|Product Name||Anti-IL7 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for Interleukin-7(IL7) detection. Tested with WB, ELISA in Human.|
|Cite This Product||Anti-IL7 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # RP1013)|
|Immunogen||E. coli-derived human IL-7 recombinant protein(Position: D26-H177).|
Assay Dilutions Overview
ELISA , 0.1-0.5μg/ml, Human
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
Images And Assay Conditions
Anti-human IL7 antibody, RP1013, Western blotting
Lane 1: Recombinant Human IL-7 Protein 10ng
Lane 2: Recombinant Human IL-7 Protein 5ng
Lane 3: Recombinant Human IL-7 Protein 2
Protein Target Info (Source: Uniprot.org)
|Molecular Weight||20187 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Hematopoietic growth factor capable of stimulating the proliferation of lymphoid progenitors. It is important for proliferation during certain stages of B-cell maturation.|
|Background||IL-7, Interleukin 7, is a protein that in humans is encoded by the IL-7 gene. IL-7 a hematopoietic growth factor secreted by stromal cells in the red marrow and thymus. It is also produced by keratinocytes, dendritic cells, hepatocytes, neurons, and epithelial cells but is not produced by lymphocytes. By the combination of approaches, IL-7 is located on 8q12-q13. IL-7 is critical for early T-cell development and homeostasis of naive and memory CD8-positive T cells. It signals through the IL-7 receptor complex, which consists of the IL7R-alpha chain and the common IL2R-gamma chain is critical for early T-cell development and homeostasis of naive and memory CD8 -positive T cells. It signals through the IL-7 receptor complex, which consists of the IL7R-alpha chain and the common IL2R-gamma chain.|
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,