Product Name: Eotaxin Antibody [1.3_17H09-02C06]
Species Reactivity: Human
Tested Applications: ELISA, WB
Applications: ELISA:In a sandwich ELISA (assuming 100 μL/well), a concentration of 1.0-2.0 μg/mL of this antibody will detect at least 800 pg/mL of recombinant human Eotaxin when used with our biotinylated antigen affinity purified anti-human Eotaxin as the detection antibody at a concentration of approximately 0.5-1.0 μg/mL. Western Blot:To detect hEotaxin by Western Blot analysis this antibody can be used at a concentration of 0.25-0.50 μg/mL. Used in conjunction with compatible secondary reagents the detection limit for recombinant hEotaxin is 0.5-1.0 ng/lane, under reducing or non-reducing conditions.
User Note: Centrifuge vial prior to opening.
Predicted Molecular Weight:
Immunogen: Eotaxin antibody is produced in BALB/c mice using highly pure (>98%) recombinant human Eotaxin as the immunizing antigen.
Host Species: Mouse
Purification: This IgG1K antibody was purified from cell culture by Protein A affinity chromatography.
Physical State: Lyophilized
CAS NO.: 405554-55-4
Product: SB-590885
Buffer:
Concentration:
Storage Conditions: Eotaxin lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20˚C. Reconstitute in sterile water to a concentration of 0.1 – 1.0 mg/mL. The antibody is stable for at least six weeks at 2-4˚C when reconstituted.
Clonality: Monoclonal
Conjugate: Unconjugated
Alternate Names: SCYA11, Eotaxin, C-C motif chemokine 11SCYA11
Accession NO.: P51671
Protein Ino: 1706661
Official Symbol: CCL11
Geneid: 6356
Background: Eotaxin is a 74 amino acid, eosinophil chemotactic CC chemokine originally found in bronchoalveolar lavage fluid from allergic inflammatory subjects. It is involved in regulating the recruitment and activation of inflammatory leukocytes, particularly eosinophils. Eotaxin binds and activates the CCR3 chemokine receptor, and may play a fundamental role in the development of allergic responses.
PubMed ID:http://aac.asm.org/content/39/11/2535.abstract
