Recombinant Mouse Bis (FHIT) Protein (His)

Name: Recombinant Mouse Bis (FHIT) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08199P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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.

Product Overview

Description	Recombinant Mouse Bis (FHIT) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O89106
Target Symbol	FHIT
Synonyms	FhitBis(5'-adenosyl)-triphosphatase; EC 3.6.1.29; AP3A hydrolase; AP3Aase; Diadenosine 5',5'''-P1,P3-triphosphate hydrolase; Dinucleosidetriphosphatase; Fragile histidine triad protein
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	SFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFRDLHPDEVADLFQVTQRVGTVVEKHFQGTSITFSMQDGPEAGQTVKHVHVHVLPRKAGDFPRNDNIYDELQKHDREEEDSPAFWRSEKEMAAEAEALRVYFQA
Expression Range	2-150aa
Protein Length	Full Length of Mature Protein
Mol. Weight	19.1kDa
Research Area	Others
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	Possesses dinucleoside triphosphate hydrolase activity. Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate. Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate. Also catalyzes the ammonolysis of adenosine 5-phosphorofluoridate and diadenosine triphosphate. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity. Functions as tumor suppressor.
Subcellular Location	Cytoplasm. Nucleus. Mitochondrion.
Database References	KEGG: mmu:14198 STRING: 10090.ENSMUSP00000123874 UniGene: Mm.397619
Tissue Specificity	Expressed in heart, brain, lung and skeletal muscle. Particularly strong expression in liver, testis and kidney, where it is confined to the tubular epithelium.

Gene Functions References

Fhit loss and subsequent thymidine kinase 1 inactivation, combined with selective pressures, leads to neoplasia-associated alterations in genes and gene expression patterns in vitro and in vivo PMID: 27513973
Fhit-deficiency mutation signature also resembles a C>T and T>C mutation signature reported for human papillary kidney cancers and a similar signature recently reported for esophageal and bladder cancers, cancers that are frequently Fhit deficient. PMID: 26782170
Fhit deficiency-induced global genome instability promotes mutation and clonal expansion PMID: 24244712
Fhit delocalizes annexin A4 from plasma membrane to cytosol and sensitizes lung cancer cells to paclitaxel. PMID: 24223161
FHIT gene is a "caretaker gene" necessary for maintenance of genome stability. PMID: 23929738
Loss of Fhit expression contributes to cell transformation. PMID: 23102829
Defects in Fhit expression may promote MHC-I down-regulation in cancer cells and allow escape from immunosurveillance. PMID: 22451343
Human and mouse orthologous genes, FHIT and Fhit, are more highly conserved through evolution than PTPRG/Ptprg and yet contain more sequence elements that are exquisitely sensitive to genomic rearrangements PMID: 14630947
Fhit has a role in bladder cancer development PMID: 15569992
UV-induced alterations of the FHIT and WWOX fragile site gene expression are involved at least partially in the checkpoint function of DNA damage PMID: 15798093
Data suggest that heterozygosity for FHIT affects susceptibility of mice to spontaneous alopecia areata and benzo[a]pyrene-induced preneoplastic lesions of the uterus and does not alter responsiveness to budesonide and N-acetyl-L-cysteine. PMID: 16672365
Nit1 and Fhit share tumor suppressor signaling pathways, while localization of the NIT1 gene at a stable chromosome site explains the paucity of gene alterations and in frequent loss of expression of the NIT1 gene in human malignancies. PMID: 16864578
It is likely that the FHIT transgene is more tightly silenced in female transgenic mice, leading to a lack of protection from tumor induction PMID: 18000371
tumor-like microdeletions in FHIT/FRA3B are induced by replication stress PMID: 18162546
reduced oxidative stress, coupled with efficient but not error-free DNA damage repair, allows unscheduled long-term survival of genotoxin-exposed Fhit-deficient hematopoietic stem cells carrying deleterious mutations PMID: 18483248
the extent of tumor susceptibility due to Nit1 and Fhit deficiency is additive PMID: 19479888

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.