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NCAM2 / OCAM Antibody (C-Term)

Peptide-affinity purified goat antibody

     
  • IHC - NCAM2 / OCAM Antibody (C-Term) AF2467a
    AF2467a (0.5 µg/ml) 24h-staining of PFA-perfused cryosection of Mouse Olfactory bub. Antigen retrieval with methanol (-20C, 10min) followed by 1% SDS(10min), IF-staning. Data obtained from anonymous customer.
  • IHC - NCAM2 / OCAM Antibody (C-Term) AF2467a
    AF2467a (0.5 µg/ml) 48h-staining of PFA-perfused cryosection of Mouse Olfactory bulb. Antigen retrieval with citrate buffer pH 6 at 95C for 10min, IF-staning for NCAM2 (red), VGLUT2 (blue) and NQO1 (green), data obtained from anonymus customer.
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
IHC, E
Primary Accession O15394
Other Accession NP_004531.2, 4685, 17968 (mouse), 288280 (rat)
Reactivity Mouse
Predicted Human, Rat, Dog, Cow
Host Goat
Clonality Polyclonal
Concentration 0.5 mg/ml
Isotype IgG
Additional Information
Other Names Neural cell adhesion molecule 2, N-CAM-2, NCAM-2, NCAM2, NCAM21
Format 0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsNCAM2 / OCAM Antibody (C-Term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name NCAM2
Synonyms NCAM21
Function May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons.
Cellular Location Cell membrane; Single-pass type I membrane protein
Tissue Location Expressed most strongly in adult and fetal brain EMBL; U75330; AAB80803.1; -; mRNA EMBL; AK302870; BAH13827.1; -; mRNA EMBL; AP001114; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AP001115; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AP001136; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AP001137; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AP001138; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AP001252; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BC052946; AAH52946.1; -; mRNA CCDS; CCDS42910.1; -. [O15394-1] RefSeq; NP_004531.2; NM_004540.3. [O15394-1] RefSeq; XP_016883847.1; XM_017028358.1. [O15394-2] UniGene; Hs.473450; - PDB; 2DOC; NMR; -; A=486-591 PDB; 2JLL; X-ray; 2.30 A; A=301-689 PDB; 2KBG; NMR; -; A=592-693 PDB; 2V5T; X-ray; 2.00 A; A=115-301 PDB; 2VAJ; X-ray; 2.70 A; A=21-113 PDB; 2WIM; X-ray; 3.00 A; A/B=19-301 PDB; 2XY1; X-ray; 1.90 A; A=209-398 PDB; 2XY2; X-ray; 1.77 A; A=19-207 PDB; 2XYC; X-ray; 2.65 A; A=301-591 PDBsum; 2DOC; - PDBsum; 2JLL; - PDBsum; 2KBG; - PDBsum; 2V5T; - PDBsum; 2VAJ; - PDBsum; 2WIM; - PDBsum; 2XY1; - PDBsum; 2XY2; - PDBsum; 2XYC; - ProteinModelPortal; O15394; - SMR; O15394; - BioGrid; 110765; 2 DIP; DIP-56211N; - IntAct; O15394; 2 STRING; 9606.ENSP00000383392; - iPTMnet; O15394; - PhosphoSitePlus; O15394; - SwissPalm; O15394; - BioMuta; NCAM2; - MaxQB; O15394; - PaxDb; O15394; - PeptideAtlas; O15394; - PRIDE; O15394; - ProteomicsDB; 48635; - Ensembl; ENST00000400546; ENSP00000383392; ENSG00000154654. [O15394-1] GeneID; 4685; - KEGG; hsa:4685; - UCSC; uc002yld.3; human. [O15394-1] CTD; 4685; - DisGeNET; 4685; - EuPathDB; HostDB:ENSG00000154654.14; - GeneCards; NCAM2; - H-InvDB; HIX0027799; - HGNC; HGNC:7657; NCAM2 HPA; HPA030900; - HPA; HPA030901; - MIM; 602040; gene neXtProt; NX_O15394; - OpenTargets; ENSG00000154654; - PharmGKB; PA31460; - eggNOG; ENOG410IQJD; Eukaryota eggNOG; ENOG41118FG; LUCA GeneTree; ENSGT00910000144011; - HOGENOM; HOG000074124; - HOVERGEN; HBG052579; - InParanoid; O15394; - KO; K06491; - OMA; RITNHED; - OrthoDB; EOG091G00V0; - PhylomeDB; O15394; - TreeFam; TF326195; - ChiTaRS; NCAM2; human EvolutionaryTrace; O15394; - GenomeRNAi; 4685; - PRO; PR:O15394; - Proteomes; UP000005640; Chromosome 21 Bgee; ENSG00000154654; - CleanEx; HS_NCAM2; - ExpressionAtlas; O15394; baseline and differential Genevisible; O15394; HS GO; GO:0030424; C:axon; IEA:Ensembl GO; GO:0016021; C:integral component of membrane; TAS:ProtInc GO; GO:0016604; C:nuclear body; IDA:HPA GO; GO:0005886; C:plasma membrane; IDA:HPA GO; GO:0042802; F:identical protein binding; IPI:IntAct GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl GO; GO:0007158; P:neuron cell-cell adhesion; TAS:ProtInc GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl CDD; cd00063; FN3; 2 Gene3D; 2.60.40.10; -; 7 InterPro; IPR003961; FN3_dom InterPro; IPR036116; FN3_sf 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; IPR009138; Neural_cell_adh Pfam; PF00041; fn3; 2 Pfam; PF07679; I-set; 4 PRINTS; PR01838; NCAMFAMILY SMART; SM00060; FN3; 2 SMART; SM00409; IG; 5 SMART; SM00408; IGc2; 5 SMART; SM00406; IGv; 3 SUPFAM; SSF48726; SSF48726; 5 SUPFAM; SSF49265; SSF49265; 1 PROSITE; PS50853; FN3; 2 PROSITE; PS50835; IG_LIKE; 5 1: Evidence at protein level; 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; Complete proteome; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix SIGNAL 1 19 CHAIN 20 837 Neural cell adhesion molecule 2 /FTId=PRO_0000015018 TOPO_DOM 20 697 Extracellular. TRANSMEM 698 718 Helical. TOPO_DOM 719 837 Cytoplasmic. DOMAIN 21 108 Ig-like C2-type 1 DOMAIN 113 202 Ig-like C2-type 2 DOMAIN 208 297 Ig-like C2-type 3 DOMAIN 302 396 Ig-like C2-type 4 DOMAIN 401 491 Ig-like C2-type 5 DOMAIN 498 591 Fibronectin type-III 1 {ECO:0000255|PROSITE-ProRule:PRU00316} DOMAIN 593 688 Fibronectin type-III 2 {ECO:0000255|PROSITE-ProRule:PRU00316} MOD_RES 765 765 Phosphoserine {ECO:0000250|UniProtKB:O35136} MOD_RES 780 780 Phosphothreonine {ECO:0000250|UniProtKB:O35136} MOD_RES 786 786 Phosphoserine {ECO:0000250|UniProtKB:O35136} CARBOHYD 177 177 N-linked (GlcNAc...) asparagine CARBOHYD 219 219 N-linked (GlcNAc...) asparagine CARBOHYD 309 309 N-linked (GlcNAc...) asparagine CARBOHYD 406 406 N-linked (GlcNAc...) asparagine CARBOHYD 419 419 N-linked (GlcNAc...) asparagine CARBOHYD 445 445 N-linked (GlcNAc...) asparagine CARBOHYD 474 474 N-linked (GlcNAc...) asparagine CARBOHYD 562 562 N-linked (GlcNAc...) asparagine DISULFID 42 93 DISULFID 136 186 DISULFID 232 281 DISULFID 322 380 DISULFID 422 475 VAR_SEQ 1 18 MSLLLSFYLLGLLVSSGQ -> MVRSDSGGQVYLDYHNRQG LFVDWKYNEALYLEEGQPETYYRT (in isoform 2) /FTId=VSP_056637 VAR_SEQ 399 399 Y -> S (in isoform 2) /FTId=VSP_056638 VAR_SEQ 400 837 Missing (in isoform 2) /FTId=VSP_056639 VARIANT 347 347 D -> N (in dbSNP:rs35654962) /FTId=VAR_047897 VARIANT 350 350 L -> P (in dbSNP:rs232518) /FTId=VAR_047898 CONFLICT 49 49 E -> R (in Ref. 1; AAB80803) CONFLICT 72 72 E -> G (in Ref. 1; AAB80803) CONFLICT 163 163 F -> L (in Ref. 1; AAB80803) CONFLICT 374 374 D -> G (in Ref. 1; AAB80803) CONFLICT 662 667 YEVQIT -> MKFRLP (in Ref. 1; AAB80803) STRAND 20 26 {ECO:0000244|PDB:2XY2} STRAND 28 33 {ECO:0000244|PDB:2XY2} STRAND 38 46 {ECO:0000244|PDB:2XY2} STRAND 49 54 {ECO:0000244|PDB:2XY2} STRAND 65 72 {ECO:0000244|PDB:2XY2} STRAND 75 80 {ECO:0000244|PDB:2XY2} HELIX 85 87 {ECO:0000244|PDB:2XY2} STRAND 89 96 {ECO:0000244|PDB:2XY2} STRAND 98 100 {ECO:0000244|PDB:2WIM} STRAND 102 112 {ECO:0000244|PDB:2XY2} STRAND 116 119 {ECO:0000244|PDB:2V5T} STRAND 123 127 {ECO:0000244|PDB:2XY2} STRAND 132 134 {ECO:0000244|PDB:2XY2} STRAND 137 139 {ECO:0000244|PDB:2V5T} STRAND 145 150 {ECO:0000244|PDB:2XY2} STRAND 152 154 {ECO:0000244|PDB:2XY2} STRAND 163 165 {ECO:0000244|PDB:2XY2} STRAND 171 173 {ECO:0000244|PDB:2XY2} HELIX 178 180 {ECO:0000244|PDB:2XY2} STRAND 182 190 {ECO:0000244|PDB:2XY2} TURN 191 194 {ECO:0000244|PDB:2XY2} STRAND 195 206 {ECO:0000244|PDB:2XY2} STRAND 210 212 {ECO:0000244|PDB:2XY1} STRAND 217 221 {ECO:0000244|PDB:2XY1} STRAND 222 224 {ECO:0000244|PDB:2WIM} STRAND 228 231 {ECO:0000244|PDB:2XY1} STRAND 233 235 {ECO:0000244|PDB:2XY1} STRAND 241 246 {ECO:0000244|PDB:2XY1} STRAND 254 260 {ECO:0000244|PDB:2XY1} TURN 261 264 {ECO:0000244|PDB:2XY1} STRAND 265 268 {ECO:0000244|PDB:2XY1} HELIX 273 275 {ECO:0000244|PDB:2XY1} STRAND 277 285 {ECO:0000244|PDB:2XY1} STRAND 288 307 {ECO:0000244|PDB:2XY1} STRAND 310 312 {ECO:0000244|PDB:2XY1} STRAND 317 328 {ECO:0000244|PDB:2XY1} STRAND 331 336 {ECO:0000244|PDB:2XY1} TURN 337 340 {ECO:0000244|PDB:2XY1} STRAND 341 343 {ECO:0000244|PDB:2XY1} STRAND 350 352 {ECO:0000244|PDB:2XYC} STRAND 354 359 {ECO:0000244|PDB:2XY1} STRAND 362 369 {ECO:0000244|PDB:2XY1} HELIX 372 374 {ECO:0000244|PDB:2XY1} STRAND 376 384 {ECO:0000244|PDB:2XY1} STRAND 387 397 {ECO:0000244|PDB:2XY1} STRAND 409 412 {ECO:0000244|PDB:2JLL} STRAND 418 422 {ECO:0000244|PDB:2JLL} STRAND 424 428 {ECO:0000244|PDB:2JLL} STRAND 431 436 {ECO:0000244|PDB:2JLL} STRAND 439 442 {ECO:0000244|PDB:2JLL} STRAND 449 453 {ECO:0000244|PDB:2JLL} STRAND 458 462 {ECO:0000244|PDB:2JLL} STRAND 469 479 {ECO:0000244|PDB:2JLL} STRAND 482 492 {ECO:0000244|PDB:2JLL} STRAND 500 507 {ECO:0000244|PDB:2JLL} STRAND 512 517 {ECO:0000244|PDB:2JLL} STRAND 527 536 {ECO:0000244|PDB:2JLL} STRAND 543 546 {ECO:0000244|PDB:2JLL} STRAND 548 550 {ECO:0000244|PDB:2DOC} STRAND 552 556 {ECO:0000244|PDB:2JLL} STRAND 564 575 {ECO:0000244|PDB:2JLL} STRAND 576 580 {ECO:0000244|PDB:2XYC} STRAND 584 587 {ECO:0000244|PDB:2JLL} STRAND 599 604 {ECO:0000244|PDB:2JLL} TURN 605 607 {ECO:0000244|PDB:2JLL} STRAND 608 613 {ECO:0000244|PDB:2JLL} STRAND 619 621 {ECO:0000244|PDB:2KBG} STRAND 625 631 {ECO:0000244|PDB:2JLL} STRAND 640 645 {ECO:0000244|PDB:2KBG} TURN 646 648 {ECO:0000244|PDB:2KBG} STRAND 650 653 {ECO:0000244|PDB:2JLL} STRAND 661 670 {ECO:0000244|PDB:2JLL} STRAND 678 683 {ECO:0000244|PDB:2JLL} SEQUENCE 837 AA; 93046 MW; 878EC1110562B3F3 CRC64; MSLLLSFYLL GLLVSSGQAL LQVTISLSKV ELSVGESKFF TCTAIGEPES IDWYNPQGEK IISTQRVVVQ KEGVRSRLTI YNANIEDAGI YRCQATDAKG QTQEATVVLE IYQKLTFREV VSPQEFKQGE DAEVVCRVSS SPAPAVSWLY HNEEVTTISD NRFAMLANNN LQILNINKSD EGIYRCEGRV EARGEIDFRD IIVIVNVPPA ISMPQKSFNA TAERGEEMTF SCRASGSPEP AISWFRNGKL IEENEKYILK GSNTELTVRN IINSDGGPYV CRATNKAGED EKQAFLQVFV QPHIIQLKNE TTYENGQVTL VCDAEGEPIP EITWKRAVDG FTFTEGDKSL DGRIEVKGQH GSSSLHIKDV KLSDSGRYDC EAASRIGGHQ KSMYLDIEYA PKFISNQTIY YSWEGNPINI SCDVKSNPPA SIHWRRDKLV LPAKNTTNLK TYSTGRKMIL EIAPTSDNDF GRYNCTATNH IGTRFQEYIL ALADVPSSPY GVKIIELSQT TAKVSFNKPD SHGGVPIHHY QVDVKEVASE IWKIVRSHGV QTMVVLNNLE PNTTYEIRVA AVNGKGQGDY SKIEIFQTLP VREPSPPSIH GQPSSGKSFK LSITKQDDGG APILEYIVKY RSKDKEDQWL EKKVQGNKDH IILEHLQWTM GYEVQITAAN RLGYSEPTVY EFSMPPKPNI IKDTLFNGLG LGAVIGLGVA ALLLILVVTD VSCFFIRQCG LLMCITRRMC GKKSGSSGKS KELEEGKAAY LKDGSKEPIV EMRTEDERVT NHEDGSPVNE PNETTPLTEP EKLPLKEEDG KEALNPETIE IKVSNDIIQS KEDDSKA
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Citations (0)

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References

Valproic acid modulates NCAM polysialylation and polysialyltransferase mRNA expression in human tumor cells. Beecken WD, Engl T, Ogbomo H, Relja B, Cinatl J, Bereiter-Hahn J, Oppermann E, Jonas D, Blaheta RA. Int Immunopharmacol. 2005 Apr;5(4):757-69. PMID: 15710344

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Cat# AF2467a
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