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200μL $ 399.00
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For research use only.

Verified Samples Verified Samples in WB: 3T3
Verified Samples in IF: Rat spleen
Dilution WB 1:500-1:2000,  IHC 1:100-1:300,  IF 1:200-1:1000
Isotype IgG
Host Rabbit
Reactivity Human,  Mouse,  Monkey
Applications WB,  IHC-p,  IF
Clonality Polyclonal
Immunogen Synthesized peptide derived from human SNAI 1 around the non-phosphorylation site of Ser246.
Abbre SNAI 1
Synonyms Drosophila,  Protein sna,  Protein snail homolog,  Protein snail homolog 1,  SLUGH2,  SNA,  SNAH,  SNAI,  SNAI1,  SNAIL,  Sna protein,  Snail 1 homolog,  Snail 1 zinc finger protein,  Snail family transcriptional repressor 1,  Snail homolog 1 (Drosophila),  dJ710H13.1,  homo,  snai1
Swissprot
Calculated MW 29 kDa
Observed MW 29 kDa

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. Cytoplasm. Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs.
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,  Cardiovascular,  Epigenetics and Nuclear Signaling
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 Drosophila embryonic protein snail is a zinc finger transcriptional repressor which downregulates the expression of ectodermal genes within the mesoderm. The nuclear protein encoded by this gene is structurally similar to the Drosophila snail protein, and is also thought to be critical for mesoderm formation in the developing embryo. At least two variants of a similar processed pseudogene have been found on chromosome 2.
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Unconjugated

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