|Product Name||Anti-Growth Hormone/GH1 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 Somatotropin(GH1) detection. Tested with WB in Mouse.|
|Cite This Product||Anti-Growth Hormone/GH1 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # RP1024)|
|Immunogen||E. coli-derived mouse GH recombinant protein(Position: F27-F216).|
Assay Dilutions Overview
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-mouse Growth Hormone antibody, RP1024, Western blotting
Lane 1: Recombinant Mouse GH Protein 10ng
Lane 2: Recombinant Mouse GH Protein 5ng
Lane 3: Recombinant Mouse GH Protein 2
Protein Target Info (Source: Uniprot.org)
|Alternative Names||Somatotropin;Growth hormone;Gh1;Gh;|
|Molecular Weight||24716 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.|
|Background||Growth Hormone(GH) is mapped to 17q22-q24. Growth hormone(GH) is synthesized by acidophilic or somatotropic cells of the anterior pituitary gland. Human growth hormone has a molecular mass of 22,005 and contains 191 amino acid residues with 2 disulfide bridges. It binds two receptor molecules and thereby induces signal transduction through receptor dimerization. At high concentrations, GH acts as an antagonist because of a large difference in affinities at the respective binding sites.|
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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.,