Recombinant Mouse Caspase-12 (CASP12) Protein (His-B2M)

Name: Recombinant Mouse Caspase-12 (CASP12) Protein (His-B2M)
Brand: Beta LifeScience
SKU: BLC-07586P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Fc receptors, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Caspase-12 (CASP12) Protein (His-B2M) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O08736
Target Symbol	CASP12
Synonyms	(CASP-12)
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-B2M
Target Protein Sequence	MAARRTHERDPIYKIKGLAKDMLDGVFDDLVEKNVLNGDELLKIGESASFILNKAENLVENFLEKTDMAGKIFAGHIANSQEQLSLQFSNDE
Expression Range	1-92aa
Protein Length	Partial
Mol. Weight	24.3 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Involved in the activation cascade of caspases responsible for apoptosis execution.
Protein Families	Peptidase C14A family
Database References	KEGG: mmu:12364 STRING: 10090.ENSMUSP00000027009 UniGene: Mm.42163
Tissue Specificity	Mainly expressed in skeletal muscle and lung.

Gene Functions References

mice ablated for caspase-12 develop spontaneous obesity and insulin resistance. PMID: 26582949
Caspase-12 plays a pivotal role in CCl4-induced hepatic apoptosis through the activation of the downstream effector caspase-3 directly and/or indirectly via caspase-9 activation. PMID: 25561786
We validated caspase-12 as a therapeutic target, ablation of which significantly protects T17M photoreceptors from deterioration. PMID: 26207309
Findings an increase in multiple unfolded protein response pathways in muscles of the dystrophin-deficient mdx mouse, the model for Duchenne muscular dystrophy. PMID: 24879640
Tauroursodeoxycholic acid intervention down-regulated GRP78 and CHOP expression and Caspase 12 activation. PMID: 22212133
Findings indicate that although caspase-12 deficiency results in enhanced pro-inflammatory and immunoregulatory cytokine levels in sera during P. yoelii 17XL infection, these responses are not essential for protection against lethal malaria infection. PMID: 21086719
caspase-12 competed with NEMO for association with IkappaB kinase-alpha/beta, effectively preventing the formation of the IkappaB kinase complex and inhibiting downstream transcriptional activation by NF-kappaB. PMID: 20876354
Caspase-12 was required for an effective antiviral immune response, especially for the production of type I interferons through the regulation of TRIM25-mediated ubiquitination of RIG-I. . PMID: 20818395
Matrix metalloproteinase-3 is increased and participates in neuronal apoptotic signaling downstream of caspase-12 during endoplasmic reticulum stress PMID: 20368330
Reactive oxygen species promote caspase-12 expression and tubular apoptosis in diabetic nephropathy. PMID: 20299359
enhanced repair response of Casp12(-/-) mice rendered them more susceptible to colorectal cancer induced by azoxymethane (AOM)+ dextran sulfate sodium. PMID: 20226691
role of caspase-12-dependent pathway in apoptosis induction by manganese(II) PMID: 11964391
caspase-12 was activated by poly(Q)(72) aggregates via a pathway independent of caspase-8 and caspase-3 activation, and caspase-12 activation was closely associated with poly(Q) aggregate-mediated cell death PMID: 12045204
procaspase-9 is a substrate of caspase-12 and ER stress triggers a specific cascade involving caspase-12, -9, and -3 in a cytochrome c-independent manner. PMID: 12097332
Caspase-12 seems to be involved in neuronal death induced by ischemia/reperfusion. PMID: 12699784
Pathways involving this enzyme are involved in a neurodegenerative disease in vivo, and thus offer novel potential targets for the treatment of prion disorders. PMID: 14532116
caspase-12 expression in caspase-12 is regulated by NF-E2 and participates in the development of fully functional signaling pathways linking some G-protein-coupled receptors to alphaIIbbeta3 activation. PMID: 15059849
both caspases and calpains are involved in 661W photoreceptor apoptosis PMID: 15210718
The results indicate that oxidative and ER induced stress causing caspase-12 activation are involved in neuronal death and disease progression in ALS. PMID: 15313203
cloning of promoter PMID: 15701691
caspase-12 and caspase-4 are not required for the induction of ER stress-induced apoptosis and that caspase-4-like activity is not always associated with an initiating event. PMID: 15975932
Ribozyme 138 prepared in vitro can site specific cleave mouse caspase-12 mRNA with an excellent efficiency. PMID: 15996037
Data show that overexpression of X-linked Inhibitor of Apoptosis Protein (XIAP)inhibits caspase-12 cleavage and reduces calpain activity in amyotrophic lateral sclerosis mice. PMID: 16566922
provides compelling genetic evidence for calpain's role in caspase-12 activation at the endoplasmic reticulum (ER), and reveals a novel role for the ubiquitous calpains in ER-stress induced apoptosis and JNK activation PMID: 16597616
In mice, caspase-12 deficiency confers resistance to sepsis and its presence exerts a dominant-negative suppressive effect on caspase-1, resulting in enhanced vulnerability to bacterial infection and septic mortality PMID: 16625199
apoptosis-inducing factor plays the major role in this apoptotic event, whereas caspase-12 has a reinforcing effect PMID: 17088543
Data show that caspase-12 can compensate for lack of caspase-2 and caspase-3 in female germ cells. PMID: 17245644
In hippocampal neuroblasts, Ca(++) mobilization from ER and caspase-12 activation are components of the molecular pathway that leads to apoptosis triggered by serum deprivation and may constitute an amplifying loop of the mitochondrial pathway. PMID: 17399692
Nod activation and resulting antimicrobial peptide production constitute an early innate defense mechanism, and caspase-12 inhibits this mucosal antimicrobial response. PMID: 18329614
caspase-12 is not necessary for mediating the neurotoxic effects of prion protein misfolding. PMID: 19164919

FAQs

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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.