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100μL $ 260.00
50μL $ 160.00
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For research use only.

Verified Samples Verified Samples in WB: Hela, A549, C2C12
Verified Samples in IHC: Human breast cancer
Dilution WB 1:500-1:1000,  IHC 1:20-1:50
Isotype IgG
Host Rabbit
Reactivity Human,  Mouse
Applications WB,  IHC-P
Clonality Rabbit Monoclonal
Immunogen Recombinant protein of human Keap1
Abbre Keap1
Synonyms Cytosolic inhibitor of Nrf2,  INrf 2,  INrf2,  KEAP1,  KIAA0132,  KLHL 19,  KLHL19,  Keap 1,  Kelch like ECH associated protein 1,  Kelch like family member 19,  Kelch like protein 19,  Kelch-like ECH-associated protein 1,  Kelch-like protein 19,  M,  MGC10630,  MGC1114,  MGC20887
Swissprot
Calculated MW 70 kDa
Observed MW 60 /64 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 Cytoplasm. Nucleus. Shuttles between cytoplasm and nucleus.
Concentration 300 μg/mL
Buffer 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.05% stabilizer and 0.05% protective protein.
Purification Method Affinity Purified
Research Areas Cancer,  Epigenetics and Nuclear Signaling
Clone No. R02-1H7
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 KEAP1,also named as INRF2,KIAA0132 and KLHL19,is part of a multiprotein complex that contains the CUL3-ROC1 ubiquitin ligase,which can ubiquitinate the N-terminal domain of NRF2. Two molecules of KEAP1 bind to two distinct sites in the N-terminal region of NRF2,the ETGE and DLG sites,which affect the KEAP1-NRF2 interaction and/or its physiological consequences. KEAP1 retains NFE2L2/NRF2 in the cytosol. It functions as substrate adapter protein for the E3 ubiquitin ligase complex formed by CUL3 and RBX1. It also retains BPTF in the cytosol. This antibody is a mouse monoclonal antibody raised against residues near the C terminus of human KEAP1.
Other Clones

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Unconjugated

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