Analytical Data
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Gene name
PGM5
- Application
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Alternative Names
PGM5；PGMRP；Phosphoglucomutase-like Protein 5
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15124
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Expression Region
1-567aa
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AA Sequence
MEGSPIPVLT VPTAPYEDQR PAGGGGLRRP TGLFEGQRNY LPNFIQSVLS SIDLRDRQGC TMVVGSDGRY FSRTAIEIVV QMAAANGIGR LIIGQNGILS TPAVSCIIRK IKAAGGIILT ASHCPGGPGG EFGVKFNVAN GGPAPDVVSD KIYQISKTIE EYAICPDLRI DLSRLGRQEF DLENKFKPFR VEIVDPVDIY LNLLRTIFDF HAIKGLLTGP SQLKIRIDAM HGVMGPYVRK VLCDELGAPA NSAINCVPLE DFGGQHPDPN LTYATTLLEA MKGGEYGFGA AFDADGDRYM ILGQNGFFVS PSDSLAIIAA NLSCIPYFRQ MGVRGFGRSM PTSMALDRVA KSMKVPVYET PAGWRFFSNL MDSGRCNLCG EESFGTGSDH LREKDGLWAV LVWLSIIAAR KQSVEEIVRD HWAKFGRHYY CRFDYEGLDP KTTYYIMRDL EALVTDKSFI GQQFAVGSHV YSVAKTDSFE YVDPVDGTVT KKQGLRIIFS DASRLIFRLS SSSGVRATLR LYAESYERDP SGHDQEPQAV LSPLIAIALK ISQIHERTGR RGPTVIT
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
PGM5, or phosphoglycerate mutase 5, is an enzyme that plays a significant role in the regulation of glycolysis and energy metabolism. As a member of the phosphoglycerate mutase family, PGM5 is involved in catalyzing the interconversion of 2-phosphoglycerate and 3-phosphoglycerate, crucial intermediates in the glycolytic pathway. Research into PGM5 has gained traction due to its potential implications in various biological processes, including cellular energy production, growth, and differentiation. Furthermore, Dysregulation of glycolysis has been linked to several disease states, including cancer, wherein tumor cells often exhibit altered metabolic pathways to sustain rapid proliferation. Understanding the structure and function of PGM5 through recombinant protein studies can provide insights into its enzymatic mechanisms, tissue-specific expression patterns, and functional regulation. Additionally, the study of PGM5 may unveil novel therapeutic targets for metabolic disorders and cancer treatment, highlighting the necessity for in-depth research into its properties and biological significance. By utilizing advanced techniques such as recombinant DNA technology, researchers aim to produce functional PGM5 proteins for further investigation, ultimately contributing to the ever-expanding knowledge of cellular metabolism and its role in health and disease.
