|Tested species reactivity||Rat|
|Published species reactivity||Not Applicable|
|Host / Isotype||Chicken / IgY|
|Immunogen||Gamma Immunoglobins Heavy and Light chains|
|Conjugate||Alexa Fluor® 488|
|Storage buffer||PBS, pH 7.5|
|Contains||5mM sodium azide|
|Storage Conditions||4° C, store in dark|
|Cross Adsorption||Against human and rabbit IgG prior to conjugation|
|Antibody Form||Whole Antibody|
|Tested Applications||Dilution *|
|Immunocytochemistry (ICC)||1-10 µg/ml|
|Immunofluorescence (IF)||1-10 µg/mL|
|Immunohistochemistry (IHC)||1-10 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Chicken anti-rat antibodies react with IgG heavy chains and all classes of immunoglobulin light chains from rat. Chicken secondary antibodies have gained popularity because they demonstrate a lower level of nonspecific binding. Chicken antibodies lack a classic “Fc” domain and will not bind to protein A or protein G, nor will they bind to mammalian IgG Fc receptors.
Anti-Rat secondary antibodies are affinity-purified antibodies with well-characterized specificity for rat immunoglobulins and are useful in the detection, sorting or purification of its specified target. Secondary antibodies offer increased versatility enabling users to use many detection systems (e.g. HRP, AP, fluorescence). They can also provide greater sensitivity through signal amplification as multiple secondary antibodies can bind to a single primary antibody. Most commonly, secondary antibodies are generated by immunizing the host animal with a pooled population of immunoglobulins from the target species and can be further purified and modified (i.e. immunoaffinity chromatography, antibody fragmentation, label conjugation, etc.) to generate highly specific reagents.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Combination Growth Factor Therapy via Electrostatically Assembled Wound Dressings Improves Diabetic Ulcer Healing In Vivo.
A-21470 was used in immunohistochemistry to calculate an improvement in diabetic ulcer healing in vivo by combination growth factor therapy via electrostatically assembled wound dressings
|Almquist BD,Castleberry SA,Sun JB,Lu AY,Hammond PT||Advanced healthcare materials (null:null)||2015|
|Not Applicable||Not Cited||Uncovering the role of APC-Cdh1 in generating the dynamics of S-phase onset.||Yuan X,Srividhya J,De Luca T,Lee JH,Pomerening JR||Molecular biology of the cell (25:441)||2014|
|Not Applicable||Not Cited||Physiologically aged red blood cells undergo erythrophagocytosis in vivo but not in vitro.||Gottlieb Y,Topaz O,Cohen LA,Yakov LD,Haber T,Morgenstern A,Weiss A,Chait Berman K,Fibach E,Meyron-Holtz EG||Haematologica (97:994)||2012|
|Not Applicable||Not Cited||Thrombospondin 1--a key astrocyte-derived neurogenic factor.||Lu Z,Kipnis J||FASEB journal : official publication of the Federation of American Societies for Experimental Biology (24:1925)||2010|
|Not Applicable||Not Cited||Vascular endothelial growth factor and semaphorin induce neuropilin-1 endocytosis via separate pathways.||Salikhova A,Wang L,Lanahan AA,Liu M,Simons M,Leenders WP,Mukhopadhyay D,Horowitz A||Circulation research (103:e71)||2008|
|Not Applicable||Not Cited||A conserved proliferating cell nuclear antigen-interacting protein sequence in Chk1 is required for checkpoint function.||Scorah J,Dong MQ,Yates JR,Scott M,Gillespie D,McGowan CH||The Journal of biological chemistry (283:17250)||2008|
|Not Applicable||Not Cited||Real-time in vivo imaging of platelets, tissue factor and fibrin during arterial thrombus formation in the mouse.||Falati S,Gross P,Merrill-Skoloff G,Furie BC,Furie B||Nature medicine (8:1175)||2002|