Data & Images
|Product Name||Anti-Cathepsin G Picoband™ Antibody|
|Description||Rabbit IgG polyclonal antibody for Cathepsin G(CTSG) detection. Tested with WB in Human;Rat.|
|Cite This Product||Anti-Cathepsin G Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9049)|
|Replacement Item||This antibody may replace the following items: sc-33206|sc-33207|sc-6511|sc-6512 from Santa Cruz Biotechnology.|
|Validated Species||Human, Rat|
*Our Boster Guarantee covers the use of this product in the above tested applications.
**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.
|Recommended Detection Systems||Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2017!
|Immunogen||E.coli-derived human Cathepsin G recombinant protein (Position: A76-L255). Human Cathepsin G shares 66% amino acid (aa) sequence identity with mouse Cathepsin G.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
*carrier free antibody available upon request.
|Concentration||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Storage||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.|
|Purification||Immunogen affinity purified.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Protein Name||Cathepsin G|
|Molecular Weight||28837 MW|
|Protein Function||Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe- CH2Cl and phenylmethylsulfonyl fluoride. .|
|Sequence Similarities||Belongs to the peptidase S1 family.|
|Subcellular Localization||Cell surface .|
|Alternative Names||Cathepsin G;CG;22.214.171.124;CTSG;|
|Research Areas|||signal transduction|cytoskeleton / ecm|extracellular matrix|ecm enzymes|other enzymes| cell biology|proteolysis / ubiquitin|proteolytic enzymes|other proteases| kits/ lysates/ other|apoptosis kits|cathepsin assay kits||
Background for Cathepsin G
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-Cathepsin G Picoband™ Antibody by testing all applications on non-spiked tissues and cell lines to ensure that the affinity of the antibody is enough to react to the endogenouse level of the target protein. Read more about our QC panel here.
|Recommended dilution ratios are listed below:|
Western blot, 0.1-0.5μg/ml, Rat, Human|
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-Cathepsin G Picoband™ Antibody Images
Click the images to enlarge.
All lanes: Anti-Cathepsin G(PB9049) at 0.5ug/ml
WB: Rat Thymus Tissue Lysate at 40ug
Predicted bind size: 38KD
Observed bind size: 38KD
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.,