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

Name: Recombinant Mouse Tripeptidyl-Peptidase 2 (TPP2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04767P
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 Mouse Tripeptidyl-Peptidase 2 (TPP2) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q64514
Target Symbol	TPP2
Synonyms	Tpp2; Tripeptidyl-peptidase 2; TPP-2; EC 3.4.14.10; Tripeptidyl aminopeptidase; Tripeptidyl-peptidase II; TPP-II
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	DTGVDPGAPGMQVTTDGKPKIIDIIDTTGSGDVNTATEVEPKDGEIIGLSGRVLKIPANWTNPLGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPIHRVALAEACRKQEEFDIANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGETWRACVDSNENGDLSKCAVLRNYKEAQEYSSFGTAEMLNYSVNIYDDGNLLSIVTSGGAH
Expression Range	44-264aa
Protein Length	Partial
Mol. Weight	29.5 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	KEGG: mmu:22019 STRING: 10090.ENSMUSP00000085244 UniGene: PMID: 23818952 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 Tripeptidyl peptidase II is crucial for nucleoprotein epitope generation during major histocompatibility complex class I complex viral antigen processing both in the presence and absence of lactacystin-sensitive proteasome action. PMID: 17088258 TPPII is not generally required for the production of major histocompatibility class I-restricted peptides, but presentation of some peptides can be negatively affected by TPPII. PMID: 17357105 Data show that mice that were homozygous for an insertion in the Tpp2 locus were embryonic lethal and Tpp2 heterozygous mutants were lean compared with wild-type littermates, although food intake was normal. PMID: 17932511 The data suggest a moderate, predominantly destructive role of TPPII in class I Ag processing. PMID: 18056356 TPPII is important for maintaining normal cellular and systemic physiology, which may be relevant for potential therapeutic applications of TPPII inhibitors PMID: 18362329 These results do not support a generally important role of TPPII for viability and proliferation of transformed cells or their p53-mediated DNA damage response. PMID: 19539606 These data indicate that while TPPII contributes to the trimming of peptides with very long N-terminal extensions, TPPII is not essential for generating most MHC class I-presented peptides or for stimulating CTL responses to several Ags in vivo. PMID: 19841172

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.