Recombinant ASGR1 Monoclonal Antibody (AN301439L)
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For research use only.
| Verified Samples |
Verified Samples in FCM: HepG2 Verified Samples in IP: HepG2 cells extracts Verified Samples in WB: HepG2, Human liver Verified Samples in IHC: Human liver Verified Samples in IF: HepG2 |
| Dilution | WB 1:500-1:1000, IHC 1:50-1:100, IF 1:50, FCM 1:50-1:100, IP 1:50-1:100 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | FCM, IP, WB, IHC, IF |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human ASGR1 fragment |
| Abbre | ASGR1 |
| Synonyms | ASGR, C type lectin domain family 4 member H, CLEC4H, ASGP-R, ASGR1, ASGPR, ASGPR1, CLEC4H1, HL-1, ASGPR 1, ASGP-R 1, Asialoglycoprotein receptor 1, C type lectin domain family 4 member H1, C-type lectin domain family 4 member H1, Hepatic lectin H1 |
| Swissprot | |
| Calculated MW | 33 kDa |
| Observed MW |
40-50 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 | Membrane |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Signal Transduction, Tags & Cell Markers |
| Clone No. | A134 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.Calcium is required for ligand binding. |
Other Clones
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Other Formats
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Unconjugated
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