E. coli biotin ligase
(BirA) is highly specific in covalently attaching biotin to the 15
amino
acid AviTag peptide. This recombinant protein was biotinylated in
vivo
by AviTag-BirA technology, which method is BriA catalyzes amide
linkage
between the biotin and the specific lysine of the AviTag.
The tag type will
be
determined during production process. If you have specified tag
type, please tell us and we will develop the specified tag
preferentially.
產品提供形式:
Lyophilized powder
Note: We will
preferentially ship the format that we have in stock, however,
if you have any special requirement for the format, please
remark your requirement when placing the order, we will prepare
according to your demand.
復溶:
We recommend that this vial be briefly centrifuged
prior
to opening to bring the contents to the bottom. Please reconstitute
protein in deionized sterile water to a concentration of 0.1-1.0
mg/mL.We recommend to add 5-50% of glycerol (final concentration)
and
aliquot for long-term storage at -20℃/-80℃. Our default final
concentration of glycerol is 50%. Customers could use it as
reference.
儲存條件:
Store at -20°C/-80°C upon receipt, aliquoting is
necessary for
mutiple use. Avoid repeated freeze-thaw cycles.
保質期:
The shelf life is related to many factors, storage
state,
buffer ingredients, storage temperature and the stability of the
protein
itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C.
The
shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期:
Delivery time may
differ from different purchasing way or location, please kindly
consult your local distributors for specific delivery time.
Note: All of our
proteins are default shipped with normal blue ice packs, if you
request to ship with dry ice, please communicate with us in
advance
and extra fees will be charged.
注意事項:
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-409'. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53.
基因功能參考文獻:
We conclude that integrative variants, haplotypes and diplotypes of the CAPN3 rs4344713 and FRMD5 rs524908, as well as DBP and BMI are associated with serum lipid variables in the Jing and Han populations. PMID: 28332615
This study demonstrates that a cluster of patients with Limb-Girdle Muscular Dystrophy Type 2A in a small Mexican village arises from a novel CAPN3 founder mutation. PMID: 28103310
Heterozygosity for c.643_663del21 in CAPN3 results in a myopathy resembling the recessive form. PMID: 27259757
Unrelated families with limb girdle muscular dystrophy shared common haplotypes with homozygote patterns in two families, and a compound heterozygote pattern in the third family. PMID: 27262448
Here, for the first time, we report a new variant in the CAPN3 gene that can be considered as a robust genetics factor causing limb-girdle muscular dystrophy type 2A disease. PMID: 27861222
Genetic analysis of CAPN3 gene by whole exome sequencing revealed five causative variants which had not been reported in the Iranian population before including a novel 6 bp deletion (c.795_800delCATTGA) and four previously reported mutations (c.1939G > T, c.2243G > A, c.2257delGinsAA, and c.2380 + 2T > G) PMID: 27020652
The allele frequency of CAPN3 gene mutation in limb-girdle muscular dystrophy patients was different in patients from Latvia and Lithuania. PMID: 27142102
Studies indicate that gene mutations causing muscle-specific calcium-activated neutral protease 3 protein (CAPN3) defects are responsible for limb-girdle muscular dystrophy type 2A (LGMD2A). PMID: 26363099
We analyzed 76 families affected with LGMD and identified 62 probands with mutations in the CANP3 gene. C.550delA was the most common mutation identified, being found in 78% of the LGMD2A families PMID: 26484845
We identified four novel CAPN3 mutations and demonstrated clinical and pathological heterogeneity in Korean patients with calpainopathy. PMID: 26632398
Cleavage of C-terminal titin by CAPN3 is associated with limb-girdle muscular dystrophy 2A and tibial muscular dystrophy. PMID: 25877298
Calpain-3 over-expression induces p53 activation and redox imbalance in melanoma A375 cells. PMID: 25658320
Phosphorylated CAPN3 is involved in the pathology of limb-girdle muscular dystrophy type 2A through defects in myofibril integrity and/or signaling pathways. PMID: 25252031
results provide evidence that WT CAPN3 can be formed by the iMOC of two different complementary CAPN3 mutants PMID: 25512505
In LGMD2A muscles the activation of the atrophy programme appeared to depend mainly upon induction of the ubiquitin-proteasome system PMID: 23414389
a heterozygous deletion of the entire CAPN3 gene was found in a patients with Limb-girdle muscular dystrophy type 2A PMID: 24715573
The results indicate that PDGF-C upregulation and calpain-3 downregulation are involved in the aggressiveness of malignant melanoma and suggest that modulators of these proteins PMID: 24126726
Suppression of transgenic CAPN3 expression in cardiac tissue prevents cardiac toxicity in a model of limb-girdle muscular dystrophy. PMID: 23908349
Authors found that PLEIAD also interacts with CTBP1 (C-terminal binding protein 1), a transcriptional co-regulator, and CTBP1 is proteolyzed in COS7 cells expressing CAPN3. PMID: 23707407
Lobulated fibers were often encountered in the muscle biopsies of LGMD2A patients. Such fibers were more frequent in patients with 550delA mutation PMID: 23821418
The findings further confirm mutations in CAPN3 as a genetic cause of eosinophilic myositis and highlight eosinophilic infiltration as an early component (or event) of primary calpainopathy. PMID: 21204801
Researchers identified 2 founder mutations in CAPN3, a missense (c.2338G>C; p.D780H) and a splice-site (c.2099-1G>T) mutation, on 2 different haplotype backgrounds in unrelated limb-girdle muscular dystrophy in the Indian Agarwal community. PMID: 23666804
An intronic mutation in CAPN3 causes severe Limb girdle muscular dystrophy 2A in a large inbred family belonging to a genetic isolate in the Italian Alps. PMID: 22486197
All 18 mutations of Chinese LGMD2A patients are distributed along the entire CAPN3 gene; 11 of the mutations are novel, including 4 missense mutations, 5 deletions, and 2 splicing mutations. PMID: 22926650
Alterations in CAPN3 and nuclear factor-kappaB signaling contribute to muscle mass loss in congenital muscular dystrophy. PMID: 22975586
Evidence from patients with limb girdle muscular dystrophies suggests that calpain 3 is needed for the regenerative process. PMID: 22443334
This is the first report on a potential pathogenic CAPN3 gene mutation resulting from an Alu insertion. PMID: 22158424
In resting human skeletal muscle, the majority (87%) of calpain-3 was present in myofibrillar fractions. PMID: 21836041
In our series of patients, six out of the 13 patients (P9-P14) carried mutations in genes not related to facioscapulohumeral muscular dystrophy, that is, CAPN3 and VCP PMID: 21984748
A homozygous transversion mutation in the CAPN3 gene confirms limb-girdle muscular dystrophy type 2A. PMID: 21386772
The benign phenotype observed in association with combined pG222R and pR748Q mutations suggests that limb-girdle muscular dystrophy type 2A may result from a compensatory effect of compound heterozygosity rather than the LGMD2A mutations themselves. PMID: 22006685
Data show that direct sequencing of CAPN3, encoding calpain-3, identified a homozygous deletion c.483delG (p.Ile162SerfsX17). PMID: 21172462
Limb-girdle muscular dystrophy patients carried a new splicing site mutation (c.1536+1G>T) in the CAPN3 gene, which leads to complete retention of intron 12 of the CAPN3 gene and total calpain3 deficiency. PMID: 20477750
5 different intronic variants (one novel) in CAPN3 that bioinformatic tools predicted would affect RNA splicing, underwent comprehensive studies which were designed to prove they are disease-causing. PMID: 20635405
CARP and its regulator calpain 3 appear to occupy a central position in the important cell fate-governing NF-kappaB pathway in skeletal muscle PMID: 20860623
The major c.550delA mutation in the CAPN3 gene was identified in 70% of Russian patients. PMID: 20517216
Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies. PMID: 20634290
The findings suggest that mutation analysis of the CAPN3 cDNA should use skeletal muscle tissue as materials instead of peripheral blood. PMID: 20533264
calpain 3 participates in the establishment of the pool of reserve cells by decreasing the transcriptional activity of the key myogenic regulator MyoD via proteolysis independently of the ubiquitin-proteasome degradation pathway. PMID: 20139084
reduced expression of calpain 3 was associated with phenotypes related to obesity and insulin resistance PMID: 12075569
effects of type of mutation, amount of calpain in the muscle, gender and ethnicity of affected patients on clinical course (age of onset and ascertainment) were analysed PMID: 12461690
reaction analysis of calpain p94 autolysis and domains PMID: 12482600
The enzyme is preferentially expressed in B- and T-lymphocytes, whereas it is poorly expressed in natural killer cells and almost undetectable in polymorphonuclear cells. PMID: 12882647
The 550delA mutation was present on 76% of CAPN3 (calpain 3) chromosomes that led us to screen general population for this mutation PMID: 14981715
Insertion sequence 1 of p94 acts as internal autoinhibitory propeptide, blocking the active site of p94 from substrates and inhibitors. PMID: 15073171
Ten novel CAPN3 mutations found in concentrated in several exons in Muscular Dystrophies patients PMID: 15221789
This study found that three novel mutations of calpain 3 gene in limb girdle muscular dystrophy type 2A (LGMD2A, calpainopathy). PMID: 15351423
Efficient and stable CAPN3 transgene expression in mouse muscle restores enzyme proteolytic activity without evident toxicity in a calpain 3-deficient mouse model of limb-girdle muscular dystrophy type 2A. PMID: 16290124
Thus, the proteolytic activity of the core of p94 and its deletion mutant lacking NS and IS1 was shown to be strictly Ca(2+)-dependent. We propose a two-stage model of activation of the proteolytic core of p94. PMID: 16533054
the importance of p94-connectin interaction in the control of p94 functions by regulating autolytic decay of p94 PMID: 16627476