Human Recombinant CTSB protein, His Tag-1 (V2LY-0526-LY2604)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant CTSB protein, His Tag consist of Amino Acid: 18-339 and predicts a molecular mass of 37.2 kDa.
Molecule Mass
37.2 kDa
Verified
HPLC
Sequence
Amino Acid: 18-339
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥97% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Sodium phosphate, NaCl, Imidazole, DTT, Glycerol
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it 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.
More Infomation

Target

Full Name
Cathepsin B
Function
Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (PubMed:12220505).

Cleaves matrix extracellular phosphoglycoprotein MEPE (PubMed:12220505).

Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity).

Has also been implicated in tumor invasion and metastasis (PubMed:3972105).
Biological Process
Cellular response to thyroid hormone stimulus Source: UniProtKB
Collagen catabolic process Source: BHF-UCL
Epithelial cell differentiation Source: UniProtKB
Neutrophil degranulation Source: Reactome
Proteolysis Source: UniProtKB
Proteolysis involved in cellular protein catabolic process Source: BHF-UCL
Regulation of apoptotic process Source: UniProtKB
Regulation of catalytic activity Source: InterPro
Toll-like receptor signaling pathway Source: Reactome
Cellular Location
Lysosome; Apical cell membrane; Extracellular space; Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells (By similarity).
Involvement in disease
Keratolytic winter erythema (KWE):
The gene represented in this entry is involved in disease pathogenesis. Tandem duplications in a non-coding genomic region containing an active enhancer element for CTSB result in CTSB abnormal expression with pathological consequences.
An autosomal dominant genodermatosis characterized by recurrent episodes of palmoplantar erythema and epidermal peeling presenting seasonal variation. KWE manifests during childhood. Skin lesions may spread to the dorsum of hands and feet and to the interdigital spaces. Lower legs, knees and thighs may also be involved. A less common finding is a slowly migratory, annular erythema that is seen mostly on the extremities. Between flares, the skin can appear unremarkable. Itching can occur, and hyperhidrosis, associated with a pungent odor, is invariably present. Formation of vesicles is rare, whereas keratolysis that causes the formation of dry blisters is regularly seen. Cold weather, moisture, febrile diseases, and physical and mental stress can trigger exacerbations. In severely affected individuals, skin manifestations persist unremittingly. Penetrance of the disease is high, but expressivity is variable, even within the same family.

Dai, J., Zhang, Q., Wan, C., Liu, J., Zhang, Q., Yu, Y., & Wang, J. (2021). Significances of viable synergistic autophagy-associated cathepsin B and cathepsin D (CTSB/CTSD) as potential biomarkers for sudden cardiac death. BMC Cardiovascular Disorders, 21(1), 1-15.

Iwama, H., Mehanna, S., Imasaka, M., Hashidume, S., Nishiura, H., Yamamura, K. I., ... & Ohmuraya, M. (2021). Cathepsin B and D deficiency in the mouse pancreas induces impaired autophagy and chronic pancreatitis. Scientific reports, 11(1), 1-10.

Mizunoe, Y., Kobayashi, M., Hoshino, S., Tagawa, R., Itagawa, R., Hoshino, A., ... & Higami, Y. (2020). Cathepsin B overexpression induces degradation of perilipin 1 to cause lipid metabolism dysfunction in adipocytes. Scientific reports, 10(1), 1-12.

Kuang, F., Liu, J., Li, C., Kang, R., & Tang, D. (2020). Cathepsin B is a mediator of organelle-specific initiation of ferroptosis. Biochemical and Biophysical Research Communications, 533(4), 1464-1469.

Ni, Y., Hai, Z., Zhang, T., Wang, Y., Yang, Y., Zhang, S., & Liang, G. (2019). Cathepsin B Turning Bioluminescence “On” for Tumor Imaging. Analytical Chemistry, 91(23), 14834-14837.

Aghdassi, A. A., John, D. S., Sendler, M., Weiss, F. U., Reinheckel, T., Mayerle, J., & Lerch, M. M. (2018). Cathepsin D regulates cathepsin B activation and disease severity predominantly in inflammatory cells during experimental pancreatitis. Journal of Biological Chemistry, 293(3), 1018-1029.

Sendler, M., Weiss, F. U., Golchert, J., Homuth, G., van den Brandt, C., Mahajan, U. M., ... & Mayerle, J. (2018). Cathepsin B-mediated activation of trypsinogen in endocytosing macrophages increases severity of pancreatitis in mice. Gastroenterology, 154(3), 704-718.

Araujo, T. F., Cordeiro, A. V., Vasconcelos, D. A., Vitzel, K. F., & Silva, V. R. (2018). The role of cathepsin B in autophagy during obesity: A systematic review. Life sciences, 209, 274-281.

Bai, H., Yang, B., Yu, W., Xiao, Y., Yu, D., & Zhang, Q. (2018). Cathepsin B links oxidative stress to the activation of NLRP3 inflammasome. Experimental cell research, 362(1), 180-187.

Yan, Y., Zhou, K., Wang, L., Wang, F., Chen, X., & Fan, Q. (2017). Clinical significance of serum cathepsin B and cystatin C levels and their ratio in the prognosis of patients with esophageal cancer. OncoTargets and therapy, 10, 1947.

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For research use only. Not intended for any clinical use.

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