Recombinant Human Elongation Factor 1-Alpha 1 (EEF1A1) Protein (His-SUMO)

Name: Recombinant Human Elongation Factor 1-Alpha 1 (EEF1A1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03667P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) EEF1A1.

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Product Overview

Description	Recombinant Human Elongation Factor 1-Alpha 1 (EEF1A1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P68104
Target Symbol	EEF1A1
Synonyms	CCS 3; CCS3; Cervical cancer suppressor 3; chunp6927; CTCL tumor antigen; EE1A1; EEF 1; EEF1A; eEF1A-1; EEF1A1; EF-1-alpha-1; EF-Tu; EF1A; EF1a like protein; EF1A1_HUMAN; Elongation factor 1 alpha subunit; Elongation factor 1-alpha 1; Elongation factor Tu; Eukaryotic elongation factor 1 A-1; Eukaryotic translation elongation factor 1 alpha 1; Eukaryotic translation elongation factor 1 alpha 1 like 14; Glucocorticoid receptor AF 1 specific elongation factor; GRAF 1EF; HNGC:16303; ik:tdsubc_2a3; ik:tdsubc_2b3; LENG7; Leukocyte receptor cluster (LRC) member 7; Leukocyte receptor cluster member 7; Prostate tumor inducing protein 1; PTI1; tdsubc_2a3; Translation elongation factor 1 alpha 1 like 14; wu:fa91c07; wu:fa94b03; wu:fi13b09; xx:tdsubc_2a3; xx:tdsubc_2b3
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
Expression Range	1-462aa
Protein Length	Full Length
Mol. Weight	66.1kDa
Research Area	Epigenetics And Nuclear Signaling
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	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1.; (Microbial infection) Required for the translation of viral proteins and viral replication during human coronavirus SARS-CoV-2 infection.
Subcellular Location	Cytoplasm. Nucleus. Nucleus, nucleolus. Cell membrane.
Protein Families	TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily
Database References	HGNC: 3189 OMIM: 130590 KEGG: hsa:1915 STRING: 9606.ENSP00000330054 UniGene: PMID: 29398204 A strong correlation was found between the dysregulation of eEF1A synthesis and Alzheimer's Disease-associated synaptic failure. PMID: 27567813 the different kinases that recognize the Ser and Thr residues of the eEF1A1 and eEF1A2 isoforms and regulate their involvement in different cellular processes like cell survival and apoptosis. PMID: 27568183 Taken together, these findings enabled us to identify a novel mechanism by which eEF1A1 regulates the cell cycle's G1 phase to promote tumor proliferation by regulating cyclin D1 expression through STAT1 signaling in HCC. PMID: 29079187 Methylation of lysine (K36) in eukaryotic elongation factor alpha (eEF1A) proteins is dependent on EEF1A lysine methyltransferase 4 (eEF1A-KMT4) in vivo. PMID: 28520920 The present study identifies METTL21B as the enzyme responsible for methylation of eEF1A on Lys-165 and shows that this modification is dynamic, inducible and likely of regulatory importance. PMID: 28108655 EEF1A1 is somatically mutated in 9% of follicular lymphoma tumors. PMID: 25713363 we show how FAT10 stabilizes the translation elongation factor eEF1A1, which contributes to cancer cell proliferation PMID: 27312528 The expression of RPL13A and EEF1A1 was not affected by differentiation, thus being these genes the most stable candidates as reference genes for RT-PCR. PMID: 27304673 Study demonstrated that PAK4 interacted with eEF1A1 to promote migration and invasion of gastric cancer cells, thereby providing new insights into the function of PAK4 and eEF1A1 in the progression of gastric cancer. PMID: 28393218 this study demonstrates that eEF1A1 regulates the subcellular location of expanded poly(A) proteins and is therefore a potential therapeutic target for combating the pathogenesis of poly(A) diseases. PMID: 28246169 analysis of eEF1A1 oligomerization reveals that specific cysteine residues are required for this oligomerization activity PMID: 26515794 Data (including data from studies using purified proteins/hepatocyte lysates) suggest eEF1A1/Sgt1a interact as multimer; D2/D3 domains of eEF1A1 and TPR domain of Sgt1 are involved in multimer formation; Sgt1 competes with viral RNA to bind to eEF1A. PMID: 26545799 Data indicate that the methylation of lysine (Lys) in elongation factor 1A (eEF1A) by methyltransferase is conserved from yeast to human. PMID: 26545399 ROCK phosphorylated eEF1A1 is a novel substrate for TIMAP-PP1 underlining the complex regulatory role of TIMAP in the endothelium. PMID: 26497934 Study found reduced levels of hippocampal eEF1A protein in Alzheimer's disease PMID: 26551858 Our results provide novel information on the intracellular distribution and interaction of eEF1A isoforms. PMID: 26212729 These results suggest that the antitumor effects of paclitaxel in breast cancer are mediated by activation of the AMPK/EF1alpha/FOXO3a signaling pathway. PMID: 26397839 These results suggest that miR-33a-5p is downregulated during Japanese encephalitis virus infection, which contributes to viral replication by increasing the intracellular level of EEF1A1, an interaction partner of the viral NS3 and NS5 proteins. PMID: 26819305 Low expression of eEF1A1 was associated with cervical squamous cell carcinoma. PMID: 25893434 eEF1A-1 protein was induced by high palmitate, and partially re-localized from its predominant location at the ER to polymerized actin at the cell periphery, coinciding with the onset of ER stress. PMID: 26102086 The combined evidence indicates a direct interaction between eEF1A and reverse transcriptase is crucial for HIV reverse transcription and replication PMID: 26624286 eEF1A interacts with 5'UTR of HIV-1 genomic RNA and the interaction is important for late DNA synthesis in reverse transcription. PMID: 26242867 Data show that translation elongation factor eEF1A1 coordinates the heat shock response by adjusting transcriptional yield to translational needs. PMID: 25233275 EEF1A1, SSRP1, and XRCC6 are novel interacting partners of the mineralocorticoid receptor PMID: 25000480 eEF1A1 may mediate SAMHD1 turnover by targeting it to the proteosome for degradation through association with Cullin4A and Rbx1. PMID: 25423367 protein expressions of stathmin and EF1alpha were found in DNs of precancerous lesions, whereas they were absent or present at very low levels in normal liver and liver cirrhosis PMID: 24885363 These data provide the experimental evidence that telomere shortening and related inflammatory proteins are associated with human IgAN, and it could be a new direction for the disease progression study. PMID: 24903994 findings suggest that eEF1A contributes to the morphology of postsynaptic membrane specializations at inhibitory synapses PMID: 23839781 Sequence differences in the EF1alpha -3 promoter likely account for the activity differences seen. Investigators need to recognize that all promoters of the same name may not be equivalent in driving transgene expression. PMID: 24688302 Describes a nuclear role for eEF1A and provide a mechanism for protein nuclear export that attenuates the activity of SNAG-containing transcription factors PMID: 24209753 results reveal a novel molecular mechanism for a non-canonical role of eEF1A1 in signal transduction via direct modulation of kinase-dependent phosphorylation events PMID: 24487064 Human eEF1A1 is a negative regulator of the pro-apoptotic function of p53 and p73 PMID: 23799104 We propose that the reduction in SphK1 activity late in DENV-2-infected cells is a consequence of DENV-2 out-competing SphK1 for eEF1A binding and hijacking cellular eEF1A for its own replication strategy. PMID: 23939980 Knocking down eEF1A1 gene has noticeable effects on the proliferation inhibition and apoptosis induction of Jurkat cells. PMID: 22931638 eEF1A binds defective polypeptides released from ribosomes, which generates a signal that triggers aggresome formation. PMID: 22357952 This study identified eEF1A1 as a FAT10-specific binding protein, and when the expression of FAT10 was reduced by siRNA knockdown, this resulted in downregulation of eEF1A1 expression in hepatoma cells. PMID: 22569823 Overexpression of eukaryotic translation elongation factor 1 alpha 1 is associated with nonepithelial ovarian cancer. PMID: 22531302 Results show a new function of eEF1A that contributes to cell regulation, including anoikis. PMID: 22399298 In Huh-7 hepatoma cells, the hepatitis B virus X protein inhibits dimer formation of eEF1A1, hence blocks filamentous actin bundling. PMID: 22499008 High eEF1A1 is associated with metastatic progression of prostate cancer. PMID: 22355332 An immunoreactive protein detected in sera from 21 of 40 infiltrating ductal breast carcinoma patients was isolated and subsequently identified as elongation factor-Tu. PMID: 21704614 Mammalian PUM2-Ago-eEF1A inhibited translation of nonadenylated and polyadenylated reporter mRNAs in vitro. PMID: 22231398 Pilot evaluation in archive prostate tissues showed the presence of EEF1A2 mRNA in near all neoplastic and perineoplastic but not in normal samples or in benign adenoma; in contrast, EEF1A1 mRNA was everywhere detectable PMID: 22095224 A co-localization of SORBS2 and eEF1A was evidenced at level of plasma membrane, thus suggesting the involvement of eEF1A1 in novel key signal transduction complexes. PMID: 21689717 study defines the mechanism regulating eEF1A-mediated SK1 activation, and also establishes SK1 as being integral for PTI-1-induced oncogenesis PMID: 20838377 These findings provide evidence that elongation factor-1 alpha correlates closely with the survival of patients with prostate cancer and may be a novel prognostic factor. PMID: 20545466 Phosphorylation of eEF1A1 by TbetaR-I is a novel regulatory mechanism that provides a direct link to regulation of protein synthesis by TGF-beta, as an important component in the TGF-beta-dependent regulation of protein synthesis and cell proliferation PMID: 20832312 Data show that EF1alpha, RPL13a and YWHAZ are suitable genes for the RT-qPCR analysis and comparison of several sources of human MSC during in vitro characterization and differentiation as well as in an ex vivo animal model of global cerebral ischemia. PMID: 20716364 Proteomics was used to study colonic epithelial aging, for differential proteins in the human normal colonic epithelial tissues from young and old people. Rack1, EF-Tu and Rhodanese, three validated differential proteins, were further investigated. PMID: 20099848

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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.

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