TNFRSF21 Polyclonal Antibody (AN006810L)
For research use only.
| Verified Samples | Verified Samples in WB: 293 |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Human TNFRSF21 protein expressed by Mammalian |
| Abbre | TNFRSF21 |
| Synonyms | UNQ, PRO, Death Receptor, Tumor Necrosis Factor Receptor Superfamily Member, TNFRSF, CD358, Death Receptor 6, Tumor Necrosis Factor Receptor Superfamily Member 21, DR6, TNFRSF21, UNQ437, PRO868, DR6, AA959878 Protein, BM 018, BM018, DR 6, DR6 Protein, MGC31965, OTTHUMP00000039915, R74815 Protein, TNFR related death receptor 6, TNFRSF 21, TNFRSF21 protein, TNR21, TR7 Protein, Tumor necrosis factor receptor superfamily member 21 precursor |
| Swissprot | |
| Calculated MW | 72 kDa |
| Observed MW |
70 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 | Cell membrane |
| Tissue Specificity | Detected in fetal spinal cord and in brain neurons, with higher levels in brain from Alzheimer disease patients (at protein level). Highly expressed in heart, brain, placenta, pancreas, lymph node, thymus and prostate. Detected at lower levels in lung, skeletal muscle, kidney, testis, uterus, small intestine, colon, spleen, bone marrow and fetal liver. Very low levels were found in adult liver and peripheral blood leukocytes. |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen 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 | Death Receptor 6 (DR6), also known as TNFRSF21 and CD358, is a type I transmembrane protein in the TNF receptor superfamily. Human DR6 consists of a 308 amino acid (aa) extracellular domain (ECD) with four cysteine‑rich motifs, a 21 aa transmembrane segment, and a 285 aa palmitylated cytoplasmic region that contains one death domain. Within the ECD, human and mouse DR6 share 82% aa sequence identity. DR6 is expressed as an approximately 110 kDa molecule that carries extensive N‑linked and O‑linked glycosylation in its extracellular region. Among hematopoietic cells, DR6 is expressed on monocytes, resting CD4+ T cells, and pro‑, pre‑, and naïve B cells. DR6 knockout mice exhibit a Th2‑biased immune response characterized by exaggerated Th2 and B cell responsiveness in combination with reduced Th1 cell responsiveness and inflammatory leukocyte infiltration. DR6 knockout mice are resistant to induced airway inflammation and experimental autoimmune encephalitis but more susceptible to severe graft versus host disease. DR6 is also expressed on developing neurons where it can bind a shed 35 kDa N‑terminal fragment of APP or a fragment of APLP2. This APP fragment is generated following deprivation of neurotrophic factors, and its binding to DR6 triggers DR6‑mediated axonal pruning. DR6 is constitutively expressed on some prostate cancer cells and can be induced by TNF‑ alpha on others. |
Other Clones
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Unconjugated
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