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ERP29 Antibody (N-term) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession P30040
Clone Names 81202036
Peptide ID 81202036
Additional Information
Other Names Endoplasmic reticulum resident protein 29, ERp29, Endoplasmic reticulum resident protein 28, ERp28, Endoplasmic reticulum resident protein 31, ERp31, ERP29, C12orf8, ERP28
Target/Specificity The synthetic peptide sequence used to generate the antibody AP2902a was selected from the N-term region of human ERP29. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
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 ERP29
Synonyms C12orf8, ERP28
Function Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
Cellular Location Endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV
Tissue Location Ubiquitous. Mostly expressed in secretory tissues EMBL; X94910; CAA64397.1; -; mRNA EMBL; AA412124; -; NOT_ANNOTATED_CDS; mRNA EMBL; CR541667; CAG46468.1; -; mRNA EMBL; AC073575; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; BC101493; AAI01494.1; -; mRNA EMBL; BC101495; AAI01496.1; -; mRNA CCDS; CCDS44977.1; -. [P30040-2] CCDS; CCDS9158.1; -. [P30040-1] PIR; T09549; T09549 RefSeq; NP_001029197.1; NM_001034025.1. [P30040-2] RefSeq; NP_006808.1; NM_006817.3. [P30040-1] UniGene; Hs.75841; - PDB; 2QC7; X-ray; 2.90 A; A/B=34-261 PDBsum; 2QC7; - ProteinModelPortal; P30040; - SMR; P30040; - BioGrid; 116160; 18 IntAct; P30040; 11 MINT; MINT-5002525; - STRING; 9606.ENSP00000261735; - iPTMnet; P30040; - PhosphoSitePlus; P30040; - SwissPalm; P30040; - BioMuta; ERP29; - DMDM; 6015110; - OGP; P30040; - REPRODUCTION-2DPAGE; IPI00024911; - SWISS-2DPAGE; P30040; - EPD; P30040; - PaxDb; P30040; - PeptideAtlas; P30040; - PRIDE; P30040; - TopDownProteomics; P30040-1; -. [P30040-1] Ensembl; ENST00000261735; ENSP00000261735; ENSG00000089248. [P30040-1] Ensembl; ENST00000455836; ENSP00000412083; ENSG00000089248. [P30040-2] GeneID; 10961; - KEGG; hsa:10961; - UCSC; uc001ttl.1; human. [P30040-1] CTD; 10961; - DisGeNET; 10961; - GeneCards; ERP29; - HGNC; HGNC:13799; ERP29 HPA; HPA039363; - HPA; HPA039456; - MIM; 602287; gene neXtProt; NX_P30040; - OpenTargets; ENSG00000089248; - PharmGKB; PA25509; - eggNOG; ENOG410IX2F; Eukaryota eggNOG; ENOG4111I8S; LUCA GeneTree; ENSGT00390000018566; - HOGENOM; HOG000169611; - HOVERGEN; HBG051508; - InParanoid; P30040; - KO; K09586; - OMA; DGCIKEF; - OrthoDB; EOG091G0NH4; - PhylomeDB; P30040; - TreeFam; TF324701; - BioCyc; ZFISH:ENSG00000089248-MONOMER; - ChiTaRS; ERP29; human EvolutionaryTrace; P30040; - GeneWiki; ERP29; - GenomeRNAi; 10961; - PRO; PR:P30040; - Proteomes; UP000005640; Chromosome 12 Bgee; ENSG00000089248; - CleanEx; HS_ERP29; - ExpressionAtlas; P30040; baseline and differential Genevisible; P30040; HS GO; GO:0009986; C:cell surface; IDA:MGI GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL GO; GO:0005788; C:endoplasmic reticulum lumen; NAS:ParkinsonsUK-UCL GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell GO; GO:0016020; C:membrane; IDA:UniProtKB GO; GO:0005790; C:smooth endoplasmic reticulum; ISS:ParkinsonsUK-UCL GO; GO:0030133; C:transport vesicle; ISS:ParkinsonsUK-UCL GO; GO:0051087; F:chaperone binding; ISS:ParkinsonsUK-UCL GO; GO:0042803; F:protein homodimerization activity; ISS:ParkinsonsUK-UCL GO; GO:0000187; P:activation of MAPK activity; IDA:ParkinsonsUK-UCL GO; GO:0006886; P:intracellular protein transport; NAS:ParkinsonsUK-UCL GO; GO:0010629; P:negative regulation of gene expression; IDA:ParkinsonsUK-UCL GO; GO:0050709; P:negative regulation of protein secretion; IDA:ParkinsonsUK-UCL GO; GO:0010628; P:positive regulation of gene expression; IDA:ParkinsonsUK-UCL GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL GO; GO:0006457; P:protein folding; NAS:ParkinsonsUK-UCL GO; GO:0009306; P:protein secretion; IEA:InterPro GO; GO:0043335; P:protein unfolding; NAS:ParkinsonsUK-UCL GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl CDD; cd00238; ERp29c; 1 Gene3D; 1.20.1150.12; -; 1 Gene3D; 3.40.30.10; -; 1 InterPro; IPR016855; ER_p29 InterPro; IPR011679; ER_p29_C InterPro; IPR012883; ERp29_N InterPro; IPR012336; Thioredoxin-like_fold Pfam; PF07749; ERp29; 1 Pfam; PF07912; ERp29_N; 1 PIRSF; PIRSF027352; ER_p29; 1 SUPFAM; SSF47933; SSF47933; 1 SUPFAM; SSF52833; SSF52833; 1 PROSITE; PS00014; ER_TARGET; 1 1: Evidence at protein level; 3D-structure; Alternative splicing; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Phosphoprotein; Reference proteome; Signal SIGNAL 1 32 CHAIN 33 261 Endoplasmic reticulum resident protein 29 /FTId=PRO_0000021197 MOTIF 258 261 Prevents secretion from ER {ECO:0000255|PROSITE-ProRule:PRU10138} MOD_RES 64 64 Phosphotyrosine; by PKDCC MOD_RES 66 66 Phosphotyrosine; by PKDCC VAR_SEQ 49 53 VIPKS -> IMVTS (in isoform 2) {ECO:0000303|Ref.2} /FTId=VSP_045680 VAR_SEQ 54 261 Missing (in isoform 2) {ECO:0000303|Ref.2} /FTId=VSP_045681 HELIX 45 49 {ECO:0000244|PDB:2QC7} HELIX 50 52 {ECO:0000244|PDB:2QC7} STRAND 54 60 {ECO:0000244|PDB:2QC7} HELIX 68 80 {ECO:0000244|PDB:2QC7} STRAND 86 91 {ECO:0000244|PDB:2QC7} STRAND 96 98 {ECO:0000244|PDB:2QC7} HELIX 102 107 {ECO:0000244|PDB:2QC7} HELIX 112 114 {ECO:0000244|PDB:2QC7} STRAND 116 122 {ECO:0000244|PDB:2QC7} HELIX 138 147 {ECO:0000244|PDB:2QC7} HELIX 159 170 {ECO:0000244|PDB:2QC7} HELIX 174 180 {ECO:0000244|PDB:2QC7} HELIX 183 187 {ECO:0000244|PDB:2QC7} HELIX 193 211 {ECO:0000244|PDB:2QC7} HELIX 217 230 {ECO:0000244|PDB:2QC7} HELIX 235 248 {ECO:0000244|PDB:2QC7} SEQUENCE 261 AA; 28993 MW; 76145006433A1983 CRC64; MAAAVPRAAF LSPLLPLLLG FLLLSAPHGG SGLHTKGALP LDTVTFYKVI PKSKFVLVKF DTQYPYGEKQ DEFKRLAENS ASSDDLLVAE VGISDYGDKL NMELSEKYKL DKESYPVFYL FRDGDFENPV PYTGAVKVGA IQRWLKGQGV YLGMPGCLPV YDALAGEFIR ASGVEARQAL LKQGQDNLSS VKETQKKWAE QYLKIMGKIL DQGEDFPASE MTRIARLIEK NKMSDGKKEE LQKSLNILTA FQKKGAEKEE L
Research Areas
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Background

ERP29 shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER.

References

Bambang,I.F., et.al., Exp. Cell Res. 315 (11), 1964-1974 (2009)

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$ 80.00
Cat# BP2902a
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