Recombinant Mouse Gasdermin-A3 (GSDMA3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00675P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Gasdermin-A3 (GSDMA3) Protein (His)

Beta LifeScience SKU/CAT #: BLC-00675P
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Product Overview

Description Recombinant Mouse Gasdermin-A3 (GSDMA3) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q5Y4Y6
Target Symbol GSDMA3
Synonyms (Gasdermin-3)(GSDMA3-NT)(GSDMA3-CT)
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence MHEDFKTLKEEVQRETQEVEKLSPVGRSSLLTSLSHLLGKKKELQDLEQKLEGALDKGQKVTLEALPKDVLLSKDAMDAILYFLGALTELTEEQLKILVKSLEKKILPVQLKLVESTLEQNFLQDKEGVFPLQPDLLSSLGEEELTLTEALVGLSGLEVQRSGPQYAWDPDTRHNLCALYAGLSLLHLLSRKSNALTYCALS
Expression Range 263-464aa
Protein Length Partial
Mol. Weight 26.6 kDa
Research Area Others
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 involved in the transition from catagen to telogen at the end of hair follicle morphogenesis. This form constitutes the precursor of the pore: upon cleavage, the released N-terminal moiety (Gasdermin-A3, N-terminal) binds to membranes and forms pores, triggering cell death.; Pore-forming protein that causes membrane permeabilization and pyroptosis. Released upon cleavage in vitro of genetically engineered Gsdma3, and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis. Binds to membrane inner leaflet lipids, including bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-bisphosphate, and more weakly to monophosphorylated phosphatidylinositols. Also binds to bacterial and mitochondrial lipids, including cardiolipin, and exhibits bactericidal activity. The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown (Probable). Plays a role in the transition from catagen to telogen at the end of hair follicle morphogenesis, possibly by regulating hair follicle stem cell niche maintenance. Also required for mammary gland development.
Subcellular Location [Gasdermin-A3]: Cytoplasm, cytosol.; [Gasdermin-A3, N-terminal]: Cell membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein.
Protein Families Gasdermin family
Database References

KEGG: mmu:450219

UniGene: PMID: 29695864

  • In this study, we describe a novel mutation (C+/H-: cornea plus, hair minus) in the far C-terminal region of Gasdermin A3 that causes both skin and corneal phenotypes. PMID: 29372254
  • The function of Gsdma3 in regulating the development of mammary glands, and it demonstratse that the Gsdma3 gene may act as a suppressor of the immune reaction. PMID: 28168650
  • induced expression caused epidermal hyperplasia, skin inflammation and hair cycle defect, suggesting gain-of-function mutations PMID: 26173759
  • crystal structure of GSDMA3 showed an autoinhibited two-domain architecture that is conserved in the gasdermin family; the gasdermin-N domain is required for pyroptosis PMID: 27281216
  • Our results indicate that the genetic mutations in the C-terminal domain of Gsdma3 are gain-of-function mutations which unmask the N-terminal functional domain of Gsdma3 PMID: 26100518
  • GSDMA3 mutation play a specific role in hair growth in alopecia. PMID: 25860385
  • Loss of conserved Gsdma3 self-regulation causes autophagy and cell death. PMID: 25825937
  • The Gsdma3 may play a role in the proliferation and differentiation of epidermal cells and hair follicles through negatively regulating beta-catenin expression. PMID: 22694914
  • in mouse skin keratinocytes, Gsdma3 expression could be regulated by TNF-alpha. PMID: 22585037
  • Gsdma3(I359N) is a novel ENU-induced mutant mouse line for studying the function of Gasdermin A3 in the hair follicle and epidermis PMID: 22682752
  • The results demonstrate that Gsdma3 causes immune-mediated destruction of bulge stem cells plays a crucial role in the pathogenesis of alopecia in AE mice, and this strain might be implicated in other PCAs including lichen planopilaris. PMID: 22155111
  • Gsdma3 gene mutation interfered with catagen formation during mouse hair follicle cycle and, by upregulation of Caspase-3 expression and promotion of apoptosis, Gsdma3 gene could play an essential role in normal catagen induction. PMID: 21805153
  • These results suggest that Gsdma3 is necessary in hair shaft differentiation, and involved in Msx2 regulatory pathway. PMID: 20977888
  • Gsdm3 reflects a mutation hotspot and that Gsdm3 mutations cause alopecia in Rco2, Re(den), and Bsk mice. PMID: 15475261
  • role for gasdermins in differentiation of the epidermis and its appendages. PMID: 15737203
  • These results suggest that Gsdma3 is involved in the proliferation and differentiation of epidermal stem cells. PMID: 17572385

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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.

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