Recombinant Human BTD Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0458

Recombinant Human BTD Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0458
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Product Overview

Tag His
Host Species Human
Accession P43251
Synonym BTD
Background Biotinidase, also known as biotinase and BTD, is a ubiquitous mammalian cell enzyme which expressed at high levels in the liver, serum, and kidney. Its primary function is to cleave biotin from biocytin, preserving the pool of biotin for use as a cofactor for biotin dependent enzymes, namely the 4 human carboxylases. Biotinidase also recycles biotin from enzymes in the body that use it as a helper component in order to function. These enzymes, known ascarboxylases, are important in the processing offats,carbohydrates, andproteins. Biotin is attached to these carboxylase enzymes through anamino acid(the building material of proteins) calledlysine, forming a complex calledbiocytin.
Description A DNA sequence encoding the human BTD (P43251) (Met1-Asp543) with a C-terminal His tag was expressed.
Source HEK293
Predicted N Terminal Ala 42
AA Sequence Met1-Asp543
Molecular Weight The recombinant human BTD comprises 513 a.a. and has a predicted molecular mass of 58.2 kDa. The apparent molecular mass of the protein is approximately 66-76 kDa in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by its ability to hydrolyze biocytin to lysine and biotin. The specific activity is >500pmol/min/ug.
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein 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.

Target Details

Target Function Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation.
Subcellular Location Secreted, extracellular space.
Protein Families Carbon-nitrogen hydrolase superfamily, BTD/VNN family
Database References
Associated Diseases Biotinidase deficiency (BTD deficiency)

Gene Functions References

  1. BTD mutation is associated with biotinidase deficiency. PMID: 29995633
  2. Biotinidase deficiency is reviewed. PMID: 26577040
  3. Four rare missense variants were identified (ACTBL2 rs73757391 (5q11.2), BTD rs200337373 (3p25.1), KRT13 rs150321809 (17q21.2) and MC2R rs104894658 (18p11.21)), but only MC2R rs104894668 had a large effect size (OR = 9.66). PMID: 27378695
  4. The history and genetic basis of biotinidase deficiency has been presented. (Review) PMID: 26456103
  5. 48 novel alterations in the biotinidase gene have been identified; correlating the individual's serum enzymatic activity with genotype, were able to determine the effect of the novel alteration on enzyme activity and, thereby, determine its likelihood of being pathogenic in 44 of these individuals PMID: 26810761
  6. The common biotinidase gene mutations (p.R157H, p.D444H, c.98-104del7ins3, p.T532M) cumulatively accounted for 72.3% of all the mutant alleles in the Turkish population. PMID: 25754625
  7. Summary of the demographic features of patients identified as biotinidase deficient from August of 2012 through August of 2013 and mutation analysis results for 20 cases in the southeast region of Turkey. PMID: 25423671
  8. Three novel pathogenic variants in BTD gene were identified in a cohort of Brazilian patients with biotinidase deficiency and control suggesting an allelic heteregeneity of the condition. PMID: 25174816
  9. Report incidence of profound biotinase deficiency in Swedish newborns and adoptive immigrant children. PMID: 20224900
  10. High frequencies of biotinidase mutations may explain the high incidence of biotinidase deficiency in Hungary. PMID: 20549359
  11. Mutation analysis revealed three novel mutations, c.del631C and c.1557T>G within exon 4 and c.324-325insTA in exon 3 in Biotinidase deficiency patients and families. PMID: 23481307
  12. Four Somali patients have the P497S mutation, with one of the four being homozygous for the mutation PMID: 19757147
  13. Six different mutations in the biotinidase gene are identified in biotinidase in four Chinese patients; determination of biotinidase activities are performed for selective screening of biotinidase deficiency PMID: 19728141
  14. loss of overall biotinidase expression is a novel marker for thyroid cancer aggressiveness. PMID: 22911723
  15. Plasma BTD activity increases in hepatic glycogen storage disease patients. PMID: 20532819
  16. 140 known mutations in the biotinidase gene (BTD) that cause biotinidase deficiency, are reported. PMID: 20556795
  17. Mutations in biotinidase is associated with biotinidase deficiency. PMID: 20539236
  18. 12 patients with multiple carboxylase deficiency, six mutations were found in the BT gene and 4 in the HLCS gene, including 5 novel mutations. PMID: 19806568
  19. review of mutations causing biotinidase deficiency PMID: 11668630
  20. report of 17 novel mutations that cause profound biotinidase deficiency. Six of the mutations are due to deletions, whereas the remaining 11 mutations are missense mutations located throughout the gene PMID: 12359137
  21. analysis of mutations in biotinidase deficiency PMID: 15776412
  22. 21 different mutations were identified in 49 patients, including four novel mutations. Ten mutations proved to be unique to the Hungarian population. PMID: 17185019
  23. Posttranslational modification of histones by biotinylation can be catalyzed by biotinidase; role of this function is ambiguous. PMID: 18479898
  24. This case indicates that biotinidase deficiency should be included in the differential diagnosis of subacute myelopathy and emphasizes the importance of a prompt diagnosis to prevent irreversible neurological damage. PMID: 18645204


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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.

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