GAL7 Polyclonal antibody (AN005900L)

For research use only.
Verified Samples | Verified Samples in WB: Mouse skin, Rat skin, A431 |
Dilution | WB 1:1000-1:2000 |
Isotype | IgG |
Host | Rabbit |
Reactivity | Mouse, Rat, Human |
Applications | WB |
Clonality | Polyclonal |
Immunogen | Recombinant Mouse GAL7 protein expressed by E.coli |
Abbre | GAL7 |
Synonyms | GAL7, Gal-7, galectin 7, HKL-14, galactoside-binding, oluble 7, LGALS7A, p53-induced gene 1 protein, PI7, PIG1, TP53I1, Lgals, Lgals7 |
Swissprot | |
Calculated MW | 15 kDa |
Observed MW |
14 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 | Nucleus, Secreted |
Concentration | 1 mg/mL |
Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
Purification Method | Antigen Affinity Purification |
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 | The galectins constitute a large family of carbohydrate-binding proteins with specificity for N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian galectins, which share structural similarities in their carbohydrate recognition domains (CRD), have been identified. The galectins have been classified into the prototype galectins (-1, -2, -5, -7, -10, -11, -13, -14), which contain one CRD and exist either as a monomer or a noncovalent homodimer; the chimera galectins (Galectin-3) containing one CRD linked to a nonlectin domain; and the tandem-repeat galectins (-4, -6, -8, -9, -12) consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified non-classical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell-surface glycoproteins. Mouse Galectin-7 is a prototype monomeric galectin. It is expressed in stratified epithelia and is significantly down-regulated in squamous cell carcinomas. Galectin-7 is a pro-apoptotic protein that is highly induced by the tumor suppressor protein p53. It functions intracellularly upstream of JNK activation to enhance cytochrome c release during apoptosis. Galectin-7 may also be involved in cell-cell and cell-matrix interactions and exogenous galectin has been found to accelerate the re‑epithelialization of wounds. |
Other Clones
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Other Formats
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Unconjugated
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