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FOXK1 Antibody (C-term) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession P85037
Peptide ID 36104
Additional Information
Other Names Forkhead box protein K1, Myocyte nuclear factor, MNF, FOXK1 {ECO:0000303|PubMed:15202027, ECO:0000303|PubMed:15289879}
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 FOXK1 {ECO:0000303|PubMed:15202027, ECO:0000303|PubMed:15289879}
Function Transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin gene (By similarity). Important regulatory factor of the myogenic progenitor cell population (By similarity). Involved in the cell cycle process, promotes proliferation by repressing Foxo4 transcriptional activity and the cyclin-dependent kinase inhibitor, p21CIP, in the myogenic progenitor cells (By similarity). Represses myogenic differentiation by inhibiting MEFC acitivity (By similarity). Has a role in remodeling processes of adult muscles that occur in response to physiological stimuli (By similarity). Required to correct temporal orchestration of molecular and cellular events necessary for muscle repair (By similarity). Positively regulates Wnt/beta-catenin signaling by translocating DVL into the nucleus (PubMed:25805136). Reduces virus replication, probably by binding the interferon stimulated response element (ISRE) to promote antiviral gene expression (PubMed:25852164).
Cellular Location Nucleus. Cytoplasm. Note=(Microbial infection) Accumulates in the nucleus upon viral infection
Tissue Location Expressed both developing and adult tissues. In adults, significant expression is seen in tumors of the brain, colon and lymph node. EMBL; AK122663; -; NOT_ANNOTATED_CDS; mRNA EMBL; AC072054; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AC092428; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AC092610; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BC038434; -; NOT_ANNOTATED_CDS; mRNA EMBL; CB959941; -; NOT_ANNOTATED_CDS; mRNA EMBL; AW206906; -; NOT_ANNOTATED_CDS; mRNA CCDS; CCDS34591.1; -. [P85037-1] RefSeq; NP_001032242.1; NM_001037165.1. [P85037-1] RefSeq; XP_011513493.1; XM_011515191.2. [P85037-2] UniGene; Hs.487393; - ProteinModelPortal; P85037; - SMR; P85037; - BioGrid; 128769; 104 IntAct; P85037; 67 MINT; P85037; - STRING; 9606.ENSP00000328720; - iPTMnet; P85037; - PhosphoSitePlus; P85037; - BioMuta; FOXK1; - DMDM; 118572324; - EPD; P85037; - jPOST; P85037; - MaxQB; P85037; - PaxDb; P85037; - PeptideAtlas; P85037; - PRIDE; P85037; - ProteomicsDB; 57762; - ProteomicsDB; 57763; -. [P85037-2] Ensembl; ENST00000328914; ENSP00000328720; ENSG00000164916. [P85037-1] GeneID; 221937; - KEGG; hsa:221937; - UCSC; uc003snc.2; human. [P85037-1] CTD; 221937; - DisGeNET; 221937; - EuPathDB; HostDB:ENSG00000164916.10; - GeneCards; FOXK1; - HGNC; HGNC:23480; FOXK1 HPA; HPA017998; - HPA; HPA018864; - MIM; 616302; gene neXtProt; NX_P85037; - OpenTargets; ENSG00000164916; - PharmGKB; PA134978307; - eggNOG; KOG2294; Eukaryota eggNOG; COG5025; LUCA GeneTree; ENSGT00940000159507; - HOGENOM; HOG000072588; - HOVERGEN; HBG051649; - InParanoid; P85037; - KO; K09404; - OMA; VTIGQHH; - OrthoDB; 1270467at2759; - PhylomeDB; P85037; - TreeFam; TF325718; - Reactome; R-HSA-5689603; UCH proteinases ChiTaRS; FOXK1; human GeneWiki; FOXK1; - GenomeRNAi; 221937; - PRO; PR:P85037; - Proteomes; UP000005640; Chromosome 7 Bgee; ENSG00000164916; Expressed in 212 organ(s), highest expression level in cerebellar vermis ExpressionAtlas; P85037; baseline and differential Genevisible; P85037; HS GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell GO; GO:0005654; C:nucleoplasm; TAS:Reactome GO; GO:0005634; C:nucleus; IBA:GO_Central GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IBA:GO_Central GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl GO; GO:0016579; P:protein deubiquitination; TAS:Reactome CDD; cd00059; FH; 1 CDD; cd00060; FHA; 1 Gene3D;; -; 1 InterPro; IPR000253; FHA_dom InterPro; IPR001766; Fork_head_dom InterPro; IPR008984; SMAD_FHA_dom_sf InterPro; IPR018122; TF_fork_head_CS_1 InterPro; IPR030456; TF_fork_head_CS_2 InterPro; IPR036388; WH-like_DNA-bd_sf InterPro; IPR036390; WH_DNA-bd_sf Pfam; PF00498; FHA; 1 Pfam; PF00250; Forkhead; 1 PRINTS; PR00053; FORKHEAD SMART; SM00339; FH; 1 SMART; SM00240; FHA; 1 SUPFAM; SSF46785; SSF46785; 1 SUPFAM; SSF49879; SSF49879; 1 PROSITE; PS50006; FHA_DOMAIN; 1 PROSITE; PS00657; FORK_HEAD_1; 1 PROSITE; PS00658; FORK_HEAD_2; 1 PROSITE; PS50039; FORK_HEAD_3; 1 1: Evidence at protein level; Acetylation; Activator; Alternative splicing; Complete proteome; Cytoplasm; Developmental protein; Differentiation; DNA-binding; Methylation; Myogenesis; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation INIT_MET 1 1 Removed. CHAIN 2 733 Forkhead box protein K1 /FTId=PRO_0000261667 DOMAIN 123 175 FHA. {ECO:0000255|PROSITE- ProRule:PRU00086} DNA_BIND 305 400 Fork-head. {ECO:0000255|PROSITE- ProRule:PRU00089} REGION 2 40 Interaction with SIN3A and SIN3B {ECO:0000250|UniProtKB:P42128} REGION 95 420 Required for interaction with FOXO4 and MEF2C. {ECO:0000250|UniProtKB:P42128} COMPBIAS 10 96 Ala-rich. COMPBIAS 35 62 Pro-rich. MOD_RES 2 2 N-acetylalanine MOD_RES 101 101 Phosphoserine MOD_RES 161 161 Omega-N-methylarginine MOD_RES 191 191 Omega-N-methylarginine MOD_RES 213 213 Phosphoserine MOD_RES 223 223 Phosphoserine MOD_RES 239 239 Phosphoserine MOD_RES 243 243 Phosphoserine MOD_RES 245 245 Phosphothreonine {ECO:0000250|UniProtKB:P42128} MOD_RES 247 247 Phosphothreonine {ECO:0000250|UniProtKB:P42128} MOD_RES 253 253 Phosphoserine MOD_RES 257 257 Phosphoserine MOD_RES 295 295 Phosphoserine {ECO:0000250|UniProtKB:P42128} MOD_RES 299 299 Phosphoserine MOD_RES 416 416 Phosphoserine MOD_RES 420 420 Phosphoserine MOD_RES 422 422 Phosphothreonine MOD_RES 428 428 Phosphoserine MOD_RES 436 436 Phosphothreonine MOD_RES 441 441 Phosphoserine MOD_RES 445 445 Phosphoserine MOD_RES 459 459 Phosphoserine VAR_SEQ 1 163 Missing (in isoform 2) /FTId=VSP_052239 VAR_SEQ 164 187 GKNGVFVDGAFQRRGAPALQLPKQ -> MAYCLGVNFVPSR FCYQLHRLLLR (in isoform 2) /FTId=VSP_052240 MUTAGEN 355 355 H->A: No effect on interaction with DVL2 CONFLICT 144 144 I -> V (in Ref. 3; CB959941) CONFLICT 154 155 QE -> KS (in Ref. 3; CB959941) CONFLICT 159 159 Y -> S (in Ref. 3; CB959941) CONFLICT 217 217 P -> A (in Ref. 4; AW206906) CONFLICT 232 232 P -> T (in Ref. 4; AW206906) CONFLICT 437 445 Missing (in Ref. 1; AK122663) SEQUENCE 733 AA; 75457 MW; C9EF4AC3C959A1C3 CRC64; MAEVGEDSGA RALLALRSAP CSPVLCAAAA AAAFPAAAPP PAPAQPQPPP GPPPPPPPPL PPGAIAGAGS SGGSSGVSGD SAVAGAAPAL VAAAAASVRQ SPGPALARLE GREFEFLMRQ PSVTIGRNSS QGSVDLSMGL SSFISRRHLQ LSFQEPHFYL RCLGKNGVFV DGAFQRRGAP ALQLPKQCTF RFPSTAIKIQ FTSLYHKEEA PASPLRPLYP QISPLKIHIP EPDLRSMVSP VPSPTGTISV PNSCPASPRG AGSSSYRFVQ NVTSDLQLAA EFAAKAASEQ QADTSGGDSP KDESKPPFSY AQLIVQAISS AQDRQLTLSG IYAHITKHYP YYRTADKGWQ NSIRHNLSLN RYFIKVPRSQ EEPGKGSFWR IDPASEAKLV EQAFRKRRQR GVSCFRTPFG PLSSRSAPAS PTHPGLMSPR SGGLQTPECL SREGSPIPHD PEFGSKLASV PEYRYSQSAP GSPVSAQPVI MAVPPRPSSL VAKPVAYMPA SIVTSQQPAG HAIHVVQQAP TVTMVRVVTT SANSANGYIL TSQGAAGGSH DAAGAAVLDL GSEARGLEEK PTIAFATIPA AGGVIQTVAS QMAPGVPGHT VTILQPATPV TLGQHHLPVR AVTQNGKHAV PTNSLAGNAY ALTSPLQLLA TQASSSAPVV VTRVCEVGPK EPAAAVAATA TTTPATATTA SASASSTGEP EVKRSRVEEP SGAVTTPAGV IAAAGPQGPG TGE
Research Areas
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FOXK1 is a transcriptional activator that binds to the upstream enhancer region (CCAC box) of myoglobin gene. It plays a role in myogenic differentiation and in remodeling processes of adult muscles that occur in response to physiological stimuli.


Olsen, J.V., et al. Cell 127(3):635-648(2006)Tsai, K.L., et al. J. Biol. Chem. 281(25):17400-17409(2006)Huang, J.T., et al. Int. J. Oncol. 25(3):751-757(2004)Katoh, M., et al. Int. J. Mol. Med. 14(1):127-132(2004)

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Cat# BP9880b
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