Recombinant RIP Monoclonal Antibody (AN301086L)

For research use only.
Verified Samples |
Verified Samples in WB: HEK293 Verified Samples in IHC: Rat kidney tissue, Human cervical cancer tissue |
Dilution | IHC 1:200-1000, WB 1:1000-5000 |
Isotype | IgG,κ |
Host | Rabbit |
Reactivity | Human |
Applications | WB, IHC |
Clonality | Monoclonal;Recombinant |
Immunogen | Recombinant Human RIP protein |
Abbre | RIP |
Synonyms | RIPK, RIP, RIP-1, RIP1, RIPK1, Cell death protein RIP, FLJ39204, OTTHUMP00000039163, Receptor (TNFRSF) interacting serine threonine kinase 1, Receptor interacting protein, receptor interacting protein 1, Receptor interacting protein kinase 1, Receptor interacting serine threonine protein kinase 1, Receptor TNFRSF interacting serine threonine kinase 1, Receptor-interacting protein 1, Receptor-interacting serine/threonine-protein kinase 1, Rinp, RIP 1, RIPK 1, Serine threonine protein kinase RIP, Serine/threonine-protein kinase RIP, RIPK1 |
Swissprot | |
Calculated MW | 76 kDa |
Observed MW |
76 kDa
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, Membranous |
Concentration | 0.2 mg/mL |
Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
Purification Method | Protein A |
Research Areas | Cell Biology, Signal Transduction, Cancer |
Clone No. | 6G10 |
Conjugation | Unconjugated |
Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
Shipping | Ice bag |
background | ATP + a protein = ADP + a phosphoprotein.,Promotes apoptosis and activation of NF-kappa-B. Required for TNFRSF1A mediated activation of NF-kappa-B.,PTM:Autophosphorylated on serine and threonine residues.,PTM:Proteolytically cleaved by caspase-8 during TNF-induced apoptosis. Cleavage abolishes NF-kappa-B activation and enhances pro-apototic signaling through the TRADD-FADD interaction.,similarity:Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.,similarity:Contains 1 death domain.,similarity:Contains 1 protein kinase domain.,subunit:Binds to the death domain of TNFRSF6 and TRADD. Is recruited by TRADD to TNFRSF1A in a TNF-dependent process. Binds RIPK3, UBCE7IP1 isoform 3 (ZIN), EGFR, IKBKG, TRAF1, TRAF2 and TRAF3. Interacts with BNLF1. Interacts with SQSTM1 upon TNF-alpha stimulation. May interacts with MAVS/IPS1. |
Other Clones
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Unconjugated
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