Phospho-ITGB1 (Thr788) Polyclonal Antibody (E-AB-20904)
For research use only.
| Verified Samples |
Verified Samples in WB: Hela |
| Dilution | WB 1:500-1:2000, IHC 1:100-1:300 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC-p |
| Clonality | Polyclonal |
| Immunogen | Synthesized peptide derived from human Integrin β1 around the phosphorylation site of Thr788 |
| Synonyms | CD29, FNRB, Fibronectin receptor subunit beta, GP IIa, GPIIA, Glycoprotein IIa, ITB1, ITGB, Integrin, Integrin beta-1, Integrin subunit beta 1, MSK12), antigen CD29 includes MDF2, beta 1 (fibronectin receptor, beta polypeptide, beta1 integrin, integrin VLA-4 beta subunit |
| Swissprot | |
| Calculated MW | 88 kDa |
| Observed MW |
135 kDa
The actual band is not consistent with the expectation.
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 | Cell membrane, sarcolemma. Cell junction. In cardiac muscle, isoform 5 is found in costameres and intercalated disks and Cell membrane. Cell projection, invadopodium membrane. Cell projection, ruffle membrane. Recycling endosome. Melanosome. Cleavage furrow. Cell projection, lamellipodium. Cell projection, ruffle. Cell junction, focal adhesion. Cell surface. Isoform 2 does not localize to focal adhesions. Highly enriched in stage I melanosomes. Located on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase and metaphase, localizes diffusely at the membrane and in a few intracellular vesicles. In early telophase, detected mainly on the matrix-facing side of the cells. By mid-telophase, concentrated to the ingressing cleavage furrow, mainly to the basal side of the furrow. In late telophase, concentrated to the extending protrusions formed at the opposite ends of the spreading daughter cells, in vesicles at the base of the lamellipodia formed by the separating daughter cells. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions sites to fibrillar adhesions in a ITGB1BP1-dependent manner. Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. |
| Tissue Specificity | Isoform 1 is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform 4, rather than isoform 3, is selectively expressed in peripheral T-cells. Isoform 3 is expressed in non-proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle). |
| Concentration | 1 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol. |
| Purification Method | Affinity purification |
| Research Areas | Cancer, Developmental Biology, Microbiology, Neuroscience, Signal Transduction, Stem Cells |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
| background | Integrin beta-1 (ITGB1), also named as CD29, is a 130 kDa single chain type I glycoprotein that is expressed in a heterodimeric complex with one of six distinct α subunits, comprising the very late activation antigen (VLA) subfamily of adhesion receptors. It is one of the essential surface molecules expressed on human MSC from bone marrow and other sources. The β1 subunit is also broadly expressed on lymphocytes and monocytes, weakly expressed on granulocytes, and not expressed on erythrocytes. These receptors are involved in a variety of cell-cell and cell-matrix interactions. |
Other Clones
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