Biotinylated Recombinant Human Gasdermin-D (GSDMD) Protein (MBP&His-Avi)

Name: Biotinylated Recombinant Human Gasdermin-D (GSDMD) Protein (MBP&His-Avi)
Brand: Beta LifeScience
SKU: BLC-06574P
Price: 815.2 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Avi-tagged proteins, Biotinylated proteins, Featured biotinylated protein molecules, Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Biotinylated Recombinant Human Gasdermin-D (GSDMD) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P57764
Target Symbol	GSDMD
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-MBP&C-6His-Avi
Target Protein Sequence	MGSAFERVVRRVVQELDHGGEFIPVTSLQSSTGFQPYCLVVRKPSSSWFWKPRYKCVNLSIKDILEPDAAEPDVQRGRSFHFYDAMDGQIQGSVELAAPGQAKIAGGAAVSDSSSTSMNVYSLSVDPNTWQTLLHERHLRQPEHKVLQQLRSRGDNVYVVTEVLQTQKEVEVTRTHKREGSGRFSLPGATCLQGEGQGHLSQKKTVTIPSGSTLAFRVAQLVIDSDLDVLLFPDKKQRTFQPPATGHKRSTSEGAWPQLPSGLSMMRCLHNFLTDGVPAEGAFTEDFQGLRAEVETISKELELLDRELCQLLLEGLEGVLRDQLALRALEEALEQGQSLGPVEPLDGPAGAVLECLVLSSGMLVPELAIPVVYLLGALTMLSETQHKLLAEALESQTLLGPLELVGSLLEQSAPWQERSTMSLPPGLLGNSWGEGAPAWVLLDECGLELGEDTPHVCWEPQAQGRMCALYASLALLSGLSQEPH
Expression Range	1-484aa
Protein Length	Full Length
Mol. Weight	100.6 kDa
Research Area	Cell Biology
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	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.
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
Database References	HGNC: 25697 OMIM: 617042 KEGG: hsa:79792 STRING: 9606.ENSP00000262580 UniGene: Hs.118983
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.

Gene Functions References

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

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.