Mouse PLD4 Protein 3788

$150.00 – $500.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Gln58-Trp503

SKU: 3788parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	Q8BG07
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Phospholipase D4 (PLD4) is a newly identified protein expressed in microglia. the expression of PLD4 was located in macrophages in the colon cancer mesenchymal and lymph nodes as shown by immunohistochemical analysis. furthermore, its expression was associated with clinical staging of colon cancer. Then, THP-1 as a cell model induced into TAMs. PLD4 could be involved in the activation process of M1 phenotype macrophages.
molecular weight	The protein has a predicted MW of 51 kDa. Due to glycosylation, the protein migrates to 60-80 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Mouse PLD4 Protein 3788

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Phospholipase D4 (PLD4) is a newly identified protein expressed in microglia. the expression of PLD4 was located in macrophages in the colon cancer mesenchymal and lymph nodes as shown by immunohistochemical analysis. furthermore, its expression was associated with clinical staging of colon cancer. Then, THP-1 as a cell model induced into TAMs. PLD4 could be involved in the activation process of M1 phenotype macrophages.
Protein names 5'-3' exonuclease PLD4 (EC 3.1.16.1) ((S,S)-bis(monoacylglycero)phosphate synthase PLD4) (EC 3.1.4.-) (Phospholipase D family member 4) (Phospholipase D4)
Gene names Pld4,Pld4
Protein family Phospholipase D family
Mass 56154Da
Function FUNCTION: 5'->3' exonuclease that hydrolyzes the phosphodiester bond of single-stranded DNA (ssDNA) and RNA molecules to form nucleoside 3'-monophosphates and 5'-end 5'-hydroxy deoxyribonucleotide/ribonucleotide fragments. Partially redundant with PLD4, can cleave all four nucleotides displaying higher efficiency for ssDNA and RNA fragments initiated with uridine and guanosine residues and lower efficiency for cytidine-initiated substrates. As a result, it does not always degrade polynucleotides to the single nucleotide level, it can stall at specific sites sparing certain fragments from exonucleolytic degradation (PubMed:30111894, PubMed:34620855, PubMed:38537643). Processes self and pathogenic ssDNA and RNA molecules that reach the endolysosomal compartment via phagocytosis or autophagy and may serve as 'danger' signals for recognition by innate immune receptors such as toll-like receptors (TLRs). Degrades mitochondrial CpG-rich ssDNA fragments to prevent TLR9 activation and autoinflammatory response, but it can cleave viral RNA to generate ligands for TLR7 activation and initiate antiviral immune responses. In plasmacytoid dendritic cells, it cooperates with endonuclease RNASET2 to release 2',3'-cyclic guanosine monophosphate (2',3'-cGMP), a potent stimulatory ligand for TLR7 (PubMed:34620855). Produces 2',3'-cGMPs and cytidine-rich RNA fragments that occupy TLR7 ligand-binding pockets and trigger a signaling-competent state. Can exert polynucleotide phosphatase activity toward 5'-phosphorylated ssDNA substrates although at a slow rate (PubMed:38537643). Transphosphatidylase that catalyzes the exchange with R to S stereo-inversion of the glycerol moiety between (S,R)-lysophosphatidylglycerol (LPG) and monoacylglycerol (MAG) substrates to yield (S,S)-bis(monoacylglycero)phosphate (BMP) (PubMed:39423811). Can synthesize a variety of (S,S)-BMPs representing the main phospholipid constituent of lysosomal intralumenal vesicle (ILV) membranes that bind acid hydrolases for lipid degradation (PubMed:39423811). Regulates the homeostasis and interorganellar communication of the endolysosomal system with an overall impact on cellular removal of dysfunctional organelles via autophagy as well as proper protein and lipid turnover. May play a role in myotube formation in response to ER stress (By similarity). {ECO:0000250\|UniProtKB:Q8IV08, ECO:0000269\|PubMed:30111894, ECO:0000269\|PubMed:34620855, ECO:0000269\|PubMed:38537643, ECO:0000269\|PubMed:39423811}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.; EC=3.1.16.1; Evidence={ECO:0000269\|PubMed:30111894, ECO:0000269\|PubMed:34620855, ECO:0000269\|PubMed:38537643}; CATALYTIC ACTIVITY: Reaction=a 5'-end 5'-dephospho-ribonucleotidyl-ribonucleotide-RNA + H2O = a ribonucleoside 3'-phosphate + a 5'-end dephospho-ribonucleoside-RNA + H(+); Xref=Rhea:RHEA:81375, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:19670, ChEBI:CHEBI:13197, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138284, ChEBI:CHEBI:231871; Evidence={ECO:0000269\|PubMed:34620855}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:81376; Evidence={ECO:0000305\|PubMed:34620855}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 3'-phosphate-2'-3'-cyclophospho-GMP + H2O = a ribonucleoside 3'-phosphate + 2',3'-cyclophospho-GMP + H(+); Xref=Rhea:RHEA:81319, ChEBI:CHEBI:13197, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:60837, ChEBI:CHEBI:231870; Evidence={ECO:0000250\|UniProtKB:Q8IV08}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:81320; Evidence={ECO:0000250\|UniProtKB:Q8IV08}; CATALYTIC ACTIVITY: Reaction=a 5'-end 5'-dephospho-2'-deoxyribonucleotidyl-2'-deoxyribonucleotide in single-stranded DNA + H2O = a 5'-end dephospho-2'-deoxyribonucleoside in single-stranded DNA + a 2'-deoxyribonucleoside 3'-phosphate + H(+); Xref=Rhea:RHEA:81379, Rhea:RHEA-COMP:19701, Rhea:RHEA-COMP:19702, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131705, ChEBI:CHEBI:136416, ChEBI:CHEBI:231873; Evidence={ECO:0000269\|PubMed:30111894, ECO:0000269\|PubMed:38537643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:81380; Evidence={ECO:0000305\|PubMed:30111894, ECO:0000305\|PubMed:38537643}; CATALYTIC ACTIVITY: Reaction=a 5'-end 5'-phospho-2'-deoxyribonucleotide in single-stranded DNA + H2O = a 5'-end 5'-dephospho-2'-deoxyribonucleotide in single-stranded DNA + phosphate; Xref=Rhea:RHEA:82335, Rhea:RHEA-COMP:19868, Rhea:RHEA-COMP:19869, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:136412, ChEBI:CHEBI:136416; Evidence={ECO:0000269\|PubMed:38537643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:82336; Evidence={ECO:0000305\|PubMed:38537643}; CATALYTIC ACTIVITY: Reaction=a 3-lyso-sn-glycero-1-phospho-(3'-acyl-1'-sn-glycerol) + a 1-acyl-sn-glycerol = a 3-acyl-sn-glycero-1-phospho-(3'-acyl-1'-sn-glycerol) + glycerol; Xref=Rhea:RHEA:82563, ChEBI:CHEBI:17754, ChEBI:CHEBI:64683, ChEBI:CHEBI:77717, ChEBI:CHEBI:232393; Evidence={ECO:0000250\|UniProtKB:Q8IV08}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:82564; Evidence={ECO:0000250\|UniProtKB:Q8IV08}; CATALYTIC ACTIVITY: Reaction=3-lyso-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + 1-(9Z-octadecenoyl)-sn-glycerol = 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + glycerol; Xref=Rhea:RHEA:82567, ChEBI:CHEBI:17754, ChEBI:CHEBI:75757, ChEBI:CHEBI:139150, ChEBI:CHEBI:232394; Evidence={ECO:0000250\|UniProtKB:Q8IV08}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:82568; Evidence={ECO:0000250\|UniProtKB:Q8IV08};
Subellular location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269\|PubMed:21085684}; Single-pass type II membrane protein {ECO:0000305\|PubMed:21085684}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269\|PubMed:21085684}; Single-pass type II membrane protein {ECO:0000305\|PubMed:21085684}. Nucleus {ECO:0000269\|PubMed:22102906}. Early endosome {ECO:0000305\|PubMed:22102906}. Cytoplasmic vesicle, phagosome {ECO:0000269\|PubMed:22102906}. Lysosome {ECO:0000250\|UniProtKB:Q8IV08}. Note=Activation of microglia induces translocation of PLD4 from the nucleus to the phagosomes. {ECO:0000269\|PubMed:22102906}.
Tissues TISSUE SPECIFICITY: Enriched in the white matter of early postnatal brains, as well as in splenic marginal zone cells (PubMed:21085684). Highly expressed in dendritic cells (DCs) and other myeloid cells, with lower expression in B cell (PubMed:30111894). {ECO:0000269\|PubMed:21085684, ECO:0000269\|PubMed:30111894}.
Post-translational modification PTM: Highly N-glycosylated. {ECO:0000269\|PubMed:21085684, ECO:0000269\|PubMed:22102906}.
Target Relevance information above includes information from UniProt accession: Q8BG07
The UniProt Consortium

Data

The purity of Mouse PLD4 is greater than 95% as determined by SEC-HPLC.

Mouse PLD4 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.