SPARCL1 is expressed in multiple tissues but absent in the liver :
Tissue | Expression Level | Key Isoforms |
---|---|---|
Brain | High | Full-length (130 kDa) and truncated forms |
Kidney | Moderate | Dominant 55 kDa C-terminal fragment |
Heart/Lung | Moderate | Full-length and truncated forms |
Liver | None | N/A |
Truncated forms (e.g., 55 kDa in mouse kidney, 25 kDa in human tumors) correlate with tissue-specific functions and disease states .
Inhibits cell adhesion and spreading on collagen-rich substrates, terminating neuronal migration during development .
Promotes excitatory synapse formation by increasing AMPA/NMDA receptor ratios independently of neurexins/neuroligins .
Production: Expressed in Sf9 Baculovirus cells as a 71.7 kDa His-tagged glycoprotein .
Applications: Used in adhesion assays, synaptic activity studies, and collagen-binding experiments .
SPARCL1 (F3V2I) Mouse mAb: Detects endogenous SPARCL1 at ~140 kDa via Western blot (1:1000 dilution) and immunofluorescence .
Sparcl1, Ecm2, hevin, mast9, Sc1, SPARC-like protein 1, Extracellular matrix protein 2, Matrix glycoprotein Sc1.
IPTSTRFLSD HSNPTTATLV TPEDATVPIA GVEATADIEN HPSDKAEKPS ALNSEEETHE
QSTEQDKTYS FEVDLKDEED GDGDLSVDPT EGTLTLDLQE GTSEPQQKSL PENGDFPATV
STSYVDPNQR ANITKGKESQ EQPVSDSHQQ PNESSKQTQD LKAEESQTQD PDIPNEEEEE
EEDEEEEEEE EPEDIGAPSD NQEEGKEPLE EQPTSKWEGN REQSDDTLEE SSQPTQISKT
EKHQSEQGNQ GQESDSEAEG EDKAAGSKEH IPHTEQQDQE GKAGLEAIGN QKDTDEKAVS
TEPTDAAVVP RSHGGAGDNG GGDDSKHGAG DDYFIPSQEF LEAERMHSLS YYLKYGGGEE
TTTGESENRR EAADNQEAKK AESSPNAEPS DEGNSREHSA GSCTNFQCKR GHICKTDPQG
KPHCVCQDPE TCPPAKILDQ ACGTDNQTYA SSCHLFATKC RLEGTKKGHQ LQLDYFGACK
SIPACTDFEV AQFPLRMRDW LKNILMQLYE PNPKHGGYLN EKQRSKVKKI YLDEKRLLAG
HPIELLLRD FKKNYHMYVY PVHWQFNELD QHPADRILTH SELAPLRASL VPMEHCITRF
FEECDPNKDK HITLKEWGHC FGIKEEDIDE NLLFLEHHHH HH
What experimental models are most appropriate for studying SPARCL1 in murine systems?
CRISPR-Cas9 knockout models: Used to generate endothelial cell (EC)-specific Sparcl1-KO mice, enabling tissue-specific functional studies (e.g., viral pneumonia outcomes) .
Tamoxifen-inducible Cre systems: Allow temporal control of Sparcl1 deletion/overexpression in adult mice .
3D prostasphere assays: Employed to study SPARCL1's anti-invasive effects in prostate cancer using primary murine/human epithelial cells .
How is SPARCL1 expression detected and quantified in mouse tissues?
Western blotting: Validates SPARCL1 protein levels in lung homogenates (e.g., EC Sparcl1-OE mice) .
RNA sequencing (RNA-seq): Profiles macrophage polarization states in Sparcl1-modulated mice post-influenza infection .
Flow cytometry: Quantifies M1/M2-like macrophage subsets (CD206, CD11b, F4/80 markers) in lung/bone marrow-derived macrophages (BMDMs) .
What are the baseline physiological roles of SPARCL1 in mice?
How does SPARCL1 differentially regulate disease outcomes in viral pneumonia vs. metabolic disorders?
How to reconcile contradictory findings on SPARCL1’s role in cancer vs. inflammatory diseases?
Prostate cancer: SPARCL1 loss increases metastasis via RHOC-mediated migration .
Viral pneumonia: SPARCL1 overexpression amplifies inflammation, worsening outcomes .
Resolution: Tissue-specific context and disease stage dictate SPARCL1’s pro- or anti-pathogenic roles. Use conditional knockout/overexpression models to isolate organ-specific effects.
What methodologies resolve SPARCL1’s dual role in macrophage polarization?
How to address species-specific SPARCL1 expression variability in translational studies?
What controls are critical for interpreting SPARCL1 knockout/overexpression phenotypes?
Why does SPARCL1 enhance synaptogenesis in neurons but inhibit adhesion in epithelial cells?
How to validate SPARCL1’s role in macrophage polarization across studies?
SPARCL1 is an anti-adhesive protein widely expressed in tissues such as the brain, heart, lung, muscle, and kidney, but notably absent in the liver . The protein contains three conserved structural domains that are implicated in the regulation of cell adhesion, migration, and proliferation . The recombinant mouse SPARCL1 protein is typically produced in cell lines such as NS0 or HEK293 cells and is often tagged with a polyhistidine tag for purification purposes .
SPARCL1 has garnered interest in cancer research due to its down-regulation in various cancers and its potential role as a tumor suppressor . Its ability to regulate angiogenesis, the formation of new blood vessels, makes it a target for therapeutic research in oncology . Additionally, SPARCL1’s role in inhibiting cell growth has been measured in studies using mink lung epithelial cells, where it demonstrated the ability to inhibit cell growth at specific concentrations .
Recombinant mouse SPARCL1 is produced for research purposes and is available in various formulations, including carrier-free versions that do not contain Bovine Serum Albumin (BSA) . This is particularly useful for applications where the presence of BSA could interfere with experimental outcomes . The protein is typically lyophilized and can be reconstituted in sterile PBS for use in various assays .