Recombinant Human Cystatin-B (CSTB) Protein (GST)

Name: Recombinant Human Cystatin-B (CSTB) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03621P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Cystatin-B (CSTB) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P04080
Target Symbol	CSTB
Synonyms	CHROW21; CPI B; CPI-B; CST 6; CST6; CSTB; Cystatin B (stefin B); Cystatin B; Cystatin-B; CYTB; CYTB_HUMAN; EPM1; EPM1A; Liver thiol proteinase inhibitor; PME; Stefin-B; STF B; STFB; ULD
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MMCGAPSATQPATAETQHIADQVRSQLEEKENKKFPVFKAVSFKSQVVAGTNYFIKVHVGDEDFVHLRVFQSLPHENKPLTLSNYQTNKAKHDELTYF
Expression Range	1-98aa
Protein Length	Full Length
Mol. Weight	38.1kDa
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	This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	Cystatin family
Database References	HGNC: 2482 OMIM: 254800 KEGG: hsa:1476 STRING: 9606.ENSP00000291568 UniGene: PMID: 29037838 The results demonstrate that cystatin B interferes with the STAT-1 signaling and IFN-beta-antiviral responses perpetuating HIV in macrophage reservoirs. PMID: 27137788 apoptosis is accompanied by degradation of the cysteine cathepsin inhibitor stefin B (StfB). CatD did not exhibit a crucial role in this step. However, this degradation was partially prevented through pre-incubation with the antioxidant N-acetyl cysteine PMID: 28543404 Homozygous for a c.218dupT (p.His75Serfs*2) mutation in exon 3 of CSTB causes neurodegeneration, progressive cerebral volume loss and diffuse hypomyelination. PMID: 28378817 CSTB downregulation may promote the development of gastric cancer. PMID: 28281969 It was shown that decreased expression of cystatin B enhances cathepsin activity in Niemann-Pick C cerebellar degeneration patient fibroblasts. PMID: 26908626 High expression of stefin B may be an important factor contributing to the development and metastasis of Hepatocellular Carcinoma. PMID: 26753874 CSTB null mutation associated with microcephaly, early developmental delay, and severe dyskinesia. PMID: 26843564 Data shows that CYTB and ANXA4 overexpression may be involved in carcinogenesis and histopathological differentiation of ovarian clear cell carcinoma and suggest they may serve as a potential diagnostic biomarkers. PMID: 25633807 A role for disease-causing mutations in cystatin B gene in patients with juvenile myoclonic epilepsy was not supported. PMID: 25752200 Even though the majority of EPM1 patients have a uniform genetic mutation, the actual size of the longer CSTB expansion mutation allele is likely to have a modulating effect on the age at disease onset, myoclonus severity, and cortical neurophysiology. PMID: 25770194 The study shows detection of stefin B dimers in HEK293 cells and the importance of their residual activity. PMID: 25047918 glutamate dehydrogenase is a euchromatin-associated enzyme, and its H3 clipping activity is regulated by chromatin structure, histone modifications and an in vivo inhibitor. PMID: 25263734 detected a homozygous expansion of dodecamer repeats in the CSTB gene in four patients with clinical diagnosis of ULD. PMID: 23883076 The increased CSTB expression in ovarian tissue represents tumor progression and is dysregulated by the TGF-beta signaling pathway. PMID: 24452274 A reciprocal influence of CSTB and SOD1 at the gene expression level and for a direct interaction of the two proteins, is reported. PMID: 24234043 The present study was performed on two more missense mutants of human stefin B, G50E and Q71P, and they similarly showed numerous aggregates upon overexpression. PMID: 24909779 The co-localization of stefin B wild type and EPM1 mutants with cathepsins showed that cathepsins accumulate around the aggregates formed by the EPM1 mutants. PMID: 23362198 Skull thickening and an increased prevalence of abnormal findings in skeletal radiographs of patients with EPM1 suggest that this condition is connected to defective cystatin B function. PMID: 23010349 This study suggested that CSTB mutations other than the common dodecamer expansion predict particular phenotypes, including marked seizure severity and polymorphous seizure types. PMID: 23205931 Elevated StefA mRNA level is associated with invasive glioblastoma. PMID: 22287159 S-glutathionylation and S-cysteinylation were described as extensive PTM of a salivary protein and the first time that these PTMs were detected in naturally occurring cystatin B. PMID: 22057043 patients compound heterozygous for the dodecamer repeat expansion and the c.202C>T mutations seem to have a severer form of Unverricht-Lundborg disease (EPM1) than patients homozygous for the expansion mutation PMID: 21757863 At pH 7.0 the mutant H75W folded in three kinetic phases to a native-like intermediate, analogous to folding of stefin B at pH 4.8. PMID: 22033403 Intracellular stefin b aggregation shows a negative correlation with cell survival PMID: 20078424 Stefin B interacts with histones and cathepsin L in the nucleus PMID: 20075068 oligomers of stefin B and amyloid-beta interact in vitro and in cells PMID: 19955183 Oligonucleotides containing EPM1 repeat adopt secondary structures that may facilitate strand slippage thereby causing the expansion. PMID: 11697734 Intramolecular i-motif structure at acidic pH for progressive myoclonus epilepsy (EPM1) repeat d(CCCCGCCCCGCG)n. PMID: 11697735 analysed eight markers flanking CSTB(GT10-D21S1890-D21S1885-D21S2040-D21S1259- CSTB-D21S1912-PFKL-D21S171) and one intragenic variant in the CSTB 3' UTR (A2575G) PMID: 12215838 first demonstration of cysteine protease activity being regulated by CSTB activity in a biological context; effects of decreased CSTB activity in EPM1 pathogenesis may be mediated by cathepsins through increased activity of cathepsins S and L PMID: 12452481 Prefibrillar oligomers/aggregates of stefin B also increase the surface pressure at an air-water interface, i.e. they have amphipathic character and are surface seeking. PMID: 15955063 These data show that cystatin B inhibits bone resorption by down-regulating intracellular cathepsin K activity despite increased osteoclast survival. PMID: 16321512 Study shows that copper binding by stefin B inhibits the amyloid fibril formation and, to a lesser degree, the initial aggregation. PMID: 16939620 Several alternatively spliced CSTB isoforms were identified in patients with progressive myoclonus epilepsy of Unverricht-Lundborg type . PMID: 17003839 Results describe the influence of pH and trifluoroethanol on amyloid fibril growth and morphology from human stefin B. PMID: 17701471 cystatin B in vivo has a polymeric structure sensitive to the redox environment and that overexpression of the protein generates aggregates. PMID: 17920138 CSTB is specifically overexpressed in most HCCs and is also elevated in the serum of a large proportion of HCC patients PMID: 18281540 Data show that wild-type stefin B and its Y31 isoform are able to form pores in planar lipid bilayers, whereas the G4R isoform destroys the bilayer by a non pore-forming process. PMID: 18397316 The mechanism of amyloid-fibril formation by stefin B: temperature and protein concentration dependence of the rates;the observed kinetics follow the nucleation and growth behavior observed for many other amyloidogenic proteins. PMID: 18636508 potential role for CSTB in HIV replication in placental macrophages PMID: 18951626 cystatin B interacts with STAT-1 and the levels of STAT-1 tyrosine phosphorylation (but not serine phosphorylation) between uninfected and HIV-infected PM and MDM are differentially regulated. PMID: 19342095

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.