Analytical Data
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Gene name
ZMYND10
- Application
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Alternative Names
ZMYND10; BLU; LUCA12.4; Zinc finger MYND domain-containing Protein 10; Protein BLu
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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
O75800
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Expression Region
1-440 aa
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AA Sequence
MGDLELLLPG EAEVLVRGLR SFPLREMGSE GWNQQHENLE KLNMQAILDA TVSQGEPIQE LLVTHGKVPT LVEELIAVEM WKQKVFPVFC RVEDFKPQNT FPIYMVVHHE ASIINLLETV FFHKEVCESA EDTVLDLVDY CHRKLTLLVA QSGCGGPPEG EGSQDSNPMQ ELQKQAELME FEIALKALSV LRYITDCVDS LSLSTLSRML STHNLPCLLV ELLEHSPWSR REGGKLQQFE GSRWHTVAPS EQQKLSKLDG QVWIALYNLL LSPEAQARYC LTSFAKGRLL KLRAFLTDTL LDQLPNLAHL QSFLAHLTLT ETQPPKKDLV LEQIPEIWER LERENRGKWQ AIAKHQLQHV FSPSEQDLRL QARRWAETYR LDVLEAVAPE RPRCAYCSAE ASKRCSRCQN EWYCCRECQV KHWEKHGKTC VLAAQGDRAK
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Molecular Weight
50.3 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
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Protein Description
ZMYND10 (Zinc Finger MYND Domain Containing 10) is a protein that has garnered attention in recent years due to its involvement in various biological processes and potential implications in disease. This protein is characterized by the presence of zinc finger domains, which are known to facilitate protein-protein interactions and play crucial roles in regulating gene expression. Research has indicated that ZMYND10 may function as a co-regulator of transcription, influencing pathways related to cell proliferation and differentiation. Moreover, studies have linked ZMYND10 to cancer biology, suggesting that dysregulation of its expression could contribute to tumorigenesis. Notably, ZMYND10 has also been implicated in immune responses and may have a role in the regulation of inflammatory processes. Given its multifaceted roles, the study of ZMYND10 is critical for understanding both normal cellular function and the molecular mechanisms underlying various diseases, particularly cancer. As a result, the generation of recombinant ZMYND10 protein has become essential for further investigations into its structure, function, and potential as a therapeutic target. This research aims to elucidate the precise mechanisms through which ZMYND10 exerts its effects in the cell, ultimately advancing our knowledge of its role in health and disease.
