Tripeptidyl Peptidase I Recombinant Protein | TPP1 recombinant protein

Recombinant Tripeptidyl Peptidase I (TPP1)

Cat. Num. AAA2029667

• Gene Names: TPP1; CLN2; GIG1; LPIC; SCAR7; TPP-1
• Applications: SDS-Page, Western Blot, ELISA, Immunoprecipitation
• Purity: >90%
• Synonyms: Tripeptidyl Peptidase I; Recombinant Tripeptidyl Peptidase I (TPP1); TPP1 recombinant protein

• Host: Host: E Coli; Source: Prokaryotic expression
• Purity/Purification: >90%
• Form/Format: Supplied as lyophilized form in PBS, pH7.4, containing 5% trehalose, 0.01% sarcosyl.
• Sequence: The target protein is fused with two N-terminal Tags, His-tag and T7-tag, its sequence is listed below.; MRLFGGNFAH QASVARVVGQ QGRGRAGIEA SLDVQYLMSA GANISTWVYSSPGRHEGQEP FLQWLMLLSN ESALPHVHTV SYGDDEDSLS SAYIQRVNTELMKAAARGLT LLFASGDSGA GCWSVSGRHQ FRPTFPASSP YVTTVGGTSFQEPFLITNEI VDYISGGGFS NVFPRPSYQE EAVTKFLSSS PHLPPSSYFNASGRAYPDVA ALSDGYWVVS NRVPIPWVSG TSASTPVFGG ILSLINEHRILSGRPPLGFL NPRLYQQHGA GLFDVTRGCH ESCLDEEVEG QGFCSGPGWDPVTGWGTPNF PALLKTLLNP
• Sequence Length: 563

• Applicable Applications for TPP1 recombinant protein: SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
• Predicted Molecular Mass: 38.2kDa
• Accurate Molecular Mass (KD): 38kDa
• Endotoxin: <1.0EU per 1ug (determined by the LAL method)
• Expression System: Prokaryotic expression
• Tag: two N-terminal Tags, His-tag and S-tag
• Organism Species: Homo sapiens (Human)
• Fragment: Met1~Pro320
• Usage: Reconstitute in sterile PBS, pH7.2-pH7.4.
• Preparation and Storage: Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.; Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. The loss of this protein is less than 5% within the expiration date under appropriate storage condition.

Sequence Information

SDS-Page

NCBI and Uniprot Product Information

• NCBI GI #: 15928808
• NCBI GeneID: 1200
• Molecular Weight: 34,464 Da
• NCBI Official Full Name: Tripeptidyl peptidase I
• NCBI Official Synonym Full Names: tripeptidyl peptidase I
• NCBI Official Symbol: TPP1
• NCBI Official Synonym Symbols: CLN2; GIG1; LPIC; SCAR7; TPP-1
• NCBI Protein Information: tripeptidyl-peptidase 1
• UniProt Protein Name: Tripeptidyl-peptidase 1
• Protein Family: Tripeptidyl-peptidase
• UniProt Gene Name: TPP1
• UniProt Synonym Gene Names: CLN2; TPP-1; LPIC; TPP-I
• UniProt Entry Name: TPP1_HUMAN

NCBI Description

This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. [provided by RefSeq, Jul 2008]

Uniprot Description

TPP1: Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus. Defects in TPP1 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2). A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles. Belongs to the peptidase S53 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Secreted; Protease; Mitochondrial; Secreted, signal peptide; EC 3.4.14.9

Chromosomal Location of Human Ortholog: 11p15

Cellular Component: lysosomal lumen; mitochondrion; lysosome; melanosome

Molecular Function: tripeptidyl-peptidase activity; peptidase activity; protein binding; serine-type peptidase activity; serine-type endopeptidase activity; metal ion binding; endopeptidase activity; peptide binding

Biological Process: nervous system development; unfolded protein response, activation of signaling protein activity; cellular protein metabolic process; epithelial cell differentiation; unfolded protein response; lysosome organization and biogenesis; peptide catabolic process; protein catabolic process; lipid metabolic process; proteolysis; neuromuscular process controlling balance; bone resorption

Disease: Ceroid Lipofuscinosis, Neuronal, 2