Recombinant Human Tripeptidyl-Peptidase 2 (TPP2) Protein (His&Myc)

Name: Recombinant Human Tripeptidyl-Peptidase 2 (TPP2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04768P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Tripeptidyl-Peptidase 2 (TPP2) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P29144
Target Symbol	TPP2
Synonyms	TPP2; Tripeptidyl-peptidase 2; TPP-2; EC 3.4.14.10; Tripeptidyl aminopeptidase; Tripeptidyl-peptidase II; TPP-II
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	DTGVDPGAPGMQVTTDGKPKIVDIIDTTGSGDVNTATEVEPKDGEIVGLSGRVLKIPASWTNPSGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPVHRVALAEACRKQEEFDVANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGEVWRACIDSNEDGDLSKSTVLRNYKEAQEYGSFGTAEMLNYSVNIYDDGNLLSIVTSGGAH
Expression Range	44-264aa
Protein Length	Partial
Mol. Weight	31.8 kDa
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	Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis.
Subcellular Location	Cytoplasm. Nucleus. Note=Translocates to the nucleus in responce to gamma-irradiation.
Protein Families	Peptidase S8 family
Database References	HGNC: 12016 OMIM: 190470 KEGG: hsa:7174 STRING: 9606.ENSP00000365233 UniGene: PMID: 26041847 Early-onset Evans syndrome, immunodeficiency, and premature immunosenescence associated with TPP2 deficiency have been described in two consanguineous siblings. PMID: 25414442 Study found that autosomal recessive TPP2 mutations cause recurrent infections, autoimmunity, and neurodevelopmental delay in humans. PMID: 25525876 TPPII, MYBBP1A and CDK2 form a protein-protein interaction network. PMID: 25303791 Previously unknown differences between TPP II orthologues and subtilisin as well as features that might be conserved within the entire family of subtilisin-like serine peptidases. PMID: 22266401 Study showed that overexpression of Tripeptidyl peptidase II (TPP2) occurs frequently during oral carcinogenesis and might be associated with the progression of Oral Squamous Cell Carcinoma (OSCC) via Spindle Assembly Checkpoint(SAC) activation. PMID: 22986808 obtained a 3D structure of the human TPPII PMID: 22483107 Current knowledge about TPPII with a focus on structural aspects. PMID: 21771670 Results suggest an important function of TPPII in the maintenance of viral growth and may have implications for anti-viral therapy. PMID: 21134372 the promoter could be localized to a 215 bp fragment upstream of the initiation codon. PMID: 15716107 TPPII appears to promote malignant cell growth by allowing exit from mitosis and the survival of cells with severe mitotic spindle damage. PMID: 16762321 TPP2 plays a specialized role in antigen processing and one that is not essential for the generation of most presented peptides. PMID: 16849449 This investigation reveals that TPP II expression could be regulated through both positive and negative regulatory elements. PMID: 17343995 Expression of mRNA for MuRF-1 increased approximately 3-fold at 10 days without changes in MAFbx or tripeptidyl peptidase II mRNA, but all decreased between 10 and 21 days of muscle disuse. PMID: 17901116 Results indicate that TPPII is dispensable for the generation of proteasome-dependent HLA class I ligands and, the enzyme is not involved significantly in generating the proteasome-independent HLA-B27-bound peptide repertoire. PMID: 18286573 Cross-presentation of NY-ESO-1/ISCOMATRIX cancer vaccine was proteasome independent and requires the cytosolic protease tripeptidyl peptidase II. PMID: 19155470 MHC class I-restricted LMP1 epitopes studied in this work are two of very few epitopes known to date to be processed proteasome independently by tripeptidyl peptidase II. PMID: 19587004

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.