Recombinant Human GAPDH Protein (His Tag)

Name: Recombinant Human GAPDH Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2199
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Human
Accession	P04406
Synonym	G3PD, GAPD, HEL-S-162eP
Background	Glyceraldehyde 3-phosphate dehydrogenase (GAPDH or G3PDH) is an enzyme of about 37kDa that is consisdered as a cellular enzyme involved in glycolysis. It catelyzes the sixth step of glycolysis. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a pleiotropic enzyme that is overexpressed in apoptosis and in several human chronic pathologies. Its role as a mediator for cell death has also been highlighted. A recent report suggests that GAPDH may be genetically associated with late-onset of Alzheimer's disease. Besides, deprenyl, which has originally been used as a monoamine oxidase inhibitor for Parkinson's disease, binds to GAPDH and displays neuroprotective actions.
Description	A DNA sequence encoding the human GAPDH (P04406) (Met 1-Glu 335) was expressed, with a His tag at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Met 1-Glu 335
Molecular Weight	The recombinant human GAPDH comprises 346 a.a. and migrates as an approximately 38 kDa band in SDS-PAGE under reducing conditions as predicted.
Purity	>93% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 50mM Tris, 30% glycerol, pH 7.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC.
Subcellular Location	Cytoplasm, cytosol. Nucleus. Cytoplasm, perinuclear region. Membrane. Cytoplasm, cytoskeleton.
Protein Families	Glyceraldehyde-3-phosphate dehydrogenase family
Database References	HGNC: 4141 OMIM: 138400 KEGG: hsa:2597 STRING: 9606.ENSP00000229239 UniGene: Hs.544577

Gene Functions References

This suggests that RX624 might be useful as a drug against polyglutamine pathologies, and that is could be administered exogenously without affecting target cell physiology. This protective effect was validated by the similar effect of an anti-GAPDH specific antibody. PMID: 28450110
GAPDH can interact with proteins participating in DNA repair, such as APE1, PARP1, HMGB1, and HMGB2. In this review, the functions of GAPDH associated with DNA repair are discussed in detail. PMID: 28601074
Nitric oxide-induced GAPDH aggregation specifically induces mitochondrial dysfunction via permeability transition pore opening, leading to cell death. PMID: 28167533
GAPDH may act as a chaperone in heme transfer to downstream areas PMID: 28315300
NAD(+) inhibited both GAPDH aggregation and co-aggregation with GOSPEL, a hitherto undescribed effect of the coenzyme against the consequences of oxidative stress. PMID: 27282776
Monoclonal Antibodies DSHB-hGAPDH-2G7 and DSHB-hGAPDH-4B7 Against Human Glyceraldehyde-3-Phosphate Dehydrogenase. PMID: 27556912
the present study suggests that GAPDH plays an important role in cancer metastasis by affecting EMT through regulation of Sp1-mediated SNAIL expression. PMID: 27878251
Knockdown of LAMP2A, a CMA-related protein, and TSG101, an mA-related protein, significantly but only partially decreased the punctate accumulation of GAPDH-HT in AD293 cells and primary cultured rat cortical neurons. PMID: 27377049
In conclusion, the data show that two GAPDH binders could be therapeutically relevant in the treatment of injuries stemming from hard oxidative stress. PMID: 26748070
transient silencing of GAPDH reduces intracellular ROS and facilitates increased autophagy, thereby reducing acute hypoxia and reoxygenation injury as well as the resulting apoptosis and necrosis. PMID: 26279122
This review will summarize our current understanding of GAPDH-mediated regulation of RNA function PMID: 26564736
analysis of PSCA level in the peripheral blood of PC patients who underwent radical prostatectomy shows it is related to a GADPH reference level (PSCA/GAPDH ratio) PMID: 26527100
In 60 % of patients with type 2 diabetes, a reversible inhibition of GAPDH is observed. PMID: 25189828
The results of this study led us to conclude that in cancer cells constantly exposed to conditions of oxidative stress, the protective power of Hsp70 should be abolished by specific inhibitors of Hsp70 expression. PMID: 26713364
GAPDH and protoporphyrinogen oxidase were shown to have higher expression in faster growing cell lines and primary tumors. Pharmacologic inhibition of GAPDH or PPOX reduced the growth of colon cancer cells in vitro PMID: 25944804
The levels of GAPDH protein were significantly up-regulated in lung squamous cell carcinoma tissues and elevated GAPDH expression is associated with the proliferation and invasion of lung and esophageal squamous cell carcinomas. PMID: 25944651
Genetic variants in GAPDH confer susceptibility to sporadic Parkinson's disease in a Chinese Han population. PMID: 26258539
Data revealed that GAPDH is a phosphorylation substrate for AMPK and its interaction with Sirt1 in the nucleus. The phosphorylation and the nuclear translocation of GAPDH mediate rapid Sirt1 activation and autophagy initiation under glucose deprivation. PMID: 26626483
findings demonstrate that dissociation of the GAPDH/Siah1 pro-apoptotic complex can block high glucose-induced pericyte apoptosis, widely considered a hallmark feature of diabetic retinopathy PMID: 26438826
Extracellular GAPDH, or its N-terminal domain, inhibited gastric cancer cell growth. GAPDH bound to E-cadherin and downregulated the mTOR-p70S6 kinase pathway. PMID: 25785838
suggests that GAPDH aggregates accelerate Abeta amyloidogenesis, subsequently leading to mitochondrial dysfunction and neuronal cell death in the pathogenesis of AD PMID: 26359500
The level of GAPDH-AP DNA adduct formation depends on oxidation of the protein SH-groups; disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA PMID: 26203648
The activity of GAPDS was significantly positively correlated with sperm motility and negatively with the incidence of infertility. PMID: 26255202
The N terminus of nuclear GAPDH binds with PARP-1, and this complex promotes PARP-1 overactivation both in vitro and in vivo. PMID: 25882840
deregulated GAPDH expression promotes NF-kappaB-dependent induction of HIF-1alpha and has a key role in lymphoma vascularization and aggressiveness PMID: 25394713
analysis of how flux through GAPDH is a limiting step in aerobic glycolysis PMID: 25009227
astrocytic production of D-serine is modulated by glycolytic activity via interactions between GAPDH and SRR. PMID: 25870284
Dimer and tetramer interface residues in adenine-uridine rich elements are important for GAPDH-RNA binding. PMID: 25451934
Siah1 is a substrate of ASK1 for activation of the GAPDH-Siah1 oxidative stress signaling cascade. PMID: 25391652
GAPDH expression is deregulated during melanoma progression. PMID: 25550585
Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase. PMID: 25086035
MZF-1 binds to and positively regulates the GAPDH promoter, indicating a role for GAPDH in calcitriol-mediated signaling. PMID: 25065746
The protein encoded by this gene contains a peptide that displays antimicrobial activity against E. coli, P. aeruginosa, and C. albicans. PMID: 22832495
GAPDH gene over expression in resected tumor samples is an adverse prognostic factor in non small cell lung cancer. PMID: 23988223
This review describes the structure and localization of GAPDH in cells as well as the latest discoveries on the multifunctional properties of the enzyme. PMID: 24018444
TG2-dependent GAPDH deamidation was suggested to participate in actin cytoskeletal remodeling. PMID: 24375405
acetylation of GAPDH (K254) is reversibly regulated by the acetyltransferase PCAF and the deacetylase HDAC5. PMID: 24362262
GAPDH binds to active Akt, leading to Bcl-xL increase and escape from caspase-independent cell death. PMID: 23645209
GAPDH is a moonlighting protein that functions as a glycolytic enzyme as well as a uracil DNA glycosylase. PMID: 20727968
Results indicate that CIB1 is uniquely positioned to regulate PI3K/AKT and MEK/ERK signaling and that simultaneous disruption of these pathways synergistically induces a nuclear GAPDH-dependent cell death. PMID: 22964641
The data presented demonstrate that up-regulation of GAPDH positively associated genes is proportional to the malignant stage of various tumors and is associated with an unfavourable prognosis. PMID: 23620736
In a yeast two-hybrid screen of a heart cDNA library with Mst1 as bait, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was identified as an Mst1-interacting protein. PMID: 23527007
interaction between prolyl oligopeptidase and glyceraldehyde-3-phosphate dehydrogenase is required for cytosine arabinoside-induced glyceraldehyde-3-phosphate dehydrogenase nuclear translocation and cell death PMID: 23348613
NleB, a bacterial glycosyltransferase, targets GAPDH function to inhibit NF-kappaB activation. PMID: 23332158
GAPDH binds to alkylated, single-stranded, double-stranded and telomeric sequences in a drug-dependent and DNA sequence/structure-dependent manner. PMID: 23409959
GAPDH negatively regulates HIV-1 infection and provide insights into a novel function of GAPDH in the HIV-1 life cycle and a new host defense mechanism against HIV-1 infection. PMID: 23237566
The strength, selectivity, reversibility, and redox sensitivity of heme binding to GAPDH are consistent with it performing heme sensing or heme chaperone-like functions in cells. PMID: 22957700
The ability of C1q to sense both human and bacterial GAPDHs sheds new insights on the role of this important defense collagen molecule in modulating the immune response. PMID: 23086952
SIRT1 functions to retain GAPDH in the cytosol, protecting the enzyme from nuclear translocation via interaction with these two proteins. PMID: 22789853
The present mini review summarizes recent findings relating to the extraglycolytic functions of GAPDH and highlights the significant role this enzyme plays in regulating both cell survival and apoptotic death--{REVIEW} PMID: 21895736

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.