Recombinant Mouse Cystatin F / CMAP Protein (Fc Tag)

Name: Recombinant Mouse Cystatin F / CMAP Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-1537
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	Fc
Host Species	Mouse
Accession	O89098
Synonym	Cmap
Background	The cystatin superfamily members are important natural cysteine protease inhibitors present in a wide variety of organisms and are divided into three classes. Cystatin F, also known as leukocystatin and CMAP (Cystatin-like Metastasis-Associated Protein), is a type 2 cystatin and its expression is limited to hematopoietic cells, with the highest expression levels being observed in monocytes, dendritic cells, and certain types of T-cells. Furthermore, cystatin F mRNA becomes up-regulated during dendritic cell maturation, and thus suggests a specific role of cystatin F in immune regulation. Cystatin F is produced as a dimer, an inactive cathepsin inhibitor which is activated by chemical reduction. In addition, Cystatin F and its homologues have been observed expressing in various human cancer cell lines established from malignant tumors, and thus indicates a new diagnosis and prevention approach of certain human carcinomas metastasis.
Description	A DNA sequence encoding the mouse CST7 (O89098) (Met1-Gln144) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
Source	HEK293
Predicted N Terminal	Ala 19
AA Sequence	Met1-Gln144
Molecular Weight	The recombinant mouse CST7 /Fc is a disulfide-linked homodimer. The reduced monomer comprises 367 a.a. and has a predicted molecular mass of 41.4 KDa. The apparent molecular mass of the protein is approximately 42 KDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity	>93% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by its ability to inhibit active Cathepsin L cleavage of a fluorogenic peptide substrate Z-LR-AMC, R&D Systems, Catalog # ES008.The IC50 is < 6 nM.
Formulation	Lyophilized from sterile 25mM Tris, 0.15M NaCl, pH 7.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system.
Subcellular Location	Secreted.
Protein Families	Cystatin family
Database References	KEGG: mmu:13011 STRING: 10090.ENSMUSP00000086606 UniGene: Mm.12965

Gene Functions References

High CST7 expression is associated with Alzheimer's disease. PMID: 28904096
Our results validate cystatin F as a useful biomarker of early pathogenesis in experimental models of prion disease, and point to unexpected species-specific differences in the transcriptional responses to prion infections. PMID: 28178353
During the active remyelinating phase, both CysF knockdown (CysFKD) and microglial-selective CatC overexpression (CatCOE) showed a worsening of the demyelination in Plp(4e/-) transgenic mice. Conversely, during the chronic demyelinating phase, CatC knockdown (CatCKD) ameliorated the demyelination. Our results suggest that the balance between CatC and CysF expression controls the demyelination and remyelination process. PMID: 28251676
The cystatin F expression in the activated microglia is closely associated with the effect of the A2A receptors, which may be related to the neuroinflammatory responses occurring during the pathological process. PMID: 23285090
an inhibitory activity other than cystatin F quenches CatL activity in activated macrophages PMID: 21956111
Expression of cystatin F indicates ongoing demyelination and remyelination; absence of cystatin F expression indicates cessation of remyelination in the demyelinating area. PMID: 21344476

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.