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RPS27A Polyclonal Antibody

Cat:E-AB-60562
Manual MSDS
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Price: $ 530

Price: $ 320

Price: $ 200

Size:
200μL 120μL 60μL
Quantity:
  • Host: Rabbit
  • Reactivity: Human;Mouse;Rat
  • Applications: WB;IHC;IF
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For research use only. Order now, ship in 3 days

Product Details
Verified Samples Verified Samples in WB:Jurkat,NIH/3T3,Mouse kidney,Mouse liver,Rat liver
Verified Samples in IHC:Rat kidney,Human placenta,Mouse brain
Verified Samples in IF:U2OS
Dilution

WB 1:500-1:2000, IHC 1:50-1:200, IF 1:50-1:200

Western Blot Operation Guide
Clonality Polyclonal
Immunogen Recombinant fusion protein of human RPS27A (NP_001170884.1).
Abbre RPS27A
Synonyms RPS27A;CEP80;HEL112;S27A;UBA80;UBC;UBCEP1;UBCEP80
Swissprot
Calculated MW 17kDa
Observed MW 14kDa
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 Cytosolic small ribosomal subunit,Endoplasmic reticulum,endoplasmic reticulum membrane,endoplasmic reticulum quality control compartment,Endosome membrane,Extracellular region or secreted,extracellular exosome,extracellular space,Mitochondrion,mitochondrial outer membrane,Nucleus,nucleolus,nucleoplasm,nucleus,Plasma Membrane,Other locations:cytoplasm,endocytic vesicle membrane,host cell,membrane,myelin sheath,small ribosomal subunit,vesicle
Concentration 1mg/mL
Buffer PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Purification Method Affinity purification
Research Areas Cell Biology; Epigenetics and Nuclear Signaling
Conjugation Unconjugated
Storage Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping Ice bag
background Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.