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Rabbit Anti-TPP1 Recombinant Antibody (CBYJT-4385) (CBMAB-T3878-YJ)

Provided herein is a Rabbit monoclonal antibody, which binds to TPP1 (Tripeptidyl Peptidase 1). The antibody can be used for immunoassay techniques, such as WB, IP.
See all TPP1 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Monkey
Clone
CBYJT-4385
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Specificity
Human, Monkey
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
PBS, pH 7.4
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
TPP1 Gene(Protein Coding) Tripeptidyl Peptidase 1
Introduction
TPP1 is a member of the sedolisin family of serine proteases. TPP1 functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. TPP1 is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in TPP1 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.
Entrez Gene ID
Human1200
Monkey709838
UniProt ID
HumanO14773
MonkeyF7BXH4
Alternative Names
Tripeptidyl Peptidase 1; Cell Growth-Inhibiting Gene 1 Protein; Tripeptidyl Aminopeptidase; Tripeptidyl Peptidase I; EC 3.4.14.9; TPP-1; CLN2; LPIC; Ceroid-Lipofuscinosis, Neuronal 2, Late Infantile (Jansky-Bielschowsky Disease); Spinocerebellar Ataxia, Autosomal Recessive 7
Function
Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:11054422, PubMed:19038966, PubMed:19038967).
May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (PubMed:11054422, PubMed:19038966, PubMed:19038967).
Requires substrates with an unsubstituted N-terminus (PubMed:19038966).
Biological Process
Biological Process bone resorption Source:UniProtKB1 Publication
Biological Process central nervous system development Source:GO_Central1 Publication
Biological Process epithelial cell differentiation Source:UniProtKB1 Publication
Biological Process lipid metabolic process Source:ProtInc1 Publication
Biological Process lysosomal protein catabolic process Source:Ensembl
Biological Process lysosome organization Source:UniProtKB
Biological Process nervous system development Source:UniProtKB1 Publication
Biological Process neuromuscular process controlling balance Source:UniProtKB
Biological Process peptide catabolic process Source:UniProtKB2 Publications
Biological Process protein catabolic process Source:UniProtKB1 Publication
Biological Process protein localization to chromosome, telomeric region Source:CACAO1 Publication
Biological Process proteolysis Source:UniProtKB2 Publications
Cellular Location
Lysosome
Melanosome
Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Involvement in disease
Ceroid lipofuscinosis, neuronal, 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.
Spinocerebellar ataxia, autosomal recessive, 7 (SCAR7):
A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR7 patients show difficulty walking and writing, dysarthria, limb ataxia, and cerebellar atrophy.
PTM
Activated by autocatalytic proteolytical processing upon acidification (PubMed:11054422, PubMed:19038966, PubMed:19038967).
N-glycosylation is required for processing and activity (PubMed:19038966, PubMed:19038967).
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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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