Native Human Calpain 1 Protein

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P07384
Synonym	Ca2 activated neutral protease Calcium activated neutral proteinase Calcium activated neutral proteinase small subunit Calcium dependent protease small subunit Calcium dependent protease small subunit 1 Calcium-activated neutral proteinase 1 Calpain 1 Calpain 1 large subunit Calpain 1, (mu/I) large subunit Calpain mu type Calpain mu-type Calpain regulatory subunit Calpain small subunit 1 Calpain, large polypeptide L1 Calpain-1 catalytic subunit Calpain-1 large subunit CAN1_HUMAN CANP CANP 1 CANP small subunit CANP1 CANPL 1 CANPL1 CAPN 1 CAPN1 Cell proliferation inducing protein 30 Cell proliferation-inducing gene 30 protein Micromolar Calpain Micromolar-calpain Mu Calpain muCANP muCL
Description	Native Human Calpain 1 Protein is native.. It is a Full length protein
Source	Native
Molecular Weight	110 kDa
Purity	>95% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	>=1,000 units per mg protein.One unit is defined as the amount of enzyme that hydrolyzes one picomole of Suc-LLVY-AMC per minute at 25degC.
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409'.
Subcellular Location	Cytoplasm. Cell membrane.
Protein Families	Peptidase C2 family
Database References	HGNC: 1476 OMIM: 114220 KEGG: hsa:823 STRING: 9606.ENSP00000279247 UniGene: Hs.502842
Associated Diseases	Spastic paraplegia 76, autosomal recessive (SPG76)
Tissue Specificity	Ubiquitous.

Gene Functions References

Unexpected role of the L-domain of calpastatin during the autoproteolytic activation of human erythrocyte calpain. PMID: 29572388
Studies indicate that reactive oxygen and nitrogen species (RONS) and calpain play important roles in the development of airway and pulmonary vascular remodeling in COPD. PMID: 29047085
Calpain-1 was significantly expressed in Triple-negative breast cancer tissues varying from low to high with a significant correlation to lymph node status but not with the other clinicopathological variables, suggesting its role as a prognostic factor PMID: 28536704
These findings suggest that calpain and AR-V7 may serve as important biomarkers in the treatment of castration-resistant prostate cancer , and targeting calpain and AR-V7 may provide a new approach in overcoming docetaxel-resistance. PMID: 28498452
Rare homozygous and compound-heterozygous nonsense, missense, frameshift, and splice-site mutations in CAPN1 were identified in all hereditary spastic paraplegia affected individuals, and sequencing in additional family members confirmed the segregation of these mutations with the disease. PMID: 27153400
the cleavage of myoferlin, yielding a membrane-associated dual C2 domain 'mini-myoferlin', is reported. PMID: 28192161
mutations in CAPN1 are an additional cause of ataxia in mammals, including humans. PMID: 27320912
Calpain-1 expression is associated with poor relapse-free survival in breast cancer patients treated with trastuzumab. PMID: 26496999
Regulation of platelet-activating factor-mediated PTP1B activation by a Janus kinase 2/ calpain pathway has been reported. PMID: 28686728
HRNR deimination improves its cross-linking by TGases and its proteolytic processing by calpain-1. PMID: 27742573
calpains and calpastatin in patients with idiopathic pulmonary arterial hypertension (PAH) and mice with hypoxic or spontaneous (SM22-5HTT(+) strain) PH, were investigated. PMID: 26974350
calpain and protein kinase Calpha abnormal release promotes a constitutive release of matrix metalloproteinase 9 in peripheral blood mononuclear cells from cystic fibrosis patients PMID: 27349634
Endoplasmic reticulum stress may be associated with apoptosis of LECs, resulting in cataract formation in diabetic patients. PMID: 27130368
our findings suggest that the gene/protein expression of both CAPN1 and CAPN2, as well as the ERK1 and ERK2 genes and related proteins, could be molecular factors associated with more invasive tumor behavior in squamous cell laryngeal cancer. PMID: 27456359
This study demonstrated that Upregulation of calpain activity precedes tau phosphorylation and loss of synaptic proteins in Alzheimer's disease brain. PMID: 27036949
the calpain-dependent cleavage of Nav1.6 channels expressed in human embryonic kidney (HEK) 293 cells caused the upregulation of I(NaP) PMID: 26974309
Increased mu-Calpain Activity in Blasts of Common B-Precursor Childhood Acute Lymphoblastic Leukemia Correlates with Their Lower Susceptibility to Apoptosis. PMID: 26317226
Data indicate that calpain is responsible for processing translation termination factor eRF3 into its IAP-binding isoform p-eRF3. PMID: 26172506
NOS stimulation via PI3K, calpain proteases, and SIRT1-dependent deacetylation downstream from VEGFR2 activation contributes to these vasodilator responses. PMID: 26284543
Junctophilin-2 is cleaved by calpain at multiple sites, resulting in dysfunctional junctophilin-2 truncations. PMID: 26063807
The results of this study indicated that reductions in kallikrein-6 and calpain-1 may contribute to the accumulation of alpha-synuclein in DLB. PMID: 25476568
findings suggest that truncation/activation of Dyrk1A by Ca(2+)/calpain I might contribute to Tau pathology via promotion of exon 10 exclusion and hyperphosphorylation of Tau in AD brain PMID: 25918155
5-LOX inhibition reduced apoptotic death, restored the initial IL-2/INF-gamma ratio, and more importantly reverted micro-calpain activation induced by simulated microgravity. PMID: 25309925
the p12/Pol delta is a target as a nuclear substrate of mu-calpain in a calcium-triggered apoptosis and appears to be a potential marker in the study of the chemotherapy of cancer therapies. PMID: 24691096
Data show the X-ray structures of calpain with (Z)-3-(4-chlorophenyl)-2-mercaptoacrylic acid and (Z)-3-(5-bromoindol-3-yl)-2-mercaptoacrylic acid. PMID: 25086406
CAPN1 anchors to two NCX1 regions and cleaves at methionine-369, leading to NCX1 inactivation in heart failure. PMID: 25336645
Besides, calpain-1, a calcium-dependent cysteine protease, was involved inherpes simplex virus type 1 intracellular trafficking. PMID: 24670325
Ayloid beta mediates calpain cleavage of NCX3 in Alzheimer's disease brain. PMID: 23919677
Increased trophoblast apoptosis and altered expression levels of syncytin-1, calpain 1, and AIF is observed in preeclamptic placentas. PMID: 24413738
The PC1 function on JAK2 and ERK signaling pathways might be regulated by calpains in response to the changes in intracellular calcium concentration. PMID: 24416790
Small interfering RNA (siRNA)-mediated silencing of micro-calpain expression significantly suppressed the adhesive, migrative and invasive potentials of human hepatoma cells. PMID: 23733271
HER2 inhibited calpain-1 activity through upregulating calpastatin, an endogenous calpain inhibitor. PMID: 23707532
Calpain activation via Ca(2) flux plays an essential role in eliciting an AIF-mediated, caspase-independent apoptotic pathway in EV71-infected cells. PMID: 23515028
a truncated fragment of Src protein kinase generated by calpain-mediated cleavage is a mediator of neuronal death in excitotoxicity PMID: 23400779
Extracellular signal-regulated kinase and glycogen synthase kinase 3beta regulate gephyrin postsynaptic aggregation and GABAergic synaptic function in a calpain-dependent mechanism PMID: 23408424
Proteolysis of calcineurin A by endogenous calpain I leads to the formation of constitutively active calcineurin in the human heart, which may contribute to the pathogenesis of myocardial disease PMID: 23289183
Data indicate that calpain-1 plays a pivotal role in matrix metalloproteinase 2 (MMP2) activation and extracellular matrix remodeling, including fibrosis and vascular calcification. PMID: 23006733
Report synthesis of emodin derivatives, emodin carbaldehyde, citreorosein, and their 10-deoxygenated derivatives and their inhibitory activities on mu-calpain. PMID: 22477191
Results show that estrogen may contribute to both up-regulation and proteolysis of cyclin E through calpain in MCF-7 cells. PMID: 22449977
APP secretion from the calpain overexpressing cells was robustly increased under both resting and stimulated conditions over wild-type cells. PMID: 22480599
Overexpression of mu-calpain in the anterior temporal neocortex is associated with intractable epilepsy as well as the clinicopathological characteristics in these patients. PMID: 21315622
Data show neutrophil calpain I (mu-calpain) was inactiveted by alpha1-antitrypsin. PMID: 21494752
With higher grading of the ovarian carcinoma, staining intensity and immunoreactive score of calpain 1 decreased. PMID: 22335024
Results show high levels of the 17-kDa tau fragment and enhanced calpain activity in the temporal cortex of AD patients and in brain samples obtained from patients with other tauopathies. PMID: 21442128
The expression of mu-calpain-induced degradation products of extracellular matrix was correlated with the degree of disc degeneration in human intervertebral disc tissue PMID: 21839844
siRNA knockdown of calpain prevented deltamethrin-induced DNA fragmentation. PMID: 21555338
it is possible to protect cells from paclitaxel-induced degradation of NCS-1 by inhibiting calpain activity PMID: 21808066
Data show that transfection of cells with GRP78 or calpain I and calpain II siRNA reduced MPTB-mediated cell apoptosis in chondrosarcoma JJ012 cells PMID: 21374734
Findings show that p73alpha and its regulation by the Ca(2+)-mediated calpain pathway are involved in CDDP-induced apoptosis in OVCA cells and that dysregulation of Ca(2+)/calpain/p73 signaling may in part be the pathophysiology of CDDP resistance. PMID: 21516125
Rad21 cleavage by calpain-1 promotes separation of chromosome arms, which coincides with a calcium-induced partial loss of cohesin at several chromosomal loci. PMID: 21876002

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.