G., Mancini A., David A., Storr H.L.,
Metherell L.A., Sternberg M.J., Cabrera C.P., Warren H.R., Barnes M.R.,
Quinton R., de Roux N., Young J., Guiochon-Mantel A., Wehkalampi K.,
Andre V., Gothilf Y., Cariboni A., Dunkel L.;
"IGSF10 mutations dysregulate gonadotropin-releasing hormone neuronal
migration resulting in delayed puberty.";
EMBO Mol. Med. 8:626-642(2016).
-!- FUNCTION: Involved in the control of early migration of neurons
expressing gonadotropin-releasing hormone (GNRH neurons) (By
similarity). May be involved in the maintenance of
osteochondroprogenitor cells pool (By similarity).
{ECO:0000250|UniProtKB:Q3V1M1, ECO:0000250|UniProtKB:Q6WRH9}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27137492}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6WRI0-1; Sequence=Displayed;
Name=2;
IsoId=Q6WRI0-2; Sequence=VSP_025195, VSP_025196;
Name=3;
IsoId=Q6WRI0-3; Sequence=VSP_025194;
-!- DISEASE: Note=Mutations in IGSF10 may be a cause of self-limited
delayed puberty. This common condition is defined as the absence of
testicular enlargement in boys or breast development in girls at an age
that is 2-2.5 standard deviations later than the population mean. Self-
limited delayed puberty segregates within families, with the majority
of families displaying an autosomal dominant pattern of inheritance.
{ECO:0000269|PubMed:27137492}.
-!- SEQUENCE CAUTION:
Sequence=BAC05429.1; Type=Erroneous initiation; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; AY273815; AAQ16156.1; -; mRNA.
EMBL; AK093069; BAC04042.1; -; mRNA.
EMBL; AK098838; BAC05429.1; ALT_INIT; mRNA.
EMBL; BC031063; AAH31063.1; -; mRNA.
CCDS; CCDS3160.1; -. [Q6WRI0-1]
RefSeq; NP_001171616.1; NM_001178145.1. [Q6WRI0-3]
RefSeq; NP_001171617.1; NM_001178146.1. [Q6WRI0-3]
RefSeq; NP_849144.2; NM_178822.4. [Q6WRI0-1]
RefSeq; XP_011511011.1; XM_011512709.2. [Q6WRI0-1]
AlphaFoldDB; Q6WRI0; -.
SMR; Q6WRI0; -.
BioGRID; 130074; 6.
IntAct; Q6WRI0; 1.
STRING; 9606.ENSP00000282466; -.
DrugBank; DB00114; Pyridoxal phosphate.
CarbonylDB; Q6WRI0; -.
GlyGen; Q6WRI0; 11 sites, 2 O-linked glycans (3 sites).
iPTMnet; Q6WRI0; -.
PhosphoSitePlus; Q6WRI0; -.
BioMuta; IGSF10; -.
DMDM; 74749492; -.
EPD; Q6WRI0; -.
jPOST; Q6WRI0; -.
MassIVE; Q6WRI0; -.
PaxDb; Q6WRI0; -.
PeptideAtlas; Q6WRI0; -.
PRIDE; Q6WRI0; -.
ProteomicsDB; 67774; -. [Q6WRI0-1]
ProteomicsDB; 67775; -. [Q6WRI0-2]
ProteomicsDB; 67776; -. [Q6WRI0-3]
Antibodypedia; 2541; 65 antibodies from 14 providers.
DNASU; 285313; -.
Ensembl; ENST00000282466.4; ENSP00000282466.3; ENSG00000152580.9.
GeneID; 285313; -.
KEGG; hsa:285313; -.
MANE-Select; ENST00000282466.4; ENSP00000282466.3; NM_178822.5; NP_849144.2.
UCSC; uc011bod.3; human. [Q6WRI0-1]
CTD; 285313; -.
DisGeNET; 285313; -.
GeneCards; IGSF10; -.
HGNC; HGNC:26384; IGSF10.
HPA; ENSG00000152580; Tissue enhanced (ovary).
MIM; 617351; gene.
neXtProt; NX_Q6WRI0; -.
OpenTargets; ENSG00000152580; -.
PharmGKB; PA134900760; -.
VEuPathDB; HostDB:ENSG00000152580; -.
eggNOG; KOG0619; Eukaryota.
GeneTree; ENSGT00940000158290; -.
HOGENOM; CLU_000580_0_0_1; -.
InParanoid; Q6WRI0; -.
OMA; IWGRGRI; -.
OrthoDB; 8971at2759; -.
PhylomeDB; Q6WRI0; -.
TreeFam; TF326318; -.
PathwayCommons; Q6WRI0; -.
SignaLink; Q6WRI0; -.
BioGRID-ORCS; 285313; 7 hits in 1065 CRISPR screens.
ChiTaRS; IGSF10; human.
GenomeRNAi; 285313; -.
Pharos; Q6WRI0; Tbio.
PRO; PR:Q6WRI0; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; Q6WRI0; protein.
Bgee; ENSG00000152580; Expressed in layer of synovial tissue and 192 other tissues.
ExpressionAtlas; Q6WRI0; baseline and differential.
Genevisible; Q6WRI0; HS.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 12.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
Pfam; PF07679; I-set; 7.
Pfam; PF13855; LRR_8; 1.
SMART; SM00409; IG; 12.
SMART; SM00408; IGc2; 12.
SMART; SM00406; IGv; 7.
SMART; SM00369; LRR_TYP; 6.
SMART; SM00082; LRRCT; 1.
SMART; SM00013; LRRNT; 1.
SUPFAM; SSF48726; SSF48726; 12.
PROSITE; PS50835; IG_LIKE; 12.
1: Evidence at protein level;
Alternative splicing; Developmental protein; Differentiation;
Disease variant; Disulfide bond; Glycoprotein; Immunoglobulin domain;
Leucine-rich repeat; Osteogenesis; Phosphoprotein; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1..28
/evidence="ECO:0000255"
CHAIN 29..2623
/note="Immunoglobulin superfamily member 10"
/id="PRO_0000286817"
DOMAIN 29..56
/note="LRRNT"
REPEAT 58..79
/note="LRR 1"
REPEAT 82..103
/note="LRR 2"
REPEAT 106..127
/note="LRR 3"
REPEAT 130..151
/note="LRR 4"
REPEAT 154..175
/note="LRR 5"
REPEAT 186..207
/note="LRR 6"
DOMAIN 219..281
/note="LRRCT"
DOMAIN 461..567
/note="Ig-like C2-type 1"
DOMAIN 571..661
/note="Ig-like C2-type 2"
DOMAIN 1648..1739
/note="Ig-like C2-type 3"
DOMAIN 1745..1836
/note="Ig-like C2-type 4"
DOMAIN 1841..1933
/note="Ig-like C2-type 5"
DOMAIN 1941..2034
/note="Ig-like C2-type 6"
DOMAIN 2037..2135
/note="Ig-like C2-type 7"
DOMAIN 2141..2229
/note="Ig-like C2-type 8"
DOMAIN 2234..2331
/note="Ig-like C2-type 9"
DOMAIN 2337..2427
/note="Ig-like C2-type 10"
DOMAIN 2432..2518
/note="Ig-like C2-type 11"
DOMAIN 2528..2623
/note="Ig-like C2-type 12"
REGION 668..692
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 767..788
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1334..1376
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1434..1453
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1340..1356
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1357..1376
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 2603
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:Q6WRH9"
CARBOHYD 319
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 439
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 627
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 774
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 999
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1899
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1962
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2101
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 497..551
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 595..645
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 1670..1723
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 1767..1820
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 1864..1917
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 1963..2016
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 2060..2119
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 2163..2213
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 2261..2313
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 2359..2411
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 2454..2506
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 2550..2605
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 1..2021
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_025194"
VAR_SEQ 1..1973
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_025195"
VAR_SEQ 1974..1987
/note="MWRLPSKAVVDQQH -> MVESVRLENQPCDL (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_025196"
VARIANT 124
/note="T -> I (in dbSNP:rs35953658)"
/id="VAR_032179"
VARIANT 150
/note="Y -> D (in dbSNP:rs7619322)"
/id="VAR_032180"
VARIANT 156
/note="R -> L (probable disease-associated variant found in
autosomal dominant self-limited delayed puberty; the mutant
protein is not secreted; dbSNP:rs138756085)"
/evidence="ECO:0000269|PubMed:27137492"
/id="VAR_078550"
VARIANT 161
/note="E -> K (probable disease-associated variant found in
autosomal dominant self-limited delayed puberty; the mutant
protein is not secreted; dbSNP:rs114161831)"
/evidence="ECO:0000269|PubMed:27137492"
/id="VAR_078551"
VARIANT 571
/note="P -> S (in dbSNP:rs17204557)"
/id="VAR_032181"
VARIANT 795
/note="D -> N (in dbSNP:rs58583961)"
/id="VAR_061313"
VARIANT 1199
/note="S -> A (in dbSNP:rs16863403)"
/id="VAR_032182"
VARIANT 1370
/note="T -> I (in dbSNP:rs34933248)"
/id="VAR_032183"
VARIANT 1875
/note="Y -> H (in dbSNP:rs12487205)"
/id="VAR_032184"
VARIANT 2264
/note="E -> G (found in autosomal dominant self-limited
delayed puberty; unknown pathological significance;
dbSNP:rs1204847665)"
/evidence="ECO:0000269|PubMed:27137492"
/id="VAR_078552"
VARIANT 2476
/note="R -> W (in dbSNP:rs3732775)"
/id="VAR_032185"
VARIANT 2579
/note="H -> Y (in dbSNP:rs7624011)"
/id="VAR_032186"
VARIANT 2614
/note="D -> N (found in autosomal dominant self-limited
delayed puberty; unknown pathological significance;
dbSNP:rs112889898)"
/evidence="ECO:0000269|PubMed:27137492"
/id="VAR_078553"
CONFLICT 2243
/note="N -> S (in Ref. 3; AAH31063)"
/evidence="ECO:0000305"
SEQUENCE 2623 AA; 290838 MW; CBE7139B0DF16CF8 CRC64;
MKVKGRGITC LLVSFAVICL VATPGGKACP RRCACYMPTE VHCTFRYLTS IPDSIPPNVE
RINLGYNSLV RLMETDFSGL TKLELLMLHS NGIHTIPDKT FSDLQALQVL KMSYNKVRKL
QKDTFYGLRS LTRLHMDHNN IEFINPEVFY GLNFLRLVHL EGNQLTKLHP DTFVSLSYLQ
IFKISFIKFL YLSDNFLTSL PQEMVSYMPD LDSLYLHGNP WTCDCHLKWL SDWIQEKPDV
IKCKKDRSPS SAQQCPLCMN PRTSKGKPLA MVSAAAFQCA KPTIDSSLKS KSLTILEDSS
SAFISPQGFM APFGSLTLNM TDQSGNEANM VCSIQKPSRT SPIAFTEEND YIVLNTSFST
FLVCNIDYGH IQPVWQILAL YSDSPLILER SHLLSETPQL YYKYKQVAPK PEDIFTNIEA
DLRADPSWLM QDQISLQLNR TATTFSTLQI QYSSDAQITL PRAEMRPVKH KWTMISRDNN
TKLEHTVLVG GTVGLNCPGQ GDPTPHVDWL LADGSKVRAP YVSEDGRILI DKSGKLELQM
ADSFDTGVYH CISSNYDDAD ILTYRITVVE PLVEAYQENG IHHTVFIGET LDLPCHSTGI
PDASISWVIP GNNVLYQSSR DKKVLNNGTL RILQVTPKDQ GYYRCVAANP SGVDFLIFQV
SVKMKGQRPL EHDGETEGSG LDESNPIAHL KEPPGAQLRT SALMEAEVGK HTSSTSKRHN
YRELTLQRRG DSTHRRFREN RRHFPPSARR IDPQHWAALL EKAKKNAMPD KRENTTVSPP
PVVTQLPNIP GEEDDSSGML ALHEEFMVPA TKALNLPART VTADSRTISD SPMTNINYGT
EFSPVVNSQI LPPEEPTDFK LSTAIKTTAM SKNINPTMSS QIQGTTNQHS STVFPLLLGA
TEFQDSDQMG RGREHFQSRP PITVRTMIKD VNVKMLSSTT NKLLLESVNT TNSHQTSVRE
VSEPRHNHFY SHTTQILSTS TFPSDPHTAA HSQFPIPRNS TVNIPLFRRF GRQRKIGGRG
RIISPYRTPV LRRHRYSIFR STTRGSSEKS TTAFSATVLN VTCLSCLPRE RLTTATAALS
FPSAAPITFP KADIARVPSE ESTTLVQNPL LLLENKPSVE KTTPTIKYFR TEISQVTPTG
AVMTYAPTSI PMEKTHKVNA SYPRVSSTNE AKRDSVITSS LSGAITKPPM TIIAITRFSR
RKIPWQQNFV NNHNPKGRLR NQHKVSLQKS TAVMLPKTSP ALPRDKVSPF HFTTLSTSVM
QIPSNTLTTA HHTTTKTHNP GSLPTKKELP FPPLNPMLPS IISKDSSTKS IISTQTAIPA
TTPTFPASVI TYETQTERSR AQTIQREQEP QKKNRTDPNI SPDQSSGFTT PTAMTPPVLT
TAETSVKPSV SAFTHSPPEN TTGISSTISF HSRTLNLTDV IEELAQASTQ TLKSTIASET
TLSSKSHQST TTRKAIIRHS TIPPFLSSSA TLMPVPISPP FTQRAVTDNV ATPISGLMTN
TVVKLHESSR HNAKPQQLVA EVATSPKVHP NAKFTIGTTH FIYSNLLHST PMPALTTVKS
QNSKLTPSPW AENQFWHKPY SEIAEKGKKP EVSMLATTGL SEATTLVSDW DGQKNTKKSD
FDKKPVQEAT TSKLLPFDSL SRYIFEKPRI VGGKAASFTI PANSDAFLPC EAVGNPLPTI
HWTRVPSGLD LSKRKQNSRV QVLPNGTLSI QRVEIQDRGQ YLCSASNLFG TDHLHVTLSV
VSYPPRILER RTKEITVHSG STVELKCRAE GRPSPTVTWI LANQTVVSES SQGSRQAVVT
VDGTLVLHNL SIYDRGFYKC VASNPGGQDS LLVKIQVIAA PPVILEQRRQ VIVGTWGESL
KLPCTAKGTP QPSVYWVLSD GTEVKPLQFT NSKLFLFSNG TLYIRNLASS DRGTYECIAT
SSTGSERRVV MLTMEERVTS PRIEAASQKR TEVNFGDKLL LNCSATGEPK PQIMWRLPSK
AVVDQQHRVG SWIHVYPNGS LFIGSVTEKD SGVYLCVARN KMGDDLILMH VSLRLKPAKI
DHKQYFRKQV LHGKDFQVDC KASGSPVPEI SWSLPDGTMI NNAMQADDSG HRTRRYTLFN
NGTLYFNKVG VAEEGDYTCY AQNTLGKDEM KVHLTVITAA PRIRQSNKTN KRIKAGDTAV
LDCEVTGDPK PKIFWLLPSN DMISFSIDRY TFHANGSLTI NKVKLLDSGE YVCVARNPSG
DDTKMYKLDV VSKPPLINGL YTNRTVIKAT AVRHSKKHFD CRAEGTPSPE VMWIMPDNIF
LTAPYYGSRI TVHKNGTLEI RNVRLSDSAD FICVARNEGG ESVLVVQLEV LEMLRRPTFR
NPFNEKIVAQ LGKSTALNCS VDGNPPPEII WILPNGTRFS NGPQSYQYLI ASNGSFIISK
TTREDAGKYR CAARNKVGYI EKLVILEIGQ KPVILTYAPG TVKGISGESL SLHCVSDGIP
KPNIKWTMPS GYVVDRPQIN GKYILHDNGT LVIKEATAYD RGNYICKAQN SVGHTLITVP
VMIVAYPPRI TNRPPRSIVT RTGAAFQLHC VALGVPKPEI TWEMPDHSLL STASKERTHG
SEQLHLQGTL VIQNPQTSDS GIYKCTAKNP LGSDYAATYI QVI


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IGS10_MOUSE ELISA Kit FOR Immunoglobulin superfamily member 10; organism: Mouse; gene name: Igsf10 96T
CSB-EL011556RA Rat immunoglobulin superfamily, member 10 (IGSF10) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL011556HU Human immunoglobulin superfamily, member 10 (IGSF10) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL011556MO Mouse immunoglobulin superfamily, member 10 (IGSF10) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB05120 CADM1,Cell adhesion molecule 1,Homo sapiens,Human,IgSF4,IGSF4,IGSF4A,Immunoglobulin superfamily member 4,NECL2,NECL-2,Nectin-like protein 2,SgIgSF,Spermatogenic immunoglobulin superfamily,Synaptic cel
EIAAB05121 Cadm1,Cell adhesion molecule 1,IgSF4,Igsf4,Immunoglobulin superfamily member 4,Mouse,Mus musculus,Necl2,NECL-2,Nectin-like protein 2,Ra175,SgIgSF,Spermatogenic immunoglobulin superfamily,Synaptic cell
27-975 Kinesin is the founding member of a superfamily of microtubule based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation. Kinesin consists of heav 0.05 mg
27-974 Kinesin is the founding member of a superfamily of microtubule based motor proteins that perform force-generating tasks such as organelle transport and chromosome segregation. Kinesin consists of heav 0.05 mg
E0273h ELISA kit Homo sapiens,Human,IGDC1,IgSF1,IGSF1,Immunoglobulin superfamily member 1,Immunoglobulin-like domain-containing protein 1,InhBP,Inhibin-binding protein,KIAA0364,p120,PGSF2,Pituitary gland-sp 96T
E0273h ELISA Homo sapiens,Human,IGDC1,IgSF1,IGSF1,Immunoglobulin superfamily member 1,Immunoglobulin-like domain-containing protein 1,InhBP,Inhibin-binding protein,KIAA0364,p120,PGSF2,Pituitary gland-specifi 96T
U0273h CLIA Homo sapiens,Human,IGDC1,IgSF1,IGSF1,Immunoglobulin superfamily member 1,Immunoglobulin-like domain-containing protein 1,InhBP,Inhibin-binding protein,KIAA0364,p120,PGSF2,Pituitary gland-specific 96T
EIAAB44562 Dasm1,Dendrite arborization and synapse maturation protein 1,Igsf9,IgSF9A,Igsf9a,Immunoglobulin superfamily member 9A,Protein turtle homolog A,Rat,Rattus norvegicus
EIAAB44561 Dasm1,Dendrite arborization and synapse maturation protein 1,Igsf9,IgSF9A,Igsf9a,Immunoglobulin superfamily member 9A,Mouse,Mus musculus,Nrt1,Protein turtle homolog A
EIAAB05129 Cadm4,Cell adhesion molecule 4,IgSF4C,Igsf4c,Immunoglobulin superfamily member 4C,Mouse,Mus musculus,Necl4,NECL-4,Nectin-like protein 4,TSLC1-like protein 2,Tsll2
EIAAB05126 Brain immunoglobulin receptor,CADM3,Cell adhesion molecule 3,Homo sapiens,Human,IgSF4B,IGSF4B,Immunoglobulin superfamily member 4B,NECL1,NECL-1,Nectin-like protein 1,Synaptic cell adhesion molecule 3,
C948 Immunoglobulin Superfamily Member 8 IGSF8 lmg
18-003-43717 Immunoglobulin superfamily member 1 - N_A Polyclonal 0.1 mg Protein A
ARP44704_P050 IGSF11(immunoglobulin superfamily, member 11) 50 µg