Recombinant ApoER2 Monoclonal Antibody (E-AB-81530)
For research use only.
| Verified Samples |
Verified Samples in WB: CHO-K1, C6 |
| Dilution | WB 1:500-1:2000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Rat, Hamster |
| Applications | WB |
| Clonality | Rabbit Monoclonal |
| Immunogen | A synthetic peptide of human ApoER2 |
| Abbre | ApoER2 |
| Synonyms | APOER2, HSZ75190, LRP-8, MCI1 |
| Swissprot | |
| Calculated MW | 106 kDa |
| Observed MW |
106 kDa
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. |
| Concentration | 300 μg/mL |
| Buffer | 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.05% stabilizer and 0.05% protective protein. |
| Purification Method | Affinity Purified |
| Research Areas | Neuroscience, Signal Transduction, Cardiovascular, Metabolism |
| Clone No. | R03-1H8 |
| 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 | Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 . Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells . |
Other Clones
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Unconjugated
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