|Product Name||Anti-SKP2 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 S-phase kinase-associated protein 2(SKP2) detection. Tested with WB, IHC-P in Human;Mouse;Rat.|
|Cite This Product||Anti-SKP2 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1102)|
|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 SKP2(2-20aa HRKHLQEIPDLSSNVATSF), different from the related rat and mouse sequences by three amino acids.|
|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-SKP2 antibody, PA1102, Western blotting
WB: MCF-7 Cell Lysate
Anti-SKP2 antibody, PA1102, IHC(P)
IHC(P): Human Mammary Cancer Tissue
Protein Target Info (Source: Uniprot.org)
|Protein Name||S-phase kinase-associated protein 2|
|Alternative Names||S-phase kinase-associated protein 2;Cyclin-A/CDK2-associated protein p45;F-box protein Skp2;F-box/LRR-repeat protein 1;p45skp2;SKP2;FBXL1;|
|Subcellular Localization||Cytoplasm . Nucleus .|
|Molecular Weight||47761 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration. .|
|Research Areas||Cancer, Cardiogenesis, Cardiovascular, Cell Biology, F Box E3 Ligase, Oncoproteins, Oncoproteins/Suppressors, Proteasome / Ubiquitin, Proteolysis / Ubiquitin, Transcription Factors/Regulators, Ubiquitin E3 Enzymes
*You can search these to find other products in these research areas.
|Background||The F box protein Skp2(S-phase kinase-associated protein 2) is oncogenic, and its frequent amplification and overexpression correlate with the grade of malignancy of certain tumors. Skp2 controls p300-p53 signaling pathways in cancer cells, making it a potential molecular target for cancer therapy. This gene positively regulates the G(1)-S transition by controlling the stability of several G(1) regulators, such as the cell cycle inhibitor p27. This study provides evidence of a role for an F-box protein in oncogenesis and establishes SKP2 as a protooncogene causally involved in the pathogenesis of lymphomas.|
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.,