For research use only.
| Verified Samples | Verified Samples in WB: A549, HT-29 |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Mouse ANGPTL4 protein expressed by Mammalian |
| Abbre | Angptl4 |
| Synonyms | ARP, Secreted protein Bk, Angiopoietin-like protein, Angiopoietin-related protein, ANGPTL, 425O18, 425O18-1, Angiopoietin-like protein 4, Angiopoietin-related protein 4, ARP4, Fasting-induced adipose factor, Hepatic fibrinogen/angiopoietin-related protein, HFARP, NL2, PGAR, pp1158, Secreted protein Bk89, Farp, Fiaf, Ng27, Angptl4 |
| Swissprot | |
| Calculated MW | 45 kDa |
| Observed MW | 50 kDa The actual band is not consistent with the expectation. Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Secreted, Extracellular space, Extracellular matrix |
| Tissue Specificity | Expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney. |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack, upon receipt, store it immediately at the temperature recommended. |
| background | Angiopoietin-related protein 4 (ANGPTL4) is a secreted protein and contains 1 fibrinogen C-terminal domain. The protein may act as a regulator of angiogenesis and modulate tumorigenesis. It inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 may exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity (By similarity). In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation. |
Other Clones
1 Results
Other Formats
1 Results
Unconjugated
