Recombinant SGK1 Monoclonal Antibody (AN301954L)

For research use only.
Verified Samples | Verified Samples in WB: SK-MEL-28, A375, HeLa |
Dilution | WB 1:1000 |
Isotype | IgG, κ |
Host | Rabbit |
Reactivity | Human, |
Applications | WB |
Clonality | Monoclonal;Recombinant |
Immunogen | Recombinant human SGK1 fragment |
Abbre | SGK1 |
Synonyms | SGK1, SGK, OTTHUMP00000017247, Serine/threonine protein kinase SGK, Serine/threonine protein kinase Sgk1, Serine/threonine-protein kinase Sgk1, Serum and glucocorticoid regulated kinase, Serum/glucocorticoid regulated kinase, Serum/glucocorticoid regulated kinase 1, Serum/glucocorticoid-regulated kinase 1, SGK 1, Sgk1 variant i3 |
Swissprot | |
Calculated MW | 49 kDa |
Observed MW |
45-55 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, Nucleus, Mitochondrion, 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, Stem Cells, Developmental Biology |
Clone No. | A670 |
Conjugation | Unconjugated |
Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
Shipping | Ice bag |
background | Serum and glucocorticoid-inducible kinase (SGK) is a serine/threonine kinase closely related to Akt. SGK is rapidly induced in response to a variety of stimuli, including serum, glucocorticoid, follicle stimulating hormone, osmotic shock, and mineralocorticoids. SGK activation can be accomplished via HGF PI3K-dependent pathways and by integrin-mediated PI3K-independent pathways. Induction and activation of SGK has been implicated in activating the modulation of anti-apoptotic and cell cycle regulation. SGK also plays an important role in activating certain potassium, sodium, and chloride channels, suggesting its involvement in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. SGK is negatively regulated by ubiquitination and proteasome degradation.In addition to its membrane channel and carrier functions, SGK1 also regulates a broad range of targets, such as GSK-3, NEDD4, iNOS, AMPAR, PSD95, Tau, NF-κB, CREB, and FKHR-L1. |
Other Clones
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Other Formats
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Unconjugated
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