Recombinant PKC mu Monoclonal Antibody (AN301985L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa,?PC-3, LNCaP |
| Dilution | WB 1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab. |
| Abbre | PKC mu |
| Synonyms | PRKD, CHDED, PKC-MU, PKCM, PKD, PRKCM, PRKD1, PKD1, KPCD1, nPKC D1, nPKC mu, nPKCD1, nPKC-D1, nPKCmu, nPKC-mu, PKC, PKC MU, PKCmu, PKD 1, PRKD 1, Protein kinase C mu, Protein kinase C mu type, Protein kinase D, Protein kinase D1, Serine/threonine protein kinase D1, Serine/threonine-protein kinase D1 |
| Swissprot | |
| Calculated MW | 102 kDa |
| Observed MW |
110 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 | Cell membrane, Golgi apparatus, Cytoplasm |
| 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, Cancer, Metabolism |
| Clone No. | A705 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction.PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters. Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660. Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization. PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity. |
Other Clones
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Unconjugated
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