Adult rat cerebellum floating section was stained with CPCA-Pvalb, polyclonal antibody (1:2,500) to parvalbumin in green. Parvalbumin is prominently expressed in the dendrites and perikarya of Purkinje cells and the molecular layer interneurons. Blue is a DNA stain.
|Western blot analysis of CPCA-Pvalb. Blot of mouse skeletal muscle lysate (lane1) and His-tagged recombinant proteins: parvalbumin (lane 2), calretinin (lane 3) and calbindin (lane 4) was probed with CPCA-Pvalb at 1:2,500. In skeletal muscle lysates, this antibody recognizes a band at 12 kDa which represents parvalbumin and it reacts only with parvalbumin and not the other calcium-binding proteins. This antibody does not recognize parvabumin in rat or mouse brain lysates on western blots.
||Chicken Polyclonal to Parvalbumin
||Full-length recombinant human protein
||Antibody is supplied as an IgY prep
||Human, rat, mouse
||Western blot, ICC/IF, IHC
|Suggestions for use
||Western blots: 1:1,000-1:5,000
ICC/IF or IHC: 1:1,000-1:5,000
Parvalbumin is a cytoplasmic Ca2+ binding proteins with low molecular weight (9-11kDa). It belongs to subclass of these containing the “EF hand” Ca2+ binding motif and is the first protein characterized in this subclass (1). Parvalbumin is expressed in fast-contracting muscles, where its levels are highest, as well as in the brain and some endocrine tissues. In brain, it is particularly concentrated in Purkinje cells and interneurons in the molecular lay, but is also found in many GABAergic interneurons in the cortex. These GABAergic interneurons in most cases express only one of three Ca2+ binding proteins, namely parvalbumin calretinin, or calbindin. As a result, these important inhibitory interneurons can be identified and subclassified based on their content of these three proteins and antibodies to these three proteins are useful for identifying specific neuronal cell types (2). Each type of neuron as defined in this fashion has particular electrophysiological and functional properties. For example, calbindin positive interneurons are not fast-spiking as are parvalbumin expressing interneurons.
Parvalbumin contains 3 EF-hand domains, domain AB, CD and EF. The N-terminal EF-hand of parvalbumin does not bind Ca2+. The functional calcium-binding loops occur between helices C and D and between helices E and F. The function of parvalbumin appears to be primarily buffering the Ca2+ level in cells and affecting intracellular calcium signal. Absence of parvalbumin and calbindin disrupts the regulation of Purkinje cell firing rate and rhythmicity in vivo and parvalbumin dysfunction in cells critically contributes to abnormalities in oscillatory rhythms and network (3,4). The HGNC name for this protein is PVALB.
1: Kretsinger RH, Nockolds CE. Carp Muscle Calcium-binding Protein: II. Structure determination and general description. J. Biol. Chem. 248:3313-3326 (1973).
2: Andressen C, Bliimcke I, Celio MR. Calcium-binding proteins: selective markers of nerve cells. Cell Tissue Res 271:181-208 (1993).
3: Bearzatto B, Schwaller B, Dumont M, De Saedeleer C, Dan B, Barski JJ, Schiffmann SN, Cheron G. Mono- and dual-frequency fast cerebellar oscillation in mice lacking parvalbumin and/or calbindin D-28k. Eur J Neurosci.22(4):861-70 (2005)
4: Schwaller B, Meyer M, Schiffmann S. ‘New’ functions for ‘old’ proteins: The role of the calcium binding proteins calbindin D-28k, calretinin and parvalbumin, in cerebellar physiology. Studies with knockout mice. The Cerebellum 1:241–258 (2002).
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