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UBQLN4 Polyclonal Antibody (E-AB-91326)

  • +3
All Size Price Qty
200μL $ 530.00
120μL $ 320.00
60μL $ 200.00
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For research use only.

Verified Samples Verified Samples in WB: various cell lines
Verified Samples in IHC: Human colon carcinoma, Human placenta, Mouse lung, Rat brain
Verified Samples in IF: PC-12
Dilution WB 1:500-1:2000,  IHC 1:50-1:200,  IF 1:50-1:200
Clonality Polyclonal
Immunogen Recombinant fusion protein of human UBQLN4
Synonyms A1U,  A1Up,  C1orf6,  CIP75,  UBIN,  UBQLN4
Swissprot
Calculated MW 24 kDa/63 kDa
Observed MW 75 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, Cytoplasmic vesicle, Endoplasmic reticulum, Nucleus, autophagosome, perinuclear region.
Concentration 1 mg/mL
Buffer PBS with 0.05% proclin300,50% glycerol,pH7.3.
Purification Method Affinity purification
Research Areas Cell Biology
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 Regulator of protein degradation that mediates the proteasomal targeting of misfolded, mislocalized or accumulated proteins. Acts by binding polyubiquitin chains of target proteins via its UBA domain and by interacting with subunits of the proteasome via its ubiquitin-like domain. Key regulator of DNA repair that represses homologous recombination repair: in response to DNA damage, recruited to sites of DNA damage following phosphorylation by ATM and acts by binding and removing ubiquitinated MRE11 from damaged chromatin, leading to MRE11 degradation by the proteasome. MRE11 degradation prevents homologous recombination repair, redirecting double-strand break repair toward non-homologous end joining (NHEJ. Specifically recognizes and binds mislocalized transmembrane-containing proteins and targets them to proteasomal degradation. Collaborates with DESI1/POST in the export of ubiquitinated proteins from the nucleus to the cytoplasm. Also plays a role in the regulation of the proteasomal degradation of non-ubiquitinated GJA1 (By similarity. Acts as an adapter protein that recruits UBQLN1 to the autophagy machinery. Mediates the association of UBQLN1 with autophagosomes and the autophagy-related protein LC3 (MAP1LC3A/B/C and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion.
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Unconjugated

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