Recombinant Mouse Cystatin-C (CST3) Protein (His&Myc)

Name: Recombinant Mouse Cystatin-C (CST3) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04018P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Mouse Cystatin-C (CST3) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P21460
Target Symbol	CST3
Synonyms	Cst3Cystatin-C; Cystatin-3
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	ATPKQGPRMLGAPEEADANEEGVRRALDFAVSEYNKGSNDAYHSRAIQVVRARKQLVAGVNYFLDVEMGRTTCTKSQTNLTDCPFHDQPHLMRKALCSFQIYSVPWKGTHSLTKFSCKNA
Expression Range	21-140aa
Protein Length	Full Length of Mature Protein
Mol. Weight	20.4 kDa
Research Area	Cardiovascular
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	As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.
Subcellular Location	Secreted.
Protein Families	Cystatin family
Database References	KEGG: mmu:13010 STRING: 10090.ENSMUSP00000028938 UniGene: PMID: 27079462 Data (including data from studies in mutant mice) suggest that up-regulation of Cst3, as observed in plasma of mice with type 2 diabetes, down-regulates insulin signaling and promotes endoplasmic reticulum stress in hepatocytes but not in myotubes. PMID: 26592151 Cystatin C is a potential pathogenic signal triggering neurodegeneration in multiple system atrophy. PMID: 24405769 The neuroprotective activity of CysC against Amyotrophic lateral sclerosis-linked mutant Cu/Zn-superoxide dismutase (SOD1)-mediated toxicity. PMID: 25356866 an important role for macrophages, DC, and ROS in diseases associated with the protease inhibitory activity or amyloidogenic properties of cystatin C. PMID: 24570004 APP expression stimulates NSPC proliferation; this effect is mediated via an increase in cystatin C secretion PMID: 23671283 Cystatin C, a protein targeted to the classical secretory pathway by its signal peptide sequence, is secreted by primary neurons in at least 9 different cystatin C glycoforms associated with exosomes. PMID: 19773092 The lack of cystatin C enhances Collagen-induced arthritis and primarily affects in vivo priming of the immune system PMID: 21443774 Inflammation causes downregulation of cystatin C expression in dendritic cells and reduces serum CstC levels. PMID: 21300820 Data show that the absence of cystatin C reduced epithelial cell apoptosis but increased proliferation in skin. PMID: 21085595 Data show that cystatin C effectively rescues cystatin B loss-of-function mutation, facilitating the reversal of pathophysiological changes and suggesting a novel therapeutic intervention for patients with neurodegenerative disorders. PMID: 20889561 CysC plays a protective role under conditions of neuronal challenge by inducing autophagy via mTOR inhibition PMID: 20352108 Oxidants induce elevated cystatin C production from cardiac myocytes. Cystatin C plays a role in cardiac extracellular matrix remodelling. PMID: 20489058 Data show that cystatin c (CystC) contributes to experimental abdominal aortic aneurysms (AAA) pathogenesis and that lack of CystC favors inflammation in AAA lesions induced in atherosclerotic mice. PMID: 20472891 The embryo's cystatin C and F expression functions as a protective mechanism against the maternal proteinase cathepsin S. PMID: 20093401 Cystatin C through this effect can act as an immunomodulatory molecule. PMID: 19446036 expressed in decidual cultures and the expression is controlled in part by TGF-beta(1) and EGF signaling PMID: 11803549 spatiotemporal up-regulation of cystatin C in the hippocampus is induced by entorhinal deafferentation (perforant path transections) PMID: 12044447 Cystatin C is neither necessary nor sufficient to control expression of major histocompatibility type II complexes and antigen presentation in dendritic cells. PMID: 14607896 In vivo overexpression of human cystatin C does not affect amyloid-beta levels in mice that do not deposit amyloid-beta. PMID: 14742906 Data indicate that cystatin C is involved in astrocyte differentiation during mouse brain development. PMID: 15509901 leukocyte-specific expression of cystatin C is actively involved in matrix remodelling associated with atherosclerosis plaque regression. PMID: 15823274 the protective role of cystatin C in atherosclerosis is dependent primarily on its expression in nonhematopoietic cell types PMID: 16051881 PKB activity is a critical downstream component of PDK-1 in mediating translation of cystatin C, RANKL, and Rab11a PMID: 16166629 These data demonstrate that cystatin C has a role in neuronal death and neurogenesis during SE-induced network reorganization. PMID: 16242633 Validity of cystatin C for generating neural stem cells from embryo stem cells in vitro. PMID: 16595632 We propose that in MS, remyelination may be impaired by increasing activity of cathepsins inadequately controlled by cystatin C. PMID: 17086443 Finally, in vivo studies using kidney-specific megalin knockout mice provide evidence that megalin mediates proximal tubular uptake of cystatin C. We conclude that megalin is an endocytic receptor of cystatin C in PTC. PMID: 17462596 These results suggest that CysC affects the BMP signaling cascades in osteoblastic cells and then promotes osteoblast differentiation, mineralization, and bone formation. PMID: 17592728 Plasminogen activator inhibitor-2, but not cystatin C, inhibits the prometastatic activity of tissue inhibitor of metalloproteinases-1 in the liver.( PMID: 18681831 CysC regulates soluble Abeta and Abeta-associated neuronal deficits through inhibiting CatB-induced Abeta degradation. PMID: 18957217

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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.