|Product Name||Anti-SSH3BP1/ABI1 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 Abl interactor 1(ABI1) detection. Tested with WB, IHC-P, ICC in Human;Mouse;Rat.|
|Cite This Product||Anti-SSH3BP1/ABI1 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1001)|
|Immunogen||A synthetic peptide corresponding to a sequence at the C-terminus of human ABI1 (483-494aa WYEGVCNRVTGL), different from the related rat and mouse sequences by one amino acid.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Immunocytochemistry , 0.5-1μg/ml, Human, -
Western blot, 0.1-0.5μg/ml, Human, Rat, Mouse
Images And Assay Conditions
Anti-ABI1 antibody, PA1001, Western blotting
Lane 1: Rat Liver Tissue Lysate
Lane 2: Rat Brain Tissue Lysate
Lane 3: MM231 Cell Lysate
Lane 4: HELA Cell Lysate
Lane 5: SMMC Cell Lysate
Lane 6: JURKAT Cell Lysate
Anti-ABI1 antibody, PA1001, IHC(P)
IHC(P): Rat Brain Tissue
Protein Target Info (Source: Uniprot.org)
|Protein Name||Abl interactor 1|
|Tissue Specificity||Widely expressed, with highest expression in brain. .|
|Alternative Names||Abl interactor 1;Abelson interactor 1;Abi-1;Abl-binding protein 4;AblBP4;Eps8 SH3 domain-binding protein;Eps8-binding protein;Nap1-binding protein;Nap1BP;Spectrin SH3 domain-binding protein 1;e3B1;ABI1;SSH3BP1;|
|Subcellular Localization||Cytoplasm . Nucleus . Cell projection, lamellipodium . Cell projection, filopodium . Cell projection, growth cone . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cytoplasm, cytoskeleton . Localized to protruding lamellipodia and filopodia tips. Also localized to neuronal growth cones and synaptosomes. May shuttle from the postsynaptic densities to the nucleus (By similarity). .|
|Molecular Weight||55081 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons. .|
|Background||ABI1 is a human homolog of mouse Abl-interactor-1(Abi1), mapped on 10p11.2. ABI1 participates in the transduction of signals from Ras to Rac by regulating Rac-specific guanine nucleotide exchange factor(GEF) activities. ABI1 dramatically promoted ABL1-mediated tyrosine phosphorylation of MENA, but not of other substrates. Abi-1 regulates c-Abl-mediated phosphorylation of Mena by interacting with both proteins. ABI1 plays a role in the leukemogenesis by translocating to MLL.|
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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.,