Recombinant Human Serine/threonine-protein kinase A-Raf (ARAF)

Code CSB-YP001976HU
MSDS
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Source Yeast
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Code CSB-EP001976HU
MSDS
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Source E.coli
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Code CSB-EP001976HU-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-BP001976HU
MSDS
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Source Baculovirus
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Code CSB-MP001976HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ARAF
Uniprot No.
Alternative Names
A raf 1; A Raf proto oncogene serine/threonine protein kinase; ARAF 1; Araf; ARaf proto oncogene serine/threonine protein kinase; ARAF_HUMAN; ARAF1; Oncogene Araf1; Oncogene PKS2; PKS 2; PKS; PKS2; Proto oncogene Pks; Proto-oncogene A-Raf; Proto-oncogene A-Raf-1; Proto-oncogene Pks; RAFA 1; RAFA1; Ras binding protein DA Raf; Serine/threonine-protein kinase A-Raf; v raf murine sarcoma 3611 viral oncogene homolog; v raf murine sarcoma 3611 viral oncogene homolog 1; v raf oncogene homolog 1 (murine sarcoma 3611 virus)
Species
Homo sapiens (Human)
Expression Region
1-606
Target Protein Sequence
MEPPRGPPAN GAEPSRAVGT VKVYLPNKQR TVVTVRDGMS VYDSLDKALK VRGLNQDCCV VYRLIKGRKT VTAWDTAIAP LDGEELIVEV LEDVPLTMHN FVRKTFFSLA FCDFCLKFLF HGFRCQTCGY KFHQHCSSKV PTVCVDMSTN RQQFYHSVQD LSGGSRQHEA PSNRPLNELL TPQGPSPRTQ HCDPEHFPFP APANAPLQRI RSTSTPNVHM VSTTAPMDSN LIQLTGQSFS TDAAGSRGGS DGTPRGSPSP ASVSSGRKSP HSKSPAEQRE RKSLADDKKK VKNLGYRDSG YYWEVPPSEV QLLKRIGTGS FGTVFRGRWH GDVAVKVLKV SQPTAEQAQA FKNEMQVLRK TRHVNILLFM GFMTRPGFAI ITQWCEGSSL YHHLHVADTR FDMVQLIDVA RQTAQGMDYL HAKNIIHRDL KSNNIFLHEG LTVKIGDFGL ATVKTRWSGA QPLEQPSGSV LWMAAEVIRM QDPNPYSFQS DVYAYGVVLY ELMTGSLPYS HIGCRDQIIF MVGRGYLSPD LSKISSNCPK AMRRLLSDCL KFQREERPLF PQILATIELL QRSLPKIERS ASEPSLHRTQ ADELPACLLS AARLVP
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.

Customer Reviews and Q&A

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Target Background

Function
Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade.; Serves as a positive regulator of myogenic differentiation by inducing cell cycle arrest, the expression of myogenin and other muscle-specific proteins, and myotube formation.
Gene References into Functions
  1. The constitutive or induced re-localization of A-Raf to the plasma membrane compromises its ability to efficiently sequester and inactivate MST2, thus rendering cells susceptible to apoptosis PMID: 26891695
  2. This review discusses the regulation of A-Raf protein expression, and the roles of A-Raf in apoptosis and cancer, with a special focus on its role in resistance to Raf inhibitors. [review] PMID: 26508523
  3. analysis of FGFR2-PPHLN1 fusion and ARAF mutations in intrahepatic cholangiocarcinoma PMID: 25608663
  4. Aberrant expression of A-, B-, and C-RAF, and COT is frequent in PTC; increased expression of COT is correlated with recurrence of PTC. PMID: 25674762
  5. Dimerization of the kinase ARAF promotes MAPK pathway activation and cell migration. PMID: 25097033
  6. The study identifies somatic activating ARAF mutations in Langerhans cell histiocytosis. PMID: 24652991
  7. Galpha12-ARAF-ERK pathway stimulates RFFL transcription through the transcription factor c-Myc. PMID: 24114843
  8. show that Araf antagonizes mesendoderm induction and patterning activity of Nodal/Smad2 signals in vertebrate embryos by directly inhibiting Smad2 signalling PMID: 23591895
  9. study investigated role of ARAF in cancer cell signaling and examined the role of ARAF in mediating paradoxical activation of the MAPK pathway in cells treated with RAF inhibitors; ARAF seems to stabilize BRAF:CRAF complexes in cells treated with RAF inhibitors and regulate cell signaling in a subtle manner to ensure signaling efficiency PMID: 22926515
  10. Ras pathway activation via EGF treatment induced strong binding between B-Raf and C-Raf and a low level of binding between B-Raf and A-Raf. PMID: 23352452
  11. hnRNP H blocks MST2-mediated apoptosis in cancer cells by regulating A-Raf transcription. PMID: 20145135
  12. In a two-hybrid screen of human fetal liver cDNA library, TH1 was detected as a new interaction partner of A-Raf; this specific interaction may have played a critical role in the activation of A-Raf. PMID: 11952167
  13. A-Raf kinase is negatively regulated by trihydrophobin 1 PMID: 14684750
  14. mutation analysis of the conserved regions in the ARAF gene in human colorectal adenocarcinoma PMID: 14688025
  15. A-Raf residues are identified that bind to specific phosphoinositides, possibly as a mechanism to localize the enzyme to particular membrane microdomains rich in these phospholipids. PMID: 15736953
  16. These data reveal that B-RAF is an important mediator of neuronal survival, migration, and dendrite formation and that A-RAF cannot fully compensate for these functions. PMID: 16980614
  17. Positive regulation of A-RAF by phosphorylation of isoform-specific hinge segment and identification of novel phosphorylation sites. PMID: 18662992
  18. A-Raf interacts with MEK1 and activates MEK1 by phosphorylation. PMID: 8621729

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Protein Families
Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily
Tissue Specificity
Predominantly in urogenital tissues.
Database Links

HGNC: 646

OMIM: 311010

KEGG: hsa:369

STRING: 9606.ENSP00000366244

UniGene: Hs.446641

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