|Product Name||Anti-Calretinin/CALB2 Antibody|
|Storage & Handling||At -20°C for one year, at 4°C for one month. Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for Calretinin(CALB2) detection. Tested with WB, IHC-P in Human;Mouse;Rat.|
|Cite This Product||Anti-Calretinin/CALB2 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1015)|
|Immunogen||A synthetic peptide corresponding to a sequence at the N-terminus of human Calretinin(4-18aa PQQQPPYLHLAELTA), identical to the related rat sequence.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat
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, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
Images And Assay Conditions
Anti-Calretinin antibody, PA1015, Western blotting
WB: HELA Cell Lysate
Anti-Calretinin antibody, PA1015, IHC(P)
IHC(P): Human Rectal Cancer Tissue
Protein Target Info (Source: Uniprot.org)
|Alternative Names||Calretinin;CR;29 kDa calbindin;CALB2;CAB29;|
|Molecular Weight||31540 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Calretinin is a calcium-binding protein which is abundant in auditory neurons.|
|Background||Calbindin is a calcium-binding protein belonging to the troponin C superfamily. Calretinin is expressed in central and peripheral nervous system and in many normal and pathological tissues. The rat and human calretinin exhibit 98% sequence homology and 91% homology to many other species. Two calcium binding proteins, calbindin and calretinin, have been reported to be expressed in abundance in Purkinje cells and other cell types in the cerebellum.|
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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.,