Recombinant ELNE Monoclonal Antibody (AN301296L)
For research use only.
| Verified Samples | Verified Samples in WB: THP-1 |
| Dilution | WB 1:2000-1:10000, |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human ELNE protein |
| Abbre | ELNE |
| Synonyms | SCN, ELA, Elastase, ELANE, ELA2, GE, HLE, HNE, NE, PMN-E, SCN1, Elastase-2, Medullasin, Neutrophil elastase, Bone marrow serine protease, Human leukocyte elastase, PMN elastase, Elastase 2, Elastase 2 neutrophil, Elastase neutrophil expressed, ELNE, Granulocyte derived elastase, Leukocyte elastase, Neutrophil expressed, PMN E, Polymorphonuclear elastase |
| Swissprot | |
| Calculated MW | 29 kDa |
| Observed MW |
30 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 | Cytoplasmic vesicle, phagosome, Localized in phagolysosomes following ingestion of E.coli by neutrophils. |
| Tissue Specificity | Bone marrow cells, Neutrophil. |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Immunology, Microbiology, Signal Transduction, Cancer, Kits, Lysates, Other |
| Clone No. | 5C7 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode structurally similar proteins. The encoded preproprotein is proteolytically processed to generate the active protease. Following activation, this protease hydrolyzes proteins within specialized neutrophil lysosomes, called azurophil granules, as well as proteins of the extracellular matrix. The enzyme may play a role in degenerative and inflammatory diseases through proteolysis of collagen-IV and elastin. This protein also degrades the outer membrane protein A (OmpA) of E. coli as well as the virulence factors of such bacteria as Shigella, Salmonella and Yersinia. Mutations in this gene are associated with cyclic neutropenia and severe congenital neutropenia (SCN). This gene is present in a gene cluster on chromosome 19. |
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Unconjugated
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