Analytical Data
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Gene name
PCMTD2
- Application
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Alternative Names
PCMTD2; C20orf36; Protein-L-isoaspartate O-methyltransferase domain-containing protein 2
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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
Q9NV79
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Expression Region
2-361 aa
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AA Sequence
GGAVSAGED NDELIDNLKE AQYIRTELVE QAFRAIDRAD YYLEEFKENA YKDLAWKHGN IHLSAPCIYS EVMEALDLQP GLSFLNLGSG TGYLSSMVGL ILGPFGVNHG VELHSDVIEY AKQKLDFFIR TSDSFDKFDF CEPSFVTGNC LEISPDCSQY DRVYCGAGVQ KEHEEYMKNL LKVGGILVMP LEEKLTKITR TGPSAWETKK ILAVSFAPLI QPCHSESGKS RLVQLPPVAV RSLQDLARIA IRGTIKKIIH QETVSKNGNG LKNTPRFKRR RVRRRRMETI VFLDKEVFAS RISNPSDDNS CEDLEEERRE EEEKTPPETK PDPPVNFLRQ KVLSLPLPDP LKYYLLYYRE K
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Molecular Weight
41.0 kDa
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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
Related Products
Protein Description
PCMTD2, or protein-L-isoaspartate O-methyltransferase domain-containing protein 2, is part of a family of enzymes that play crucial roles in protein repair and stabilization, particularly by addressing the detrimental effects of protein damage associated with aging and stress. The study of PCMTD2 has garnered attention due to its potential implications in various pathological conditions, including neurodegenerative diseases and cancer. Research indicates that proteins can undergo modifications leading to misfolding and aggregation, which can impair cellular function. PCMTD2 is believed to counteract these modifications by facilitating the repair of misfolded proteins, thereby enhancing cellular resilience. Investigating PCMTD2's recombinant forms can shed light on its enzymatic mechanisms and interactions with target proteins, offering insights into its role in maintaining proteostasis. Additionally, understanding the structure-function relationship of PCMTD2 could lead to the development of therapeutic strategies aimed at alleviating diseases characterized by protein misfolding and aggregation. Given the increasing incidence of age-related disorders, the exploration of PCMTD2’s functionalities may provide new avenues for drug discovery and the design of novel interventions to combat the effects of protein damage in various diseases.
