Recombinant KLK8/Kallikrein 8 Monoclonal Antibody (AN300243P)
For research use only.
| Verified Samples | Verified Samples in WB:HeLa, A431, Jurkat |
| Dilution | WB: 1:1000-1:1000;IHC-P: 1:50-1:100 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB, IHC-P |
| Clonality | Recombinant;Monoclonal |
| Immunogen | Recombinant Human KLK8 / Kallikrein 8 Protein |
| Abbre | KLK8 |
| Synonyms | KLK, UNQ, PRO, Kallikrein, Serine Protease, TADG, PRSS, Serine Protease TADG, hK8, Kallikrein-8, Neuropsin, NP, Ovasin, Serine Protease 19, Serine Protease TADG-14, Tumor-Associated Differentially Expressed Gene 14 Protein, NRPN, PRSS19, TADG14, KLK8, UNQ283, PRO322, Brain serine protease 1, BSP1, HNP, homolog of, HPN, included, Kallikrein 8 (neuropsin/ovasin), Kallikrein related peptidase 8, Kallikrein8, KLK 8, KLK8 protein type 1, KLK8 protein type 2, mouse, neuropsin type 1, Neuropsin type 2, Protease serine 19, PRSS 19, Serine protease kallikrein, Serine protease kallikrein/ovasin/neuropsin, Serine protease TADG 14, Serine protease TADG14, TADG 14, Tumor associated differentially expressed gene 14, Tumor associated differentially expressed gene 14 protein |
| Swissprot | |
| Calculated MW | 28, 33 kDa |
| Observed MW |
36 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. |
| Concentration | 1 mg/mL |
| Buffer | 0.2 μm filtered solution in PBS |
| Purification Method | Protein A |
| Research Areas | Signal Transduction, Cancer, Cell Biology |
| Clone | B161 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen kallikrein subfamily members located in tandem in a gene cluster on chromosome 19. The encoded protein may be involved in proteolytic cascade in the skin and may serve as a biomarker for ovarian cancer. Alternate splicing of this gene results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2013] |
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