Analytical Data
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Gene name
TRIM44
- Application
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Alternative Names
AN3; DIPB; HSA249128; MC7 ; MGC3490; Protein DIPB; TRI44_HUMAN; TRIM44; Tripartite motif containing 44; Tripartite motif containing Protein 44; Tripartite motif-containing Protein 44
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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
Q96DX7
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Expression Region
1-344 aa
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AA Sequence
MASGVGAAFE ELPHDGTCDE CEPDEAPGAE EVCRECGFCY CRRHAEAHRQ KFLSHHLAEY VHGSQAWTPP ADGEGAGKEE AEVKVEQERE IESEAGEESE SEEESESEEE SETEEESEDE SDEESEEDSE EEMEDEQESE AEEDNQEEGE SEAEGETEAE SEFDPEIEME AERVAKRKCP DHGLDLSTYC QEDRQLICVL CPVIGAHQGH QLSTLDEAFE ELRSKDSGGL KAAMIELVER LKFKSSDPKV TRDQMKMFIQ QEFKKVQKVI ADEEQKALHL VDIQEAMATA HVTEILADIQ SHMDRLMTQM AQAKEQLDTS NESAEPKAEG DEEGPSGASE EEDT
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Molecular Weight
38.4 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
TRIM44, a member of the tripartite motif (TRIM) family of proteins, has garnered attention in recent years due to its potential roles in various biological processes, including cell proliferation, apoptosis, and immune response. Previous studies have shown that TRIM44 is involved in the regulation of several signaling pathways, particularly those associated with cancer progression and development. For instance, it has been implicated in promoting cellular transformation and tumorigenesis in various cancer types, suggesting that it may act as an oncogene. The study of TRIM44 is further motivated by its involvement in the modulation of the p53 signaling pathway, which plays a crucial role in cell cycle regulation and tumor suppression. As a result, understanding the functional mechanisms of TRIM44 and its interactions with other cellular proteins could yield significant insights into cancer biology and potential therapeutic targets. Researchers are increasingly focusing on the recombinant expression of TRIM44 protein to elucidate its structure-function relationship and investigate its biological activities in vitro and in vivo. This approach aims to clarify TRIM44’s role in disease mechanisms, particularly in oncogenesis, thereby potentially offering novel avenues for targeted cancer therapies. As the field continues to evolve, further elucidation of TRIM44's functions and interactions is essential to harness its potential in clinical applications and therapeutic strategies.
