Recombinant Human Calpastatin (CAST) Protein (His)

Name: Recombinant Human Calpastatin (CAST) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10878P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Calpastatin (CAST) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P20810
Target Symbol	CAST
Synonyms	BS 17; Calpain inhibitor; Calpastatin; Cast; Heart type calpastatin ; ICAL_HUMAN; MGC9402; Sperm BS 17 component ; Sperm BS-17 component
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MNPTETKAVKTEPEKKSQSTKPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD
Expression Range	1-667aa
Protein Length	Full Length of isoform 4
Mol. Weight	75.9kDa
Research Area	Neuroscience
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	Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
Protein Families	Protease inhibitor I27 (calpastatin) family
Database References	HGNC: 1515 OMIM: 114090 KEGG: hsa:831 UniGene: PMID: 29428799 Kaposi sarcoma-associated herpesvirus reduces CAST (calpastatin) and consequently decreases ATG5 expression in both THP-1 monocytoid cells and primary monocytes. PMID: 27715410 Loss of CAST in angiogenic ECs facilitates mu-calpain-induced SOCS3 degradation, which amplifies pathological angiogenesis through interleukin-6/STAT3/VEGF-C axis. PMID: 25648699 We describe PLACK syndrome, as a clinical entity of defective epidermal adhesion, caused by loss-of-function mutations in calpastatin. PMID: 25683118 Calpastatin binds with Cav1.2 amino acid motifs in a calcium dependent manner. PMID: 24462690 Calpastatin gene (CAST) is not associated with late onset sporadic Parkinson's disease in the Han Chinese population. PMID: 23951044 Linkage analysis and genetic association support involvement of CAST gene in the genetic susceptibility to keratoconus. PMID: 23449483 Neuronal overexpression of calpastatin modulates amyloid precursor protein processing in brains of transgenic beta-amyloid depositing mice. PMID: 22206846 Calpastatin overexpression reduces calpain-mediated proteolysis and behavioral impairment after traumatic brain injury. PMID: 22572592 Mycoplasma hyorhinis membrane lipoproteins induce calpastatin upregulation in human cells PMID: 22288381 calpastatin-calpain balance varied during Th-1,2, and -17 development; overexpression of a domain of calpastatin suppressed production of IL-6 and IL-17 by Th cells and of IL-6 by fibroblasts; suppression of IL-6 occurred by reducing NF-kappaB signaling PMID: 22046434 The data supports the hypothesis that calpastatin may play a role in regulating the initial metastatic dissemination of breast cancer. PMID: 21531560 calpain basal activity becomes measurable at a significant extent in peripheral blood mononuclear cells from cystic fibrosis patients due to a 40-60% decrease in both calpastatin protein and inhibitory activity PMID: 21983488 CSL competes with CaM as a partial agonist for the site in the IQ domain in the C-terminal region of the Cav1.2 channel, which may be involved in activation of the channel. PMID: 21937422 intervertebral discs at early stages of degeneration expressed low levels of calpastatin, and few cells expressed degenerative enzymes. At more advanced stages of degeneration, expression and number of cells immunopositive for calpastatin were higher PMID: 21839844 Variations in CAST gene is associated with femoral neck Low bone mineral density. PMID: 21424381 A confirmation study reports that a single nucleotide polymorphism and CAST are associated with Parkinson disease. PMID: 20127884 involved in the proteolysis of amyloid precursor protein, which is thought to be abnormal in patients with Alzheimer's disease PMID: 11849768 Overexpression of calpastatin reduced muscle atrophy during 10 day unloading period. Overexpression completely prevented shift in myofibrillar myosin content from slow to fast isoforms, which normally occurs in muscle unloading. PMID: 12482888 insights into how the calpain/calpastatin network is spatially and temporally regulated in cells binding to the extracellular matrix PMID: 14559243 Calpastatin amino acid side chains at leucine-11 and isoleucine-18 interact with hydrophobic pockets in calpain, and each of these interactions is indispensable for effective inhibition of calpain. PMID: 14992597 Overexpression of calpastatin in transgenic mice is associated with an increase in GLUT4 protein. PMID: 15014085 A complete calpain-calpastatin system is expressed in the human oocyte and may play a role in the various calcium-mediated processes occurring during activation of human oocytes. PMID: 15950654 Results suggest a regulation on the calpain-calpastatin expression response to muscle damaging eccentric exercise, but not concentric exercise. PMID: 18340456 genetically determined IL-1alpha levels may modulate transcription of calpain and calpastatin PMID: 18498295 NMR data of calapastin tripartite binding mode to capain induced by calcium were presented. PMID: 18519038 performed a full NMR assignment of hCSD1 to characterize it in its solution state PMID: 18537264 Role of the calpain-calpastatin system in the density-dependent growth arrest. PMID: 18809371 recruitment of calpastatin into aggregates allows translocation and activation of protease to the membranes; on the contrary, the presence of large amounts of calpastatin in the cytosol prevents both processes, protecting the cell from proteolysis PMID: 19103264 Genome-wide association study of gene-disease association and pharmacogenomic / toxicogenomic. (HuGE Navigator) PMID: 18195134

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.