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>   home   >   Products   >   Peptides   >   Blocking Peptides   >   UNC45A Antibody (N-term) Blocking peptide   

UNC45A Antibody (N-term) Blocking peptide

Synthetic peptide

Product Information
Primary Accession Q9H3U1
Clone Names 100405095
Peptide ID 100405095
Additional Information
Other Names Protein unc-45 homolog A, Unc-45A, GCUNC-45, Smooth muscle cell-associated protein 1, SMAP-1, UNC45A, SMAP1
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name UNC45A
Synonyms SMAP1
Function Acts as co-chaperone for HSP90. Prevents the stimulation of HSP90AB1 ATPase activity by AHSA1. Positive factor in promoting PGR function in the cell. May be necessary for proper folding of myosin (Potential). Necessary for normal cell proliferation. Necessary for normal myotube formation and myosin accumulation during muscle cell development. May play a role in erythropoiesis in stroma cells in the spleen (By similarity).
Cellular Location Cytoplasm. Cytoplasm, perinuclear region Nucleus. Note=Predominant in the perinuclear region. Little protein in the nucleus
Tissue Location Detected in peripheral blood leukocytes, bone marrow, adrenal gland, trachea, spinal cord, thyroid, lymph node and stomach. EMBL; AB014729; BAB20266.1; -; mRNA EMBL; AB014736; BAB20273.1; -; mRNA EMBL; AL357537; CAB93428.1; -; mRNA EMBL; AL357538; CAB93429.1; -; mRNA EMBL; AK291622; BAF84311.1; -; mRNA EMBL; AK125721; BAG54239.1; -; mRNA EMBL; CH471101; EAX02127.1; -; Genomic_DNA EMBL; BC006214; AAH06214.1; -; mRNA EMBL; BC010995; AAH10995.2; -; mRNA EMBL; BC037992; AAH37992.1; -; mRNA EMBL; BC045635; AAH45635.1; -; mRNA CCDS; CCDS10367.1; -. [Q9H3U1-1] CCDS; CCDS42082.1; -. [Q9H3U1-2] RefSeq; NP_001034764.1; NM_001039675.1. [Q9H3U1-2] RefSeq; NP_001310548.1; NM_001323619.1. [Q9H3U1-1] RefSeq; NP_001310550.1; NM_001323621.1. [Q9H3U1-2] RefSeq; NP_061141.2; NM_018671.4. [Q9H3U1-1] RefSeq; XP_011520081.1; XM_011521779.2 UniGene; Hs.389461; - PDB; 2DBA; NMR; -; A=1-135 PDBsum; 2DBA; - ProteinModelPortal; Q9H3U1; - SMR; Q9H3U1; - BioGrid; 120986; 94 IntAct; Q9H3U1; 62 MINT; Q9H3U1; - STRING; 9606.ENSP00000407487; - iPTMnet; Q9H3U1; - PhosphoSitePlus; Q9H3U1; - SwissPalm; Q9H3U1; - BioMuta; UNC45A; - DMDM; 74761419; - EPD; Q9H3U1; - jPOST; Q9H3U1; - MaxQB; Q9H3U1; - PaxDb; Q9H3U1; - PeptideAtlas; Q9H3U1; - PRIDE; Q9H3U1; - ProteomicsDB; 80756; - ProteomicsDB; 80757; -. [Q9H3U1-2] ProteomicsDB; 80758; -. [Q9H3U1-3] DNASU; 55898; - Ensembl; ENST00000394275; ENSP00000377816; ENSG00000140553. [Q9H3U1-2] Ensembl; ENST00000418476; ENSP00000407487; ENSG00000140553. [Q9H3U1-1] GeneID; 55898; - KEGG; hsa:55898; - UCSC; uc002bqd.3; human. [Q9H3U1-1] CTD; 55898; - DisGeNET; 55898; - EuPathDB; HostDB:ENSG00000140553.16; - GeneCards; UNC45A; - HGNC; HGNC:30594; UNC45A HPA; HPA039228; - MIM; 611219; gene neXtProt; NX_Q9H3U1; - OpenTargets; ENSG00000140553; - PharmGKB; PA142670638; - eggNOG; KOG4151; Eukaryota eggNOG; ENOG410XQNT; LUCA GeneTree; ENSGT00940000159320; - HOGENOM; HOG000285994; - HOVERGEN; HBG057344; - InParanoid; Q9H3U1; - KO; K21991; - OMA; QSRTMAI; - OrthoDB; 1059433at2759; - PhylomeDB; Q9H3U1; - TreeFam; TF314096; - ChiTaRS; UNC45A; human EvolutionaryTrace; Q9H3U1; - GeneWiki; UNC45A; - GenomeRNAi; 55898; - PRO; PR:Q9H3U1; - Proteomes; UP000005640; Chromosome 15 Bgee; ENSG00000140553; Expressed in 212 organ(s), highest expression level in lower esophagus ExpressionAtlas; Q9H3U1; baseline and differential Genevisible; Q9H3U1; HS GO; GO:0005829; C:cytosol; IDA:HPA GO; GO:0005794; C:Golgi apparatus; IDA:HPA GO; GO:0016607; C:nuclear speck; IDA:HPA GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW Gene3D;; -; 2 Gene3D;; -; 1 InterPro; IPR011989; ARM-like InterPro; IPR016024; ARM-type_fold InterPro; IPR013026; TPR-contain_dom InterPro; IPR011990; TPR-like_helical_dom_sf InterPro; IPR019734; TPR_repeat InterPro; IPR024660; UCS_central_dom Pfam; PF13181; TPR_8; 1 Pfam; PF11701; UNC45-central; 1 SMART; SM00028; TPR; 3 SUPFAM; SSF48371; SSF48371; 2 SUPFAM; SSF48452; SSF48452; 1 PROSITE; PS50005; TPR; 3 PROSITE; PS50293; TPR_REGION; 1 1: Evidence at protein level; 3D-structure; Acetylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Myogenesis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; TPR repeat CHAIN 1 944 Protein unc-45 homolog A /FTId=PRO_0000249888 REPEAT 21 54 TPR 1 REPEAT 58 91 TPR 2 REPEAT 92 125 TPR 3 MOD_RES 15 15 Phosphothreonine MOD_RES 70 70 N6-acetyllysine MOD_RES 483 483 N6-acetyllysine VAR_SEQ 1 722 Missing (in isoform 3) {ECO:0000303|Ref.2} /FTId=VSP_020584 VAR_SEQ 1 17 MTVSGPGTPEPRPATPG -> MT (in isoform 2) {ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1, ECO:0000303|Ref.2} /FTId=VSP_020585 VARIANT 796 796 T -> M (in dbSNP:rs8041035) /FTId=VAR_052629 MUTAGEN 33 33 K->E: Abolishes interaction with HSP90AB1; when associated with D-40. No effect on interaction with PGR MUTAGEN 40 40 A->D: Abolishes interaction with HSP90AB1; when associated with E-33. No effect on interaction with PGR MUTAGEN 70 70 K->E: Abolishes interaction with HSP90AB1; when associated with D-77. No effect on interaction with PGR MUTAGEN 77 77 A->D: Abolishes interaction with HSP90AB1; when associated with E-70. No effect on interaction with PGR CONFLICT 921 921 T -> R (in Ref. 2; CAB93429) HELIX 21 32 {ECO:0000244|PDB:2DBA} TURN 33 35 {ECO:0000244|PDB:2DBA} HELIX 37 48 {ECO:0000244|PDB:2DBA} HELIX 54 70 {ECO:0000244|PDB:2DBA} HELIX 74 87 {ECO:0000244|PDB:2DBA} HELIX 92 105 {ECO:0000244|PDB:2DBA} HELIX 108 121 {ECO:0000244|PDB:2DBA} HELIX 126 135 {ECO:0000244|PDB:2DBA} SEQUENCE 944 AA; 103077 MW; 398707D0FF2A703D CRC64; MTVSGPGTPE PRPATPGASS VEQLRKEGNE LFKCGDYGGA LAAYTQALGL DATPQDQAVL HRNRAACHLK LEDYDKAETE ASKAIEKDGG DVKALYRRSQ ALEKLGRLDQ AVLDLQRCVS LEPKNKVFQE ALRNIGGQIQ EKVRYMSSTD AKVEQMFQIL LDPEEKGTEK KQKASQNLVV LAREDAGAEK IFRSNGVQLL QRLLDMGETD LMLAALRTLV GICSEHQSRT VATLSILGTR RVVSILGVES QAVSLAACHL LQVMFDALKE GVKKGFRGKE GAIIVDPARE LKVLISNLLD LLTEVGVSGQ GRDNALTLLI KAVPRKSLKD PNNSLTLWVI DQGLKKILEV GGSLQDPPGE LAVTANSRMS ASILLSKLFD DLKCDAEREN FHRLCENYIK SWFEGQGLAG KLRAIQTVSC LLQGPCDAGN RALELSGVME SVIALCASEQ EEEQLVAVEA LIHAAGKAKR ASFITANGVS LLKDLYKCSE KDSIRIRALV GLCKLGSAGG TDFSMKQFAE GSTLKLAKQC RKWLCNDQID AGTRRWAVEG LAYLTFDADV KEEFVEDAAA LKALFQLSRL EERSVLFAVA SALVNCTNSY DYEEPDPKMV ELAKYAKQHV PEQHPKDKPS FVRARVKKLL AAGVVSAMVC MVKTESPVLT SSCRELLSRV FLALVEEVED RGTVVAQGGG RALIPLALEG TDVGQTKAAQ ALAKLTITSN PEMTFPGERI YEVVRPLVSL LHLNCSGLQN FEALMALTNL AGISERLRQK ILKEKAVPMI EGYMFEEHEM IRRAATECMC NLAMSKEVQD LFEAQGNDRL KLLVLYSGED DELLQRAAAG GLAMLTSMRP TLCSRIPQVT THWLEILQAL LLSSNQELQH RGAVVVLNMV EASREIASTL MESEMMEILS VLAKGDHSPV TRAAAACLDK AVEYGLIQPN QDGE
Research Areas
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UNC45A plays a role in cell proliferation and myoblastfusion, binds progesterone receptor (PGR; MIM 607311) and HSP90(HSPCA; MIM 140571), and acts as a regulator of the progesteronereceptor chaperoning pathway (Price et al., 2002 [PubMed 12356907];Chadli et al., 2006 [PubMed 16478993]).


Chadli, A., et al. J. Biol. Chem. 283(15):9509-9512(2008)Bazzaro, M., et al. Am. J. Pathol. 171(5):1640-1649(2007)Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :Olsen, J.V., et al. Cell 127(3):635-648(2006)Olsen, J.V., et al. Cell 127(3):635-648(2006)

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Cat# BP12832a
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