ANGPTL4 Antibody - #DF6751
Product: | ANGPTL4 Antibody |
Catalog: | DF6751 |
Description: | Rabbit polyclonal antibody to ANGPTL4 |
Application: | WB IHC |
Reactivity: | Human, Mouse, Rat |
Mol.Wt.: | 45kDa; 45kD(Calculated). |
Uniprot: | Q9BY76 |
RRID: | AB_2838713 |
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Protocols
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# DF6751, RRID:AB_2838713.
Fold/Unfold
Angiopoietin like 4; Angiopoietin related protein 4; Angiopoietin-like protein 4; Angiopoietin-related protein 4; ANGL4_HUMAN; ANGPT L2; ANGPT L4; ANGPTL2; Angptl4; ARP4; Fasting induced adipose factor; FIAF; HARP; Hepatic angiopoietin related protein; Hepatic fibrinogen/angiopoietin related protein; Hepatic fibrinogen/angiopoietin-related protein; HFARP; NL2; Peroxisome proliferator-activated receptor (PPAR) gamma induced angiopoietin related protein; PGAR; pp1158; PPARG angiopoietin related protein; PSEC0166; TGQTL; UNQ171; Weakly similar to angiopoietin 1 [H.sapiens];
Immunogens
A synthesized peptide derived from human ANGPTL4, corresponding to a region within N-terminal amino acids.
Detected in blood plasma (at protein level) (PubMed:29899519). Detected in liver (PubMed:10698685). Detected in white fat tissue and placenta (PubMed:10866690). Expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney.
- Q9BY76 ANGL4_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSGAPTAGAALMLCAATAVLLSAQGGPVQSKSPRFASWDEMNVLAHGLLQLGQGLREHAERTRSQLSALERRLSACGSACQGTEGSTDLPLAPESRVDPEVLHSLQTQLKAQNSRIQQLFHKVAQQQRHLEKQHLRIQHLQSQFGLLDHKHLDHEVAKPARRKRLPEMAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEFWLGLEKVHSITGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTAYSLQLTAPVAGQLGATTVPPSGLSVPFSTWDQDHDLRRDKNCAKSLSGGWWFGTCSHSNLNGQYFRSIPQQRQKLKKGIFWKTWRGRYYPLQATTMLIQPMAAEAAS
PTMs - Q9BY76 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S30 | Phosphorylation | Uniprot | |
R164 | Methylation | Uniprot | |
R180 | Methylation | Uniprot |
Research Backgrounds
Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. May also play a role in regulating glucose homeostasis and insulin sensitivity (Probable). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro). Depending on context, may modulate tumor-related angiogenesis (By similarity).
Mediates inactivation of the lipoprotein lipase LPL, and thereby plays an important role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. Has higher activity in LPL inactivation than the uncleaved protein.
N-glycosylated.
Forms disulfide-linked dimers and tetramers.
Cleaved into a smaller N-terminal chain and a larger chain that contains the fibrinogen C-terminal domain; both cleaved and uncleaved forms are detected in the extracellular space. The cleaved form is not present within the cell.
Secreted. Secreted>Extracellular space>Extracellular matrix.
Note: The unprocessed form interacts with the extracellular matrix (PubMed:17068295, PubMed:21398697). This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4 (Probable).
Detected in blood plasma (at protein level). Detected in liver. Detected in white fat tissue and placenta. Expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney.
Homooligomer; disulfide-linked via Cys residues in the N-terminal part of the protein. The homooligomer undergoes proteolytic processing to release the ANGPTL4 C-terminal chain, which circulates as a monomer. The homooligomer unprocessed form is able to interact with the extracellular matrix.
Research Fields
· Organismal Systems > Endocrine system > PPAR signaling pathway.
· Organismal Systems > Digestive system > Cholesterol metabolism.
References
Application: WB Species: Rat Sample:
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