Clusterin/Apolipoprotein J/Apo-J/CLU Monoclonal Antibody (AN200024P)
For research use only.
| Verified Samples |
Verified Samples in WB: Hela Verified Samples in FCM: A549 |
| Dilution | WB 1:500-1:1000, FCM 1:100-1:500, ICC/IF 1:100-1:500, |
| Isotype | IgG1 |
| Host | Mouse |
| Reactivity | Human |
| Applications | WB, FCM, ICC/IF |
| Clonality | Monoclonal |
| Immunogen | Recombinant Human Clusterin / Apolipoprotein J / Apo-J Protein |
| Abbre | CLU |
| Synonyms | KUB, AAG, Ku70-binding protein, Sulfated glycoprotein, Complement-associated protein SP, Testosterone-repressed prostate message, NA1/NA, SGP, CLU, AAG4, APO-J, APOJ, CLI, CLU1, CLU2, KUB1, NA1/NA2, SGP-2, SGP2, SP-40, TRPM-2, TRPM2, clusterin, CLUS, Aging-associated gene 4 protein, Apolipoprotein J, Complement cytolysis inhibitor, Complement-associated protein SP-40, Ku70-binding protein 1, Sulfated glycoprotein2, Testosterone-repressed prostate message 2, Complement cytolysis inhibitor a chain, Clusterin alpha chain, Complement cytolysis inhibitor b chain, APOJ CLI, Sulfated glycoprotein 2 |
| Swissprot | |
| Calculated MW | 52 kDa |
| Observed MW |
57 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 | Nucleus, Cytoplasm, Mitochondrion membrane, Peripheral membrane protein, Cytoplasm, Microsome, Endoplasmic reticulum, Mitochondrion |
| Tissue Specificity | Detected in blood plasma, cerebrospinal fluid, milk, seminal plasma and colon mucosa. Detected in brain, testis, ovary, liver and pancreas, lower levels in kidney, heart, spleen and lung. |
| Concentration | 1 mg/mL |
| Buffer | 0.2 μm filtered solution in PBS |
| Purification Method | Protein A |
| Research Areas | Immunology, Cardiovascular, Signal Transduction, Cancer, Metabolism |
| Clone No. | 1F14 |
| Conjugation | Unconjugated |
| Storage | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles. |
| Shipping | Ice bag |
| background | Clusterin, also known as complement-associated protein SP-40, Complement cytolysis inhibitor, Apolipoprotein J, Testosterone-repressed prostate message 2, Aging-associated gene 4 protein, CLU and APOJ, is a secreted protein which belongs to the clusterin family. Clusterin/Apolipoprotein J/Apo-J is an enigmatic glycoprotein with a nearly ubiquitous tissue distribution and an apparent involvement in biological processes ranging from mammary gland involution to neurodegeneration in Alzheimer's disease. Its major form, a heterodimer, is secreted and present in physiological fluids, but truncated forms targeted to the nucleus have also been identified. Clusterin/Apolipoprotein J/Apo-J is a widely distributed glycoprotein with a wide range of biologic properties. A prominent and defining feature of clusterin is its marked induction in such disease states as glomerulonephritis, cystic renal disease, renal tubular injury, neurodegenerative conditions, atherosclerosis, and myocardial infarction. Upregulation of clusterin mRNA and protein levels detected in diverse disease states and in in vitro systems have led to suggestions that it functions in membrane lipid recycling, in apoptotic cell death, and as a stress-induced secreted chaperone protein, amongst others. |
Other Clones
{{antibodyDetailsPage.numTotal}} Results
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
Other Formats
{{formatDetailsPage.numTotal}} Results
Unconjugated
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
-
IF：{{item.impact}}
Journal：{{item.journal}} ({{item.year}})
DOI：{{item.doi}}Reactivity：{{item.species}}
Sample Type：{{item.organization}}
-
Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}
