Recombinant Human Gasdermin-D (GSDMD)

Baculovirus
Mammalian cell

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

GSDMD

Uniprot NO.

P57764

Alternative Names

C-terminal; Gasdermin domain-containing protein 1; Gasdermin-D; GSDMD; GSDMD-CT; GSDMD-NT; GSDMD_HUMAN

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

1-484

Target Protein Sequence

MGSAFERVVR RVVQELDHGG EFIPVTSLQS STGFQPYCLV VRKPSSSWFW KPRYKCVNLS IKDILEPDAA EPDVQRGRSF HFYDAMDGQI QGSVELAAPG QAKIAGGAAV SDSSSTSMNV YSLSVDPNTW QTLLHERHLR QPEHKVLQQL RSRGDNVYVV TEVLQTQKEV EVTRTHKREG SGRFSLPGAT CLQGEGQGHL SQKKTVTIPS GSTLAFRVAQ LVIDSDLDVL LFPDKKQRTF QPPATGHKRS TSEGAWPQLP SGLSMMRCLH NFLTDGVPAE GAFTEDFQGL RAEVETISKE LELLDRELCQ LLLEGLEGVL RDQLALRALE EALEQGQSLG PVEPLDGPAG AVLECLVLSS GMLVPELAIP VVYLLGALTM LSETQHKLLA EALESQTLLG PLELVGSLLE QSAPWQERST MSLPPGLLGN SWGEGAPAWV LLDECGLELG EDTPHVCWEP QAQGRMCALY ASLALLSGLS QEPH
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Full length protein

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 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.

Customer Reviews and Q&A

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■ Q&A

Please let me know if you can provide Gasdermin D Protein (GSDMD) for human. If so, please send the product datasheets and pricing information.

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Recombinant Human Gasdermin-D(GSDMD)
CSB-YP009956HU >> Yeast
CSB-EP009956HU >> E.coli
CSB-BP009956HU >> Baculovirus
CSB-MP009956HU >> Mammalian cell
Expression region: 1-484aa; Full length.
Tag information: EP, BP, MP: N-terminal 10xHis-tagged and C-terminal Myc-tagged; YP: N-terminal 6xHis-tagged
Sequence:

Target Background

Function(From Uniprot)

Precursor of a pore-forming protein that plays a key role in host defense against pathogen infection and danger signals. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-D, N-terminal) binds to membranes and forms pores, triggering pyroptosis.; Promotes pyroptosis in response to microbial infection and danger signals. Produced by the cleavage of gasdermin-D by inflammatory caspases CASP1, CASP4 or CASP5 in response to canonical, as well as non-canonical (such as cytosolic LPS) inflammasome activators. After cleavage, moves to the plasma membrane where it strongly binds to inner leaflet lipids, including monophosphorylated phosphatidylinositols, such as phosphatidylinositol 4-phosphate, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-bisphosphate, and more weakly to phosphatidic acid and phosphatidylserine. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature IL1B and triggering pyroptosis. Exhibits bactericidal activity. Gasdermin-D, N-terminal released from pyroptotic cells into the extracellular milieu rapidly binds to and kills both Gram-negative and Gram-positive bacteria, without harming neighboring mammalian cells, as it does not disrupt the plasma membrane from the outside due to lipid-binding specificity. Under cell culture conditions, also active against intracellular bacteria, such as Listeria monocytogenes. Also active in response to MAP3K7/TAK1 inactivation by Yersinia toxin YopJ, which triggers cleavage by CASP8 and subsequent activation. Strongly binds to bacterial and mitochondrial lipids, including cardiolipin. Does not bind to unphosphorylated phosphatidylinositol, phosphatidylethanolamine nor phosphatidylcholine.

Gene References into Functions

lncRNA RP185F18.6 and DeltaNp63 may be considered unfavorable biomarkers, whereas GSDMD may be a favorable biomarker in colorectal cancer (CRC) ; these markers may prove valuable in the future diagnosis and prognosis of CRC PMID:30226619
High GSDMD expression is associated with tumor-node-metastasis in nonsmall cell lung cancer. PMID:30106450
the gasdermin-D pore: Executor of pyroptotic cell death PMID:27557502
Results implicate pyroptosis induced by the CASP11/4-GSDMD pathway in the pathogenesis of alcoholic hepatitis PMID:29108122
The present study not only contributes to our understanding of GSDMD recognition by inflammatory caspases but also reports a specific inhibitor for these caspases that can serve as a tool for investigating inflammasome signaling. PMID:29891674
Pyroptosis regulator gasdermin D was necessary for IL-1beta secretion from living macrophages that have been exposed to inflammasome activators, such as bacteria and their products or host-derived oxidized lipids PMID:29195811
These findings reveal that GSDMD-C acts as an auto-inhibition executor and GSDMD-N could form pore structures via a charge-charge interaction upon cleavage by caspases during cell pyroptosis. PMID:28928145
This study reveals the pore-forming activity of GSDMD and channel-forming activity of MLKL determine different ways of plasma membrane rupture in pyroptosis and necroptosis. PMID:27573174
GsdmD p30 kills cells by forming pores that compromise the integrity of the cell membrane. PMID:27339137
Data, including data from studies using recombinant fusion forms of GSDMD, suggest that GSDMD participates in inflammasome-dependent pyroptosis of macrophages in response to various stimuli; this mechanism involves proteolysis of GSDMD by caspase-1 and caspase-11. PMID:28726636
Remarkably, the Enterovirus 71 protease 3C directly targets GSDMD and induces its cleavage, which is dependent on the protease activity. PMID:28679757
The pyroptosis is redefined as gasdermin D-mediated programmed necrosis. Gasdermin D are associated with various genetic diseases, and their cellular function and mechanism of activation. PMID:27932073
Overall, these data demonstrate that GSDMD is the direct and final executor of pyroptotic cell death. PMID:27418190
Studies show that the membrane-pores composed of gasdermin D-N domains (GSDMD-N domain) are required for pyroptosis. PMID:27460194
Studies indicate that gasdermin D (GSDMD) is cleaved by the activated caspases-1/4/5/11 between its N-terminal and C-terminal domains. PMID:27604419
Gene deletion of GSDMD demonstrated that GSDMD is required for pyroptosis and for the secretion but not proteolytic maturation of IL-1beta in both canonical and non-canonical inflammasome responses. PMID:26611636
GSDMD N-terminal cleavage product oligomerizes in membranes to form pores that are visible by electron microscopy PMID:27383986
caspase-1 and caspase-4/5/11 specifically cleaved the linker between the amino-terminal gasdermin-N and carboxy-terminal gasdermin-C domains in GSDMD, which was required and sufficient for pyroptosis PMID:26375003

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Subcellular Location

[Gasdermin-D]: Cytoplasm, cytosol. Inflammasome.; [Gasdermin-D, N-terminal]: Cell membrane; Multi-pass membrane protein. Secreted.; [Gasdermin-D, C-terminal]: Cytoplasm, cytosol.

Protein Families

Gasdermin family

Tissue Specificity

Expressed in the suprabasal cells of esophagus, as well as in the isthmus/neck, pit, and gland of the stomach, suggesting preferential expression in differentiating cells.

Database Links

HGNC: 25697

UNIGENE: Hs.118983

KEGG: hsa:79792

STRING: 9606.ENSP00000262580

OMIM: 617042

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