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Goat Anti-FHL3 / SLIM2 Antibody

Peptide-affinity purified goat antibody

     
  • WB - Goat Anti-FHL3 / SLIM2 Antibody AF1416a
    AF1416a (1 µg/ml) staining of Human Skeletal Muscle lysate (35 µg protein in RIPA buffer). Primary incubation was 1 hour. Detected by chemiluminescence.
  • SPECIFICATION
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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
WB, E
Primary Accession Q13643
Other Accession NP_004459, 2275, 56726 (mouse), 302363 (rat)
Reactivity Human, Mouse, Rat
Predicted Pig, Cow
Host Goat
Clonality Polyclonal
Concentration 100ug/200ul
Isotype IgG
Additional Information
Other Names Four and a half LIM domains protein 3, FHL-3, Skeletal muscle LIM-protein 2, SLIM-2, FHL3, SLIM2
Format 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, 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.
PrecautionsGoat Anti-FHL3 / SLIM2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name FHL3
Synonyms SLIM2
Tissue Location Expressed only in skeletal muscle. EMBL; U60116; AAC04466.2; -; mRNA EMBL; AK290641; BAF83330.1; -; mRNA EMBL; BT007052; AAP35701.1; -; mRNA EMBL; CR457425; CAG33706.1; -; mRNA EMBL; AL603790; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; CH471059; EAX07301.1; -; Genomic_DNA EMBL; CH471059; EAX07302.1; -; Genomic_DNA EMBL; BC001351; AAH01351.1; -; mRNA EMBL; BC011697; AAH11697.1; -; mRNA CCDS; CCDS30678.1; - PIR; T09504; T09504 RefSeq; NP_001230807.1; NM_001243878.1 RefSeq; NP_004459.2; NM_004468.4 UniGene; Hs.57687; - PDB; 1WYH; NMR; -; A=101-159 PDB; 2CUQ; NMR; -; A=152-218 PDB; 2EHE; NMR; -; A=30-99 PDBsum; 1WYH; - PDBsum; 2CUQ; - PDBsum; 2EHE; - ProteinModelPortal; Q13643; - SMR; Q13643; - BioGrid; 108566; 128 CORUM; Q13643; - DIP; DIP-42030N; - IntAct; Q13643; 151 MINT; Q13643; - STRING; 9606.ENSP00000362107; - iPTMnet; Q13643; - PhosphoSitePlus; Q13643; - BioMuta; FHL3; - DMDM; 209572768; - EPD; Q13643; - MaxQB; Q13643; - PaxDb; Q13643; - PeptideAtlas; Q13643; - PRIDE; Q13643; - ProteomicsDB; 59647; - DNASU; 2275; - Ensembl; ENST00000373016; ENSP00000362107; ENSG00000183386 GeneID; 2275; - KEGG; hsa:2275; - UCSC; uc001cck.4; human CTD; 2275; - DisGeNET; 2275; - EuPathDB; HostDB:ENSG00000183386.9; - GeneCards; FHL3; - HGNC; HGNC:3704; FHL3 HPA; HPA045723; - MIM; 602790; gene neXtProt; NX_Q13643; - OpenTargets; ENSG00000183386; - PharmGKB; PA28142; - eggNOG; KOG1704; Eukaryota eggNOG; ENOG410XP0W; LUCA GeneTree; ENSGT00760000118910; - HOGENOM; HOG000231075; - HOVERGEN; HBG074526; - InParanoid; Q13643; - OMA; YEDRHYH; - OrthoDB; EOG091G07C5; - PhylomeDB; Q13643; - TreeFam; TF314113; - SignaLink; Q13643; - ChiTaRS; FHL3; human EvolutionaryTrace; Q13643; - GeneWiki; FHL3; - GenomeRNAi; 2275; - PRO; PR:Q13643; - Proteomes; UP000005640; Chromosome 1 Bgee; ENSG00000183386; - CleanEx; HS_FHL3; - Genevisible; Q13643; HS GO; GO:0005925; C:focal adhesion; HDA:UniProtKB GO; GO:0005634; C:nucleus; IEA:Ensembl GO; GO:0001725; C:stress fiber; IEA:Ensembl GO; GO:0030018; C:Z disc; IEA:Ensembl GO; GO:0003779; F:actin binding; IEA:Ensembl GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl GO; GO:0007517; P:muscle organ development; TAS:ProtInc InterPro; IPR037987; FHL2/3/5 InterPro; IPR001781; Znf_LIM PANTHER; PTHR24205; PTHR24205; 1 Pfam; PF00412; LIM; 4 SMART; SM00132; LIM; 4 PROSITE; PS00478; LIM_DOMAIN_1; 4 PROSITE; PS50023; LIM_DOMAIN_2; 4 1: Evidence at protein level; 3D-structure; Acetylation; Complete proteome; LIM domain; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger INIT_MET 1 1 Removed. CHAIN 2 280 Four and a half LIM domains protein 3 /FTId=PRO_0000075740 DOMAIN 40 92 LIM zinc-binding 1. {ECO:0000255|PROSITE- ProRule:PRU00125} DOMAIN 101 153 LIM zinc-binding 2. {ECO:0000255|PROSITE- ProRule:PRU00125} DOMAIN 162 212 LIM zinc-binding 3. {ECO:0000255|PROSITE- ProRule:PRU00125} DOMAIN 221 275 LIM zinc-binding 4. {ECO:0000255|PROSITE- ProRule:PRU00125} ZN_FING 7 31 C4-type. MOD_RES 2 2 N-acetylserine MOD_RES 157 157 N6-acetyllysine {ECO:0000250|UniProtKB:Q9R059} MOD_RES 235 235 N6-acetyllysine {ECO:0000250|UniProtKB:Q9R059} CONFLICT 82 82 C -> R (in Ref. 1; AAC04466) CONFLICT 130 130 S -> I (in Ref. 1; AAC04466) CONFLICT 140 140 S -> P (in Ref. 1; AAC04466) CONFLICT 157 157 K -> N (in Ref. 1; AAC04466) CONFLICT 166 166 S -> T (in Ref. 1; AAC04466) CONFLICT 174 174 V -> L (in Ref. 1; AAC04466) CONFLICT 179 179 Q -> L (in Ref. 1; AAC04466) CONFLICT 183 184 RE -> PK (in Ref. 1; AAC04466) CONFLICT 250 252 SCA -> TCD (in Ref. 1; AAC04466) CONFLICT 252 252 A -> D (in Ref. 4; CAG33706) CONFLICT 256 256 T -> N (in Ref. 1; AAC04466) TURN 41 43 {ECO:0000244|PDB:2EHE} TURN 63 65 {ECO:0000244|PDB:2EHE} TURN 69 71 {ECO:0000244|PDB:2EHE} STRAND 80 83 {ECO:0000244|PDB:2EHE} STRAND 86 89 {ECO:0000244|PDB:2EHE} TURN 90 92 {ECO:0000244|PDB:2EHE} STRAND 102 104 {ECO:0000244|PDB:1WYH} STRAND 110 112 {ECO:0000244|PDB:1WYH} TURN 124 126 {ECO:0000244|PDB:1WYH} TURN 130 132 {ECO:0000244|PDB:1WYH} TURN 136 138 {ECO:0000244|PDB:1WYH} STRAND 141 144 {ECO:0000244|PDB:1WYH} STRAND 147 150 {ECO:0000244|PDB:1WYH} HELIX 151 157 {ECO:0000244|PDB:1WYH} TURN 163 165 {ECO:0000244|PDB:2CUQ} STRAND 174 181 {ECO:0000244|PDB:2CUQ} TURN 183 185 {ECO:0000244|PDB:2CUQ} STRAND 189 191 {ECO:0000244|PDB:2CUQ} STRAND 200 202 {ECO:0000244|PDB:2CUQ} STRAND 204 209 {ECO:0000244|PDB:2CUQ} HELIX 210 216 {ECO:0000244|PDB:2CUQ} SEQUENCE 280 AA; 31192 MW; D1A037C260370DFD CRC64; MSESFDCAKC NESLYGRKYI QTDSGPYCVP CYDNTFANTC AECQQLIGHD SRELFYEDRH FHEGCFRCCR CQRSLADEPF TCQDSELLCN DCYCSAFSSQ CSACGETVMP GSRKLEYGGQ TWHEHCFLCS GCEQPLGSRS FVPDKGAHYC VPCYENKFAP RCARCSKTLT QGGVTYRDQP WHRECLVCTG CQTPLAGQQF TSRDEDPYCV ACFGELFAPK CSSCKRPIVG LGGGKYVSFE DRHWHHNCFS CARCSTSLVG QGFVPDGDQV LCQGCSQAGP
Research Areas
Citations (0)

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Background

LIM proteins are defined by the possession of a highly conserved double zinc finger motif called the LIM domain.

References

Identification of the transactivation domain of the human FHL3. Huang X, et al. Mol Biol (Mosk), 2010 Mar-Apr. PMID 20586194.
Human four-and-a-half LIM family members suppress tumor cell growth through a TGF-beta-like signaling pathway. Ding L, et al. J Clin Invest, 2009 Feb. PMID 19139564.
FHL3 binds MyoD and negatively regulates myotube formation. Cottle DL, et al. J Cell Sci, 2007 Apr 15. PMID 17389685.
Towards a proteome-scale map of the human protein-protein interaction network. Rual JF, et al. Nature, 2005 Oct 20. PMID 16189514.
The SRF target gene Fhl2 antagonizes RhoA/MAL-dependent activation of SRF. Philippar U, et al. Mol Cell, 2004 Dec 22. PMID 15610731.

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$ 335.00
Cat# AF1416a
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