Data & Images
|Product Name||Anti-CCL1/I 309 Antibody|
|Description||Rabbit IgG polyclonal antibody for C-C motif chemokine 1(CCL1) detection. Tested with WB, ELISA in Human.|
|Cite This Product||Anti-CCL1/I 309 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9028)|
|Replacement Item||This antibody may replace the following items: sc-1412 from Santa Cruz Biotechnology.|
*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 I-309 recombinant protein (Position: K24-K96). Human I-309 shares 38% amino acid (aa) sequence identity with mouse I-309.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. Carrier free (No BSA) form available in stock. If you want this antibody carrier free please specify "Carrier Free" or "No BSA" in your order note.|
|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||C-C motif chemokine 1|
|Molecular Weight||154793 MW|
|Protein Function||Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K- driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R.|
|Tissue Specificity||Found as a hybrid receptor with INSR in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts, spleen and placenta (at protein level). Expressed in a variety of tissues. Overexpressed in tumors, including melanomas, cancers of the colon, pancreas prostate and kidney. .|
|Sequence Similarities||Belongs to the intercrine beta (chemokine CC) family.|
|Subcellular Localization||Cell membrane ; Single-pass type I membrane protein .|
|Alternative Names||Insulin-like growth factor 1 receptor;184.108.40.206;Insulin-like growth factor I receptor;IGF-I receptor;CD221;Insulin-like growth factor 1 receptor alpha chain;Insulin-like growth factor 1 receptor beta chain;IGF1R;|
|Research Areas|||immunology|innate immunity|chemokines|beta chemokines (cc)| kits/ lysates/ other|elisa kits|cytokines and cytokine receptors elisa kits||
Background for C-C motif chemokine 1
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-CCL1/I 309 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, Human, -|
ELISA , 0.1-0.5μg/ml, Human
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-CCL1/I 309 Antibody Images
Click the images to enlarge.
All lanes: Anti-I-309(PB9028) at 0.5ug/ml
Lane 1: U87 Whole Cell Lysate at 40ug
Lane 2: MCF-7 Whole Cell Lysate at 40ug
Lane 3: COLO320 Whole Cell Lysate at 40ug
Predicted bind size: 11KD
Observed bind size: 11KD
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.,