Tripeptidyl-peptidase 1 Antibodies

Tripeptidyl-peptidase 1 (TPP1)

Lysosomal serine protease with tripeptidyl-peptidase I action. May act as a non invasive lysosomal peptidase which generates tripeptides from the breakdown products created by lysosomal proteinases.

Requires substrates having an unsubstituted N-terminus (By similarity). .

Gene Information

Human
Gene Name:	TPP1
Uniprot:	O14773
Entrez:	1200

Family

Belongs to:
No superfamily

Alternative Names

Cell growth-inhibiting gene 1 protein; ceroid-lipofuscinosis, neuronal 2, late infantile (Jansky-Bielschowsky disease); CLN2; CLN2EC 3.4.14.9; growth-inhibiting protein 1; LINCL; LPIC; lysosomal pepstatin insensitive protease; Lysosomal pepstatin-insensitive protease; MGC21297; TPP1; TPP-1; TPP-I; Tripeptidyl aminopeptidase; tripeptidyl peptidase I; tripeptidyl-peptidase 1; TripeptidylPeptidase I; Tripeptidyl-Peptidase I

Molecular Weight

Mass (kDA):
61.248 kDA

Genomic Context

Human
Location:	11p15.4
Sequence:	11; NC_000011.10 (6612768..6619422, complement)

Tissue Specificity

Detected in all tissues examined with highest levels in heart and placenta and relatively similar levels in other tissues.

Subcellular Localizations

Lysosome. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Diseases

• Neuronal Ceroid-lipofuscinoses
• Late-infantile Neuronal Ceroid Lipfuscinosis
• Malignant Neoplasms
• Infantile Neuronal Ceroid Lipofuscinosis
• Neurodegenerative Disorders
• Neoplasms
• Nerve Degeneration
• Telomere Shortening
• Nervousness
• Lysosomal Storage Diseases
• Blind Vision
• Ataxia

• Cytogenetic Abnormality
• Genomic Instability
• Epilepsy
• Dysplasia
• Visual Impairment
• Atrophy

Interacting Proteins

• STN1
• TERT

Pathways

• Telomere Maintenance
• Pathogenesis
• Localization
• Dna Repair
• Senescence
• S Phase
• Cell Cycle
• Telomere Binding
• Rna Interference
• Transport
• Aging
• Segmentation
• Telosome Assembly

• Cell Death
• Cell Growth
• Single-stranded Dna Binding
• Secretion
• Hair Follicle Morphogenesis
• Cellular Senescence
• Immune Response

PTMs

• Cleavage
• Glycosylation
• Oxidation

• Deglycosylation
• Phosphorylation
• Dephosphorylation

Research Areas

• Neuroscience

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/TPP1

Best Uses of the TPP1 Marker

TPP1 is a protein that is common in humans as well as other animals. Researchers who study the gene are often asked questions about bioactivity and pharmacology. Boster Bio has a comprehensive product list for this gene. This includes special samples, species, and applications. Scientists from all over the world can receive product credits for their work. This article will discuss the most common uses of the TPP1 gene marker in various fields.

Codon optimized nucleic Acid Sequence

A codon optimized sequence of nucleic acids is critical for protein expression, particularly when produced in heterologous system. E. coli uses more common codons to increase the success of protein synthesis. Codons can be used to transmit genetic information to mRNA. Codon optimization refers to selecting preferred codons, and removing rare codons.

The software allows users enter DNA sequences or amino acid sequences to optimize codons. It can optimize Genes and gBlocks gene segments, as well as recombinant protein sequences. It automatically detects how complex the sequence is and suggests the most efficient option with the least complexity. The process of codon optimizing is fully customizable. Users can adjust the results to fit their needs.

Consider the differences between the wild type protein and the variants of it when designing the codon optimized nucleic- acid sequence. Codon optimization is a way to increase protein expression, and also improve the immunogenicity. For instance, TSOL18 may be more immunogenic when produced with optimal codons. This strategy can also increase production rates of recombinant protein.

A high-quality codon optimization algorithm will increase protein expression by increasing its elongation as well as accuracy. Many studies have found a weak correlation in the relationship between codon bias, gene expression, and codon bias. Different strategies may be more effective in different organisms. OptimumGeneTM allows you to enhance protein expression by altering a wide range factors that are crucial for the expression of proteins. It also considers the various transcription cis-elements.

Pharmacology/bioactivity endpoints

The TPP1 Gene is an important candidate in the detection of Parkinson's disease and other neurodegenerative illnesses. Several animal models have been used to study the role of TPP1 in disease progression. In a pharmacological study on PD, the Tpp1m1j mouse was used. To express the optimal TPP1 in brain tissues, mice were given a nucleic acids sequence. Mice expressing the gene showed early signs of the disease in this model. They had tremors and gait abnormalities as well as generalized fatal seizures.

Mouse model

A TPP1-marker is a strategic tool to aid in drug discovery. To facilitate communication between regulators and drug developers, the FDA has published draft guidelines. The TPPs establish shared definitions of success and are an essential component of refinement in public health. TCPs are constantly being updated because drug development can often take years or decades.

While no single molecule has a single TCP, several molecules share some biological activities. One molecule may accomplish several TCPs. For malaria patients to be treated, it may be necessary to use a combination TCPs. Researchers can identify gaps within the TCP framework with the TCP Framework. Vaccines against Pfs25, 230 and 230 are in development. This is vital for the future of malaria treatment.

Pharmacological Applications

The TPP1 gene contains many alleles. Below are the frequencies. Most of these alleles can be found in CLN2-positive individuals, while a few may also occur in those without the disease. The mutations in TPP1 are caused by changes in the RNA coding sequence. They are located within the propeptide domain, and were obtained through CRISPR/Cas9 Homology Direct Repair Technology.

TPP1 deficiency causes early death in zebrafish, which exhibit widespread storage material containing ATP synthase subunit c. This material is more evident in the CNS and muscles than in other tissues. TPP1 is absent in zebrafish, resulting in an early neurodegenerative condition. This is accompanied by hyperactivity, which is consistent and indicative of seizures. Storage bodies, which accumulate in all visceral organs, are key targets for potential treatments.

TPP1 is expressed in two forms - the proenzyme and the mature enzyme. TPP1 was detected by Western blot in the control H9 and homozygous mutant HESCs c.622C–T. The latter form was detected in lower concentrations than the control H9 hESCs.

A gene variant testing can be used to identify TPP1 enzyme deficiency. The American College of Medical Genetics recommends reporting gene mutations based upon their clinical and phenotypic importance. It is still difficult for people to understand novel missense or in-frame variants. This disease-associated variant genetic variation is a reliable standard for CLN2 diagnostics. The presence of TPP1 enzyme activity confirms the diagnosis.

Clinical trials

Understanding the evolutionary and molecular history of TPP1 mutations is important, as they are often linked to human diseases. This knowledge could be used as a guideline for understanding human mutations. It could also be extended to other elements in the shelterin complex. This knowledge could be used to make clinical trials easier based upon these genetic variations. It would also make it easier for NBS data to be interpreted, as they are often based around the mutation of one gene.

TPP1 OB contains the TEL patch, and NOB mutations. These mutations prevent the recruitment of telomerase to telomeres, and are associated with telomeropathies. A severe form of DC is caused by the deletion of K170. It is called Hoyeraal Hreidarsson syndrome. Clinical trials with this marker may reveal the genetic causes of telomeropathies.

Although the TPP1 gene mutation update revealed that the gene coding the CLN2 enzyme was associated with a variety diseases, it has been difficult for scientists to interpret. Many of these disorders have novel missense and/or in frame mutations making it difficult to interpret. The diagnosis of CLN2 disease was confirmed by the presence two pathogenic variants in CLN2 sufferers. TPP1 enzyme activation can also be confirmed in patients with CLN2 disease.

The TPP1 gene that encodes soluble Lysosomal Peptide 1 (TPP1) has been identified. It has 563 amino acid residues, and it consists of three major domains. While most research in this area focuses on the CNS and other visceral organs, the storage bodies can also be found in other areas. This genetic mutation has a high chance of being treated.