Recombinant Endoplasmin Monoclonal Antibody (AN300683L)
For research use only.
| Verified Samples | Verified Samples in WB: Hela |
| Dilution | WB 1:2000-1:10000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human Endoplasmin protein |
| Abbre | Endoplasmin |
| Synonyms | HEL, TRA, GRP, HSP90B, HSP90B1, ECGP, GP96, GRP94, HEL-S-125m, HEL35, TRA1, endoplasmin, ECGP, endoplasmin, GP96, GRP94, HEL35, HEL-S-125m, TRA1, 90 kDa, 94 kDa glucose regulated protein, 94 kDa glucose-regulated protein, beta, Endothelial cell (HBMEC) glycoprotein, ENPL, ERp99, Glucose regulated protein 94kDa, gp96 homolog, GRP 94, GRP-94, Heat shock protein, Heat shock protein 90 kDa beta member 1, heat shock protein 90kDa beta (Grp94), Heat shock protein 90kDa beta member 1, member 1, Stress inducible tumor rejection antigen GP96, tumor rejection antigen (gp96) 1, Tumor rejection antigen 1, Tumor rejection antigen gp96, Tumor rejection antigen-1 (gp96) |
| Swissprot | |
| Calculated MW | 93 kDa |
| Observed MW |
100 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 | Endoplasmic reticulum |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Tags & Cell Markers, Signal Transduction, Cancer, Metabolism |
| Clone No. | 6A4 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | This gene encodes a member of a family of adenosine triphosphate(ATP)-metabolizing molecular chaperones with roles in stabilizing and folding other proteins. The encoded protein is localized to melanosomes and the endoplasmic reticulum. Expression of this protein is associated with a variety of pathogenic states, including tumor formation. There is a microRNA gene located within the 5' exon of this gene. There are pseudogenes for this gene on chromosomes 1 and 15. |
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Unconjugated
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