癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
phospho-FADD (Ser194) Rabbit pAb
phospho-FADD (Ser194) Rabbit pAb
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Application 
| IHC-P, IHC-F, IF |
|---|---|
| Primary Accession | Q13158 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 23279 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated Synthesised phosphopeptide derived from human FADD around the phosphorylation site of Ser194 |
| Epitope Specificity | AM(p-S)PM |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SIMILARITY | Contains 1 death domain. Contains 1 DED (death effector) domain. |
| SUBUNIT | Can self-associate. Interacts with CFLAR, PEA15 and MBD4. When phosphorylated, part of a complex containing HIPK3 and FAS. May interact with MAVS/IPS1. Interacts with MOCV v-CFLAR protein and LRDD. Interacts (via death domain) with FAS (via death domain). Interacts with CASP8. |
| DISEASE | The interaction between the FAS and FADD death domains is crucial for the formation of the death-inducing signaling complex (DISC). Defects in FADD are the cause of infections recurrent associated with encephalopathy hepatic dysfunction and cardiovascular malformations (IEHDCM) [MIM:613759]. A condition with biological features of autoimmune lymphoproliferative syndrome such as high-circulating CD4(-)CD8(-)TCR-alpha-beta(+) T-cell counts, and elevated IL10 and FASL levels. Affected individuals suffer from recurrent, stereotypical episodes of fever, encephalopathy, and mild liver dysfunction sometimes accompanied by generalized seizures. The episodes can be triggered by varicella zoster virus (VZV), measles mumps rubella (MMR) attenuated vaccine, parainfluenza virus, and Epstein-Barr virus (EBV). |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | Predicted to enable several functions, including caspase binding activity; death effector domain binding activity; and tumor necrosis factor receptor superfamily binding activity. Involved in several processes, including hematopoietic or lymphoid organ development; negative regulation of activation-induced cell death of T cells; and positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation. Acts upstream of or within extrinsic apoptotic signaling pathway in absence of ligand; motor neuron apoptotic process; and regulation of programmed cell death. Predicted to be located in several cellular components, including cell body; cytosol; and membrane raft. Predicted to be part of CD95 death-inducing signaling complex and ripoptosome. Predicted to be active in cytoplasm. Is expressed in several structures, including alimentary system; brain; genitourinary system; hemolymphoid system gland; and liver and biliary system. Human ortholog(s) of this gene implicated in leukemia. Orthologous to human FADD (Fas associated via death domain). [provided by Alliance of Genome Resources, Apr 2022] |
| Gene ID | 8772 |
|---|---|
| Other Names | FAS-associated death domain protein, FAS-associating death domain-containing protein, Growth-inhibiting gene 3 protein {ECO:0000303|Ref.3}, Mediator of receptor induced toxicity, FADD {ECO:0000303|PubMed:7538907, ECO:0000312|HGNC:HGNC:3573} |
| Target/Specificity | Expressed in a wide variety of tissues, except for peripheral blood mononuclear leukocytes. |
| Dilution | IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500 |
| Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
| Name | FADD {ECO:0000303|PubMed:7538907, ECO:0000312|HGNC:HGNC:3573} |
|---|---|
| Function | Apoptotic adapter molecule that recruits caspases CASP8 or CASP10 to the activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors (PubMed:16762833, PubMed:19118384, PubMed:20935634, PubMed:23955153, PubMed:24025841, PubMed:7538907, PubMed:9184224). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:16762833, PubMed:19118384, PubMed:20935634, PubMed:7538907, PubMed:9184224). Active CASP8 initiates the subsequent cascade of caspases mediating apoptosis (PubMed:16762833). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (PubMed:21109225, PubMed:24204270). |
| Cellular Location | Cytoplasm. |
| Tissue Location | Expressed in a wide variety of tissues, except for peripheral blood mononuclear leukocytes. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Predicted to enable several functions, including caspase binding activity; death effector domain binding activity; and tumor necrosis factor receptor superfamily binding activity. Involved in several processes, including hematopoietic or lymphoid organ development; negative regulation of activation-induced cell death of T cells; and positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation. Acts upstream of or within extrinsic apoptotic signaling pathway in absence of ligand; motor neuron apoptotic process; and regulation of programmed cell death. Predicted to be located in several cellular components, including cell body; cytosol; and membrane raft. Predicted to be part of CD95 death-inducing signaling complex and ripoptosome. Predicted to be active in cytoplasm. Is expressed in several structures, including alimentary system; brain; genitourinary system; hemolymphoid system gland; and liver and biliary system. Human ortholog(s) of this gene implicated in leukemia. Orthologous to human FADD (Fas associated via death domain). [provided by Alliance of Genome Resources, Apr 2022]
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