Recombinant Human Engulfment and cell motility protein 1 (ELMO1)

Code CSB-YP856404HU
MSDS
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Source Yeast
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Code CSB-EP856404HU
MSDS
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Source E.coli
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Code CSB-EP856404HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP856404HU
MSDS
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Source Baculovirus
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Code CSB-MP856404HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ELMO1
Uniprot No.
Alternative Names
CED 12; Ced 12 homolog 1; Ced 12 homolog; CED-12; CED12; Ced12 homolog 1; Ced12 homolog; ELMO 1; ELMO-1; Elmo1; ELMO1_HUMAN; Engulfment and cell motility 1; Engulfment and cell motility protein 1; KIAA0281; MGC126406; Protein ced-12 homolog
Species
Homo sapiens (Human)
Expression Region
1-727
Target Protein Sequence
MPPPADIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA LQHADSSNFY ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK LEALKDLASL SRDVTFAQEF INLDGISLLT QMVESGTERY QKLQKIMKPC FGDMLSFTLT AFVELMDHGI VSWDTFSVAF IKKIASFVNK SAIDISILQR SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGSDQEIQ TYTIAVINAL FLKAPDERRQ EMANILAQKQ LRSIILTHVI RAQRAINNEM AHQLYVLQVL TFNLLEDRMM TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS MYTRDYKKLG FINHVNPAMD FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL ENSSREDKHE CPFGRSSIEL TKMLCEILKV GELPSETCND FHPMFFTHDR SFEEFFCICI QLLNKTWKEM RATSEDFNKV MQVVKEQVMR ALTTKPSSLD QFKSKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI QPEILELIKQ QRLNRLVEGT CFRKLNARRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP HDSLQDKLPV ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC QLNFIAPDKH EYCIWTDGLN ALLGKDMMSD LTRNDLDTLL SMEIKLRLLD LENIQIPDAP PPIPKEPSNY DFVYDCN
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1.
Gene References into Functions
  1. ELMO1 genetic variation is associated with with type 2 diabetes. PMID: 28752301
  2. This study revealed the association of the SNP rs1345365 of the ELMO1 gene in a Mexican population PMID: 29938964
  3. A significant association of the SLC12A3 rs11643718 and ELMO1 rs741301 (Single nucleotide Polymorphism) SNPs with diabetic nephropathy in south Indians. PMID: 27699784
  4. Cdc27 is a novel binding partner of Elmo1.Cdc27-Elmo1 has a cellular role independent from the Elmo-Dock1-Rac signal module. PMID: 26882976
  5. ELMO1 is expressed in rheumatoid arthritis synovium, promotes cell migration and invasion, and regulates Rac1 activity, thereby mediating rheumatoid arthritis pathogenicity. PMID: 25901943
  6. Src-mediated Y724 phosphorylation in ELMO1 plays a critical role for cell spreading via activation of Rac1, leading to promotion of cell migration. PMID: 26205662
  7. high ELMO1 expression is an independent negative prognostic factor in normal karyotype (NK) acute myeloid leukemia. PMID: 25360637
  8. For ELMO1 (+9170 G>A), the GG genotype frequency was higher in the diabetic versus control group, but there were no differences between diabetic patients with and without nephropathies. PMID: 24433479
  9. Thus, Elmo1 and Dock180 facilitate blood vessel formation by stabilization of the endothelium during angiogenesis. PMID: 25586182
  10. There is a low frequency rate of the ancestral genotype for the ELMO1 polymorphism rs1345365 in mestizos from the western and southeastern regions of Mexico. PMID: 25167351
  11. High ELMO1 expression is associated with serous ovarian cancer. PMID: 24819662
  12. the present study characterized a novel Nck-1-ELMO1 interaction and defined a new role for Nck-1 in regulating Rac1 activity. PMID: 24928514
  13. findings reveal a previously unknown, nonredundant role for Elmo1 in controlling Dock2 levels and Dock2-dependent T cell migration in primary lymphocytes. PMID: 24821968
  14. genetic association study in population in China: Data suggest that 2 SNPs in ELMO1 (rs741301; rs10951509) are associated with diabetic nephropathy in Chinese subjects with type 2 diabetes. PMID: 22842811
  15. ELMO1 mutations are associated with esophageal adenocarcinoma. PMID: 23525077
  16. Analysis of SNP databases of Japanese patuients with diabetic nephropathy revealed ELMO1 as a gene related to the above-cited diabetic complication. PMID: 23156397
  17. findings suggest that clearance of apoptotic cells in living vertebrates is accomplished by the combined actions of apoptotic cell migration and elmo1-dependent macrophage engulfment PMID: 22503503
  18. Over-expression of NELL1 is associated with alveolar rhabdomyosarcoma. PMID: 22415709
  19. The C-terminal Pro-rich tail of ELMO1 winds around the Src-homology 3 domain of DOCK2 to form an intermolecular 5-helix bundle. The entire regions of both DOCK2 a& ELMO1 assemble to create a rigid structure required for the DOCK2 & ELMO1 binding. PMID: 22331897
  20. We sequenced 17.4 kb of ELMO1 and identified 19 variants. PMID: 20826100
  21. The protein-protein interaction between ELMO1 and COX-2 increased the cyclooxygenase activity of COX-2 and, correspondingly, fibronectin expression.(ELMO1 protein, human) PMID: 20732417
  22. findings demonstrate an in vivo role for ELMO1-dependent clearance in the testes, with implications for spermatogenesis PMID: 20958313
  23. Dock180 ELMO complex functions as an unconventional two-part exchange factor for Rac. PMID: 12134158
  24. the association of DOCK2 with ELMO1 is critical for DOCK2-mediated Rac activation, thereby suggesting that their association might be a therapeutic target for immunologic disorders caused by lymphocyte infiltration PMID: 12829596
  25. Rac activation by the ELMO.Dock180 complex at discrete intracellular locations mediated by the N-terminal 330 amino acids of ELMO1 plays a role in cell migration PMID: 14638695
  26. Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis PMID: 14737186
  27. while N-terminal SH3 of CrkII promotes assembly between CrkII and DOCK180, the C-terminal SH3 of CrkII regulates the stability and turnover of the DOCK180/ELMO complex PMID: 15700267
  28. ELMO binding to the SH3 domain of Dock180 disrupted the SH3:Docker interaction, facilitated Rac access to the Docker domain, and contributed to the GEF activity of the Dock180/ELMO complex. PMID: 15723800
  29. These results indicate that ELMO1 is a novel candidate gene that both confers susceptibility to diabetic nephropathy and plays an important role in the development and progression of this disease. PMID: 15793258
  30. Src family kinase mediated tyrosine phosphorylation of ELMO1 might represent an important regulatory mechanism that controls signaling through the ELMO1/Crk/Dock180 pathway. PMID: 15952790
  31. ARNO and ARF6 coordinate with the Dock180/Elmo complex to promote Rac activation at the leading edge of migrating cells. PMID: 16213822
  32. Using pulldown assays, we identified engulfment and cell motility (ELMO) protein as the IpgB1 binding partner. IpgB1 colocalized with ELMO and Dock180 in membrane ruffles induced by Shigella. PMID: 17173036
  33. Overexpression of ELMO1 and Dock180, a bipartite Rac1 guanine nucleotide exchange factor is associated with glioma cell invasion PMID: 17671188
  34. The DOCK180-ELMO1 interaction is mapped to the N-terminal 200 amino acids of DOCK180, and to the C-terminal 200 amino acids of ELMO1, comprising the ELMO1 PH domain. PMID: 18768751
  35. Variants in intron 13 of the ELMO1 gene appear to confer risk for diabetic nephropathy in African Americans. PMID: 19183347
  36. Report of genetic associations in ELMO1 with diabetic nephropathy, further establishing its role in the susceptibility of this disease. PMID: 19651817

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Subcellular Location
Cytoplasm. Cell membrane. Note=Translocation to plasma membrane seems to be mediated by DOCK1 and CRK.
Tissue Specificity
Widely expressed, with a higher expression in the spleen and placenta.
Database Links

HGNC: 16286

OMIM: 606420

KEGG: hsa:9844

STRING: 9606.ENSP00000312185

UniGene: Hs.434989

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