Recombinant Mouse Glutamate Decarboxylase 2 (GAD2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-09990P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Gad2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Gad2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Gad2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Gad2.

Recombinant Mouse Glutamate Decarboxylase 2 (GAD2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-09990P
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Product Overview

Description Recombinant Mouse Glutamate Decarboxylase 2 (GAD2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P48320
Target Symbol GAD2
Synonyms Gad2; Gad65Glutamate decarboxylase 2; EC 4.1.1.15; 65 kDa glutamic acid decarboxylase; GAD-65; Glutamate decarboxylase 65 kDa isoform
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence MASPGSGFWSFGSEDGSADPENPGTARAWCQVAQKFTGGIGNKLCALLYGDSGKPAEGGGSVTSRAATGKVACTCDQKPCNCPKGDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILTHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMLIARYKMFPEVKEKGMAAVPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEVKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHIDKCLELAEYLYTIIKNREGYEMVFDGKPQHTNVCFWFVPPSLRTLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
Expression Range 1-585aa
Protein Length Full Length
Mol. Weight 69.2kDa
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 Catalyzes the production of GABA.
Subcellular Location Cytoplasm, cytosol. Cytoplasmic vesicle. Cell junction, synapse, presynaptic cell membrane; Lipid-anchor. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families Group II decarboxylase family
Database References

Gene Functions References

  1. These results thus identify a molecularly distinct, orexin-activated lateral hypothalamus submodule that governs physical activity in mice. PMID: 28396414
  2. Increased activity due to bicuculline preferentially up-regulated GAD65. This was reduced by AP5, a selective blocker of Ca2+-permeable ion channels and NMDA-Rs, and by U0126, KN93, and K252a, affecting BDNF pathways. PMID: 26241953
  3. Data show that miRNAs are involved in regulating the expression of the major type 1 diabetes (T1D) autoantigens IA-2, IA-2beta, and GAD65 enzyme. PMID: 26148972
  4. Results show that GAD65 is required for efficient GABAergic synaptic transmission and plasticity, and for maintaining extracellular GABA at a level needed for associative plasticity at cortical inputs in the lateral amygdala PMID: 24663011
  5. Menin regulates spinal glutamate-GABA balance through GAD65 contributing to neuropathic pain. PMID: 24905306
  6. Our data suggest a role of GAD65-mediated GABA synthesis in the encoding of circadian information to fear memory PMID: 24300892
  7. Autoimmunity to GAD65 may play a role in the development of Stiff person syndrome. PMID: 24058450
  8. Prenatal and postnatal maternal effects influence GAD65 and GAD67 gene expression depending on the age of the offspring. PMID: 23876745
  9. These findings indicate novel, differential roles for GluN2A, B and D receptors and for GAD65-mediated GABA in the regulation of individual topographies of orofacial movement PMID: 23892010
  10. SMAR1 and p53 act synergistically to up-regulate GAD65 expression upon Streptozotocin treatment. PMID: 22978699
  11. Data show that chronic pain epigenetically suppresses Gad2 transcription through histone deacetylase-mediated histone hypoacetylation, resulting in impaired gamma-aminobutyric acid synaptic inhibition. PMID: 21983856
  12. These results suggest that modulation of the synaptic transmission from primary afferents to SG neurons by group III mGluR agonist is specific to the type of nociceptive primary afferents but not to the type of target neurons. PMID: 21177998
  13. GAD65 is crucial for maintenance of biosynthesis of synaptic GABA particularly by direct synthesis from astrocytic glutamine via glutamate. PMID: 20664610
  14. An impaired tonic inhibition in GAD65-deficient mice is revealed demonstrating a significant role of GAD65 in the synthesis of GABA acting extrasynaptically. PMID: 21039523
  15. Mice possessing a monoclonal GAD65-specific CD4-positive T cell population develop a lethal encephalomyelitis-like disease in the absence of any other T cells or B cells. PMID: 20348424
  16. Deletion of Gad2 reduced the effect of flurazepam on motor incoordination and increased the effect of extrasynaptic GABAA receptor agonist gabaxadol without changing the duration of loss of righting reflex produced by these drugs. PMID: 20002022
  17. GAD65 plays an important role in regulating fear responses during extinction of cued but apparently not contextual fear. PMID: 20016086
  18. Absence of long-term depression in the visual cortex of GAD65 knock-out mice PMID: 12097476
  19. CD4+ T cells from glutamic acid decarboxylase (GAD)65-specific T cell receptor transgenic mice are not diabetogenic and can delay diabetes transfer PMID: 12186840
  20. Induction of autoimmune diabetes through insulin (but not this enzyme)DNA vaccination in NOD mice PMID: 12401715
  21. No significant GAD65 gene expression differences are detected in either drug-naive or acute ethanol withdrawn mouse brain. PMID: 12691782
  22. Results indicate that glutamic acid decarboxylase (GAD65) is not an essential autoantigen in the pathogenesis of diabetes. PMID: 12796471
  23. Selectively altered behavioral fear response in GAD65 deficient mice, most likely due to deficits in threat estimation or elicitation of appropriate conditioned fear behavior. GAD65 is a genetic determinant of conditioned fear behavior. PMID: 12884963
  24. The cumulative incidence of autoimmune diabetes was found not to be influenced by GAD65 deficiency in NOD mice. PMID: 14676944
  25. These results suggest that GAD65-generated GABA is implicated more complex processing of taste information including taste mixtures and palatability may be finely tuned by GAD65-mediated GABA synthesis. PMID: 15036622
  26. GAD65 knockout mice showed robust deficits in prepulse inhibition which were reversed by the atypical antipsychotic agent clozapine PMID: 15114343
  27. Similar to the rat at P5, mice at P6 are unable to sustain an increase in CO2 induced respiratory frequency and GAD65 contributes to this fall off. PMID: 15134589
  28. P boutons can be distinguished from other GABAergic terminals in the ventral horn of rat and mouse spinal cord by their high level of the glutamic acid decarboxylase (GAD) 65 isoform of GAD. PMID: 15947074
  29. lack of gad65 impairs the function of the respiratory network in mouse fetuses and the impairment progresses with fetal age PMID: 17418495
  30. GAD65 plays a major role in GABA transmission in normal physiological condition. PMID: 17482148
  31. GAD65-mediated GABA synthesis is critical for the consolidation of stimulus-specific fear memory PMID: 18323571
  32. anti-whole GAD65-reactive T cells have the ability to regulate the development of type 1 diabetes PMID: 19188044
  33. There are reduced NMDA NR2A levels and slower NMDA currents in visual cortex of GAD65 knockout mice PMID: 19406876
  34. study found that the number of somatic GAD65-puncta on individual layer 2/3 pyramidal neurons is reduced when mice are dark-reared from birth and reverted to normal levels by re-exposure to light PMID: 19503840
  35. GAD65-mediated gamma-aminobutyric acid (GABA) synthesis plays relatively small but significant roles in nociceptive processing via supraspinal mechanisms. PMID: 19571163
  36. MHC class I-restricted responses to GAD65 provide an inflammatory focus for the generation of islet-specific pathogenesis and beta cell destruction, as well as a therapeutic role for GAD65 peptide determinants in type I diabetes. PMID: 11466400

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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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