Recombinant Human Gamma-Glutamyl Hydrolase (GGH) Protein (His-GST&Myc)

Name: Recombinant Human Gamma-Glutamyl Hydrolase (GGH) Protein (His-GST&Myc)
Brand: Beta LifeScience
SKU: BLC-07400P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Gamma-Glutamyl Hydrolase (GGH) Protein (His-GST&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q92820
Target Symbol	GGH
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-GST&C-Myc
Target Protein Sequence	TNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEE
Expression Range	219-293aa
Protein Length	Partial
Mol. Weight	43.9 kDa
Research Area	Metabolism
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	Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates.
Subcellular Location	Secreted, extracellular space. Lysosome. Melanosome.
Protein Families	Peptidase C26 family
Database References	HGNC: 4248 OMIM: 601509 KEGG: hsa:8836 STRING: 9606.ENSP00000260118 UniGene: PMID: 28278270 the results of our study identify GGH as an ERG subtype specific molecular marker with modest prognostic relevance, which may have clinical relevance if analyzed in combination with other molecular markers. PMID: 28146062 the highest expression of GGH and EGFR was noted in the left-sided colon; the highest expression of DHFR, FPGS, TOP1 and ERCC1 was noted in the rectosigmoid, whereas TYMP expression was approximately equivalent in the right-sided colon and rectum PMID: 26676887 This study shows that polymorphisms on genes related to the metabolic pathway of pemetrexed, especially, ATIC and GGH genes, would have a therapeutic implication in pemetrexed-treated patients with lung adenocarcinoma PMID: 25823786 Polymorphism of GGH rs3758149 C>T is associated with response to therapy in acute lymphoblastic leukemia. PMID: 24908438 An interaction term, between FPGS rs7033913 heterozygotes and GGH rs11988534 homozygotes for the minor allele, had a p-value <0.0001 and may contribute to metotrexate toxicity in rheumatoid arthritis. PMID: 24447348 GG genotype of GGH -354 T > G polymorphism may have high predictive value for myelosuppression in methotrexate treated rheumatoid arthritis patients. PMID: 22763757 Suggest that GGH may serve as a potential biomarker of unfavorable clinical outcomes over short-term follow-up in breast cancer. PMID: 23374458 Genotyping of DHFR 829C>T and GGH -401C>T was performed using a polymerase chain reaction. PMID: 22994778 The results of our study suggested the potential interest of GGH -401C>T as a predictive factor of the outcome of cervical carcinoma treated with cisplatin-based chemoradiotherapy. PMID: 23107767 There was no significant difference in gamma-glutamyl hydrolase genotype or T allele frequency between the two groups (P> 0.05). PMID: 22678806 Genetic polymorphism of gamma-glutamyl hydrolase in Chinese acute leukemia children and identification of a novel double nonsynonymous mutation. PMID: 22568793 a SNP in the GGH gene remained associated with reduced CVD risk, with a stronger association in early onset CVD cases. PMID: 22649255 This is one of the first studies to assess FPGS and GGH genetic variants in relation to plasma homocysteine. PMID: 22018726 Genotypes in GGH gene of acute lymphoblastic leukemia patients were evaluated PMID: 21538980 The -401C/T polymorphism in the gamma-glutamyl hydrolase may be a factor involved in the generation of relapse to disease in patients with acute lymphoblastic leukemia. PMID: 20197200 Data revealed that high FPGS gene expression, low GGH gene expression and low ABCC1 gene expression in CRC tissues were predictive factors for a high reduced folate level after LV administration. PMID: 19636555 data implicate GGH as a novel biomarker for bladder cancer; suggest presence of GGH & diazepam-binding inhibitor in urine serves as a rationale for developing them as urinary markers of clinical outcomes for patients treated with neoadjuvant chemotherapy PMID: 19815704 Three-dimensional structure PMID: 11953431 cDNA microarray analysis led to the identification of 2 novel biomarkers that should facilitate molecular diagnosis and further study of pulmonary neuroendocrine tumors. PMID: 15492986 lack of dissociation of the dimer, large monomer-monomer interface, & presence of catalytically essential Tyr-36 in the homodimer interface sequences suggest that homodimer formation is required for hGH monomer to fold into an active conformation. PMID: 16945597 The genotype distribution and gene frequency of the GGH gene polymorphism was studied in a Japanese population. PMID: 17409534 CpG island methylator phenotype (CIMP+) in ColoRectal Cancer (CRC) is associated with low expression of GGH, suggesting involvement of the folate pathway in the development of this phenotype. PMID: 18414409

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.