C0603
Anti-Calpain LP-82/LP-85 (Lens-Specific Calpain) (Domain III), Large Subunit antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
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About This Item
MDL number:
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous glycerol solution
species reactivity
rat
concentration
~1 mg/mL
technique(s)
western blot: 1:1,000
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
rat ... Capn3(29155)
General description
Lens-specific LP82 and LP85 proteins are localized in the eye tissues of rodents. Muscle-preferred p94 calpain gene encodes for the splice variants, LP82 and LP85. These two proteins are members of the alternative exon 1 (AX1) subclass of calpains.
Specificity
The antibody reacts with latent and active LP-82/LP-85 calpain. By immunoblotting against the reduced protein, the antibody reacts with bands at 85 kDa, 82 kDa, 62 kDa and 60 kDa and a series of further cleaved active forms. It also reacts with non-reduced calpain LP-82/LP-85. The antibody does not cross-react with other calpain family members (μ-calpain, m-calpain, calpain-94, ncl-2, ncl-3, etc.).
Immunogen
synthetic peptide corresponding to the C-terminal of the domain-III in the large subunit of rat LP-82 calpain (lens-specific calpain).
Application
Anti-Calpain LP-82/LP-85 (Lens-Specific Calpain) (Domain III), Large Subunit antibody produced in rabbit has been used in western blotting.
Biochem/physiol Actions
LP82 may regulate calpain activities. It may also play a role in hydrolyzing crystallins during lens cataract formation. LP82 and LP85 along with m-calpain might mediate proteolysis during the typical lens development and maturation or the course of cataract formation in young rodents.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 50% glycerol and 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Susmita Barman et al.
Biological trace element research, 187(1), 212-223 (2018-05-15)
Non-enzymatic glycation of lens proteins and elevated polyol pathway in the eye lens have been the characteristic features of a diabetic condition. We have previously reported the benefits of zinc supplementation in reducing hyperglycemia and associated metabolic abnormalities and oxidative
H Ma et al.
Current eye research, 20(3), 183-189 (2000-03-01)
To clone and sequence the cDNA for Lp85 calpain from young rat lens, and to test for Lp85 protein expression and proteolytic activity. RT-PCR and molecular cloning were performed on total RNA from 12 day-old rats. Lp85 protein expression was
M Shih et al.
Experimental eye research, 82(1), 146-152 (2005-08-02)
Lens-specific Lp82 and ubiquitous m-calpain are neutral, calcium-activated, cysteine proteases. Both calpains are activated during rodent lens maturation and cataract formation. Lp85 calpain (Lens protein with MW=85 kDa) is a slightly larger splice variant of Lp82. Lp85 contains a 28
Chiho Fukiage et al.
The Journal of biological chemistry, 277(23), 20678-20685 (2002-03-21)
Eye tissues contain splice variants of muscle-preferred p94 (calpain 3), such as lens-specific Lp82 and Lp85, retina-specific Rt88, and cornea-specific Cn94. The purpose of the present experiment was to analyze the activation and regulation of the best characterized p94 splice
Magdalena Derbis et al.
Frontiers in genetics, 9, 216-216 (2018-07-05)
Fragile X-associated tremor/ataxia syndrome (FXTAS) is a late-onset neurodegenerative disorder caused by expanded CGG (CGGexp) trinucleotides in the 5'UTR of the FMR1 gene encoding fragile X mental retardation protein (FMRP). The patients, with the number of the repeats ranging from
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