|Product Name||Anti-Morg1/WDR83 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for WD repeat domain-containing protein 83(WDR83) detection. Tested with WB, IHC-P in Human;Mouse;Rat.|
|Cite This Product||Anti-Morg1/WDR83 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1053)|
|Contents/Buffer||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.|
|Immunogen||A synthetic peptide corresponding to a sequence at the N-terminus of human Morg1(29-43aa RAVRFNVDGNYCLTC), identical to the related mouse and rat sequences.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, Rat, Mouse, By Heat
Western blot, 0.1-0.5μg/ml, Human, Rat, Mouse
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
Images And Assay Conditions
Anti-Morg1 antibody, PA1053, Western blotting
WB: Rat Brain Tissue Lysate
Anti-Morg1 antibody, PA1053, IHC(P)
IHC(P): Rat Lung Tissue
Protein Target Info (Source: Uniprot.org)
|Protein Name||WD repeat domain-containing protein 83|
|Alternative Names||WD repeat domain-containing protein 83;Mitogen-activated protein kinase organizer 1;MAPK organizer 1;WDR83;MORG1;|
|Subcellular Localization||Cytoplasm . Nucleus . Predominantly cytoplasmic. Partially nuclear. .|
|Molecular Weight||34343 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Molecular scaffold protein for various multimeric protein complexes. Acts as a module in the assembly of a multicomponent scaffold for the ERK pathway, linking ERK responses to specific agonists. At low concentrations it enhances ERK activation, whereas high concentrations lead to the inhibition of ERK activation. Also involved in response to hypoxia by acting as a negative regulator of HIF1A/HIF-1-alpha via its interaction with EGLN3/PHD3. May promote degradation of HIF1A. May act by recruiting signaling complexes to a specific upstream activator (By similarity). May also be involved in pre-mRNA splicing. .|
|Research Areas||Associated Proteins, Cardiovascular, Dna / Rna, Epigenetics And Nuclear Signaling, Hypoxia, Mapk Pathway, Protein Phosphorylation, Rna Processing, Ser / Thr Kinases, Signal Transduction, Splicing
*You can search these to find other products in these research areas.
|Background||MORG1(mitogen-activated protein kinase organizer 1), a member of the WD-40 protein family that was isolated as a binding partner of the extracellular signal-regulated kinase(ERK) pathway scaffold protein MP1. MORG1 specifically associates with several components of the ERK pathway, including MP1, Raf-1, MEK, and ERK, and stabilizes their assembly into an oligomeric complex. MORG1 facilitates ERK activation when cells are stimulated with lysophosphatidic acid, phorbol 12-myristate 13-acetate, or serum, but not in response to epidermal growth factor. Suppression of MORG1 by short interfering RNA leads to a marked reduction in ERK activity when cells are stimulated with serum. MORG1 is a component of a modular scaffold system that participates in the regulation of agonist-specific ERK signaling.|
Other Recommended Resources
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,