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AB162872

Recombinant Human DPP8 protein

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(1 Publication)

Recombinant Human DPP8 protein is a Human Full Length protein, in the 1 to 898 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

DPRP1, MSTP097, MSTP135, MSTP141, DPP8, Dipeptidyl peptidase 8, DP8, Dipeptidyl peptidase IV-related protein 1, Dipeptidyl peptidase VIII, Prolyl dipeptidase DPP8, DPRP-1, DPP VIII

1 Images
SDS-PAGE - Recombinant Human DPP8 protein (AB162872)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human DPP8 protein (AB162872)

ab162872 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

WB, ELISA

applications

Biologically active

No

Accession

Q6V1X1

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":898,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q6V1X1","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Dipeptidyl peptidase 8 also known as DPP8 is a serine protease enzyme that cleaves x-proline dipeptides from the N-termini of peptides. It has a molecular mass of around 88 kDa and shares structural similarities with DPP4. DPP8 is expressed in various tissues including the brain liver and skin but shows a notably high expression in immune cells. The enzyme is involved in regulating various physiological processes depending on its tissue distribution.
Biological function summary

DPP8 seems to play roles in modulating immune responses and cell proliferation. It functions independently and is not typically part of a larger protein complex. Studies suggest a connection between DPP8 and cellular processes such as apoptosis and inflammation although the exact biological roles require more detailed investigation.

Pathways

The peptidase activity of DPP8 integrates within metabolic and immune system pathways. In the context of metabolism it relates closely to proteins like DPP4 which influences glucose homeostasis. In immune pathways DPP8 regulates the processing of peptides affecting immune cell communication and activity sharing roles with other immune-related proteases.

DPP8 exhibits connections with inflammatory and metabolic conditions. For example its dysregulation may relate to inflammatory bowel disease (IBD) possibly affecting inflammatory cytokine release. DPP8's function parallels with DPP4 linking it indirectly to disorders like type 2 diabetes where DPP4 inhibitors are a therapeutic angle. Further exploration of DPP8's roles could indicate potential as a therapeutic target in these conditions.
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Specifications

Form

Liquid

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General info

Function

Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed : 11012666, PubMed : 12534281, PubMed : 12662155, PubMed : 15039077, PubMed : 15664838, PubMed : 20536396, PubMed : 29382749). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed : 27820798, PubMed : 29967349, PubMed : 32796818). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed : 33731929, PubMed : 33731932, PubMed : 34019797). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP8, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (By similarity).

Sequence similarities

Belongs to the peptidase S9B family. DPPIV subfamily.

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Product protocols

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Target data

Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed : 11012666, PubMed : 12534281, PubMed : 12662155, PubMed : 15039077, PubMed : 15664838, PubMed : 20536396, PubMed : 29382749). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed : 27820798, PubMed : 29967349, PubMed : 32796818). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed : 33731929, PubMed : 33731932, PubMed : 34019797). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP8, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (By similarity).
See full target information DPP8
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Frontiers in oncology 11:714527 PubMed34490111

2021

Fluorescence Imaging Using Enzyme-Activatable Probes for Real-Time Identification of Pancreatic Cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Ryugen Takahashi,Takeaki Ishizawa,Masumitsu Sato,Yoshinori Inagaki,Mariko Takanka,Yugo Kuriki,Mako Kamiya,Tetsuo Ushiku,Yasuteru Urano,Kiyoshi Hasegawa
View all publications
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