Recombinant Human Cathepsin W (CTSW) Protein (His&Myc)

Name: Recombinant Human Cathepsin W (CTSW) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00377P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Enzymes, Featured enzyme molecules, High-quality recombinant proteins, Protease, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Human Cathepsin W (CTSW) 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	P56202
Target Symbol	CTSW
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	VPFSCDWRKVASAISPIKDQKNCNCCWAMAAAGNIETLWRISFWDFVDVSVQELLDCGRCGDGCHGGFVWDAFITVLNNSGLASEKDYPFQGKVRAHRCHPKKYQKVAWIQDFIMLQNNEHRIAQYLATYGPITVTINMKPLQLYRKGVIKATPTTCDPQLVDHSVLLVGFGSVKSEEGIWAETVSSQSQPQPPHPTPYWILKNSWGAQWGEKGYFRLHRGSNTCGITKFPLTARVQKPDMKPRVSCPP
Expression Range	128-376aa
Protein Length	Full Length
Mol. Weight	33.1 kDa
Research Area	Cell Biology
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	May have a specific function in the mechanism or regulation of T-cell cytolytic activity.; (Microbial infection) Plays a role during influenza virus infection in lungs cells ex vivo. Acts at the level of virus entering host cytoplasm from late endosome.
Subcellular Location	Endoplasmic reticulum.
Protein Families	Peptidase C1 family
Database References	HGNC: 2546 OMIM: 602364 KEGG: hsa:1521 STRING: 9606.ENSP00000311300 UniGene: Hs.416848
Tissue Specificity	Expressed predominantly in natural killer cells, and in cytotoxic T cells.

Gene Functions References

These results establish CtsW as an important host factor for entry of influenza A virus into target cells and suggest that CtsW could be a promising target for the development of future antiviral drugs. PMID: 26060270
The predominant expression of wildtype form by infiltrating immune cells was confirmed in 116 patients with gastroesophageal reflux disease and 27 reflux-negative individuals demonstrating that cathepsin W expression is not altered in this disease. PMID: 22050231
Cathepsin W-positive cells had a 'lymphocyte phenotype', but the relative portion of cathepsin W-positive cells among the infiltrating leukocytes in gastrointestinal disease differed remarkably. PMID: 12437118
a genetic variant and a novel isoform of cathepsin W are present in about 14% and 12%, respectively, within the Caucasian population PMID: 15358123
Despite being expressed in the effector subset of CD8(+) and NK cells and of being released during target cell killing, our functional inhibition studies exclude an essential role of CatW in the process of cytotoxicity. PMID: 19100676
Endogenous cathepsin W is expressed predominantly in NK cells, is up-regulated by IL-2, and is mainly targeted to the endoplasmic reticulum. PMID: 11490002

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.