Recombinant Human Dna Fragmentation Factor Subunit Beta (DFFB) Protein (His)

Name: Recombinant Human Dna Fragmentation Factor Subunit Beta (DFFB) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00905P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Dna Fragmentation Factor Subunit Beta (DFFB) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O76075
Target Symbol	DFFB
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSRIYKPQTRLKRKQPVRKRQ
Expression Range	1-338aa
Protein Length	Full Length
Mol. Weight	45.1 kDa
Research Area	Cancer
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	Nuclease that induces DNA fragmentation and chromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.
Subcellular Location	Cytoplasm. Nucleus.
Database References	HGNC: 2773 OMIM: 601883 KEGG: hsa:1677 STRING: 9606.ENSP00000367454 UniGene: PMID: 28981092 Dff40 expression is upregulated in atherosclerotic plaque. PMID: 28007744 the low expression levels of DFF40/CAD and the absence of DNA laddering as common molecular traits in glioblastoma PMID: 26755073 Data suggest DFF40 expression in breast cancer cell line is involved in drug sensitivity/resistance to doxorubicin; apoptotic cell death due to doxorubicin (a topoisomerase II inhibitor) is enhanced by DFF40 overexpression in breast cancer cell line. PMID: 26529233 Combinatorial use of some sulfonamides such as acetazolamide along with increased expression of DFF40 can potently kill tumor cells via apoptosis. PMID: 25086620 DFF40/CAD-independent mechanism driving conformational nuclear changes during caspase-dependent cell death PMID: 24838313 the highest order of chromatin compaction observed in the later steps of caspase-dependent apoptosis relies on DFF40/CAD-mediated DNA damage by generating 3'-OH ends in single-strand rather than double-strand DNA nicks/breaks PMID: 23430749 These results suggest a cooperative activity between CAD and DNAS1L3 to accomplish internucleosomal DNA fragmentation . PMID: 23229555 Human papillomavirus type 16 E6 protein inhibits DNA fragmentation via interaction with DNA fragmentation factor 40 PMID: 22609799 During apoptotic rearrangement of interchromatin granule clusters, the nuclear matrix (NuMa rearrangement) and chromatin are closely associated. This process occurs in defined stages and depends on the activity of protein phosphatases, caspases and CAD. PMID: 22023725 the cytosolic levels of DFF40/CAD are determinants in achieving a complete apoptotic phenotype, including oligonucleosomal DNA degradation. PMID: 22253444 Data show that among the 13 SNPs in the 3 genes, only 3 were found to be polymorphic: R196K and K277R in the DFFB gene, and S12L in the EndoG gene, and all 6 SNPs in the FEN-1 gene were entirely monoallelic. PMID: 22011247 These data suggest that DFF 40 mediated apoptosis plays a significant role in mediating sepsis induced cellular dysfunction. PMID: 21820410 Mutations and aberrantly spliced transcripts for the CAD gene are frequently associated with hepatocellular carcinoma. PMID: 12610505 Hsp70 binds free CAD in TCR-stimulated T cells to stabilize and augment its activity. PMID: 12738667 CAD involves unrestricted accessibility of chromosomal DNA at the initial phase of apoptosis, followed by its nuclear immobilization that may prevent the release of the active nuclease into the extracellular environment. PMID: 15569712 PARP-1 poly(ADP-ribosyl)ation is a terminal event in the apoptotic response that occurs in response to DNA fragmentation and directly influences DFF40 activity PMID: 15703174 Interactions identified here between human placenta histone H1 carboxyl-terminal domain and DFF40/CAD target and activate linker DNA cleavage during the terminal stages of apoptosis. PMID: 15910001 Our findings of high frequency of Alu-mediated hCAD deletion in human hepatoma underscore the implication of hCAD in hepatocarcinogenesis PMID: 16007181 AIF is responsible for stage I nuclear morphology and HMW DNA degradation is a caspase-activated DNase and AIF-independent process PMID: 16049016 levels of CAD were significantly higher in the nuclear fraction of temporal lobe epilepsy samples PMID: 16121124 DFFB haploinsufficiency from 1p allelic loss is a contributing factor in oligodendroglioma development PMID: 16156899 in apoptotic cells, endogenous and exogenous CAD forms limited oligomers, representing the active nuclease PMID: 16204257 the N-terminal region was found to be responsible for the requirement of salt for fibril formation PMID: 16428311 CAD is downregulated at the mRNA and protein level during the erythroid differentiation in TF-1 cells. PMID: 16529748 poly-glutamic acid and heparin inhibit DFF40/CAD, the latter one being highly effective at nanomolar concentrations. The inhibitory poly-anions bind to the nuclease and impair its ability to bind double-stranded DNA. PMID: 16699957 These results suggest that CAD is the endogenous endonuclease that mediates internucleosomal DNA degradation in rotenone-induced apoptosis. PMID: 17239993 Data suggest that erythroblast chromatin degradation may involve caspase activated DNase and apoptosis inducing factor, enzymes distinct from those active in apoptotic cells. PMID: 17492772 changes induced in DNA conformation upon HMG-box binding makes the substrate more accessible to cleavage by DFF40/CAD nuclease and thus may contribute to preferential linker DNA cleavage during apoptosis PMID: 18239742 We have found that neither single-stranded DNA, single-stranded RNA, double-stranded RNA nor RNA-DNA heteroduplexes are cleaved by the DFF40/CAD nuclease. PMID: 18283539

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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.