ACTR2 Protein (AA 1-394) (Strep Tag)
Quick Overview for ACTR2 Protein (AA 1-394) (Strep Tag) (ABIN3089210)
Target
See all ACTR2 ProteinsProtein Type
Origin
Source
Application
Purity
Grade
-
-
Protein Characteristics
- AA 1-394
-
Purification tag / Conjugate
- This ACTR2 protein is labelled with Strep Tag.
-
Sequence
-
MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRNCKILLT EPPMNPTKNR EKIVEVMFET YQFSGVYVAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFSLPHLTR RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL VESYTLPDGR IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR KHMVFLGGAV LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR
Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If you have a special request, please contact us.. -
Characteristics
-
Key Benefits:
- Made in Germany - from design to production - by highly experienced protein experts.
- Protein expressed with ALiCE® and purified in one-step affinity chromatography
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a predefined custom protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.
The big advantage of ordering our predefined custom proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.
Expression System:- ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
- During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!
Concentration:- The concentration of our recombinant proteins is measured using the absorbance at 280nm.
- The protein's absorbance will be measured against its specific reference buffer.
- We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.
-
Purification
- One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).
-
-
Want other Options for this Protein ?
!Discover Our Catalog and Custom Protein Service Options!ProductExpression SystemConjugateOriginPriceExpression System Wheat germConjugate GST tagOrigin HumanPrice $488.72Expression System Escherichia coli (E. coli)Conjugate His tagOrigin HumanPrice $387.01Expression System Baculovirus infected Insect CellsConjugate GST tagOrigin HumanPrice $1,317.85Expression System BacteriaConjugate His tagOrigin HumanPrice $520.52Your project requires further customization? Contact us and discover our custom protein solutions
-
-
-
Application Notes
- In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.
-
Comment
-
ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein! -
Restrictions
- For Research Use only
-
-
-
Format
- Liquid
-
Buffer
-
The buffer composition is at the discretion of the manufacturer.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein. -
Handling Advice
- Avoid repeated freeze-thaw cycles.
-
Storage
- -80 °C
-
Storage Comment
- Store at -80°C.
-
Expiry Date
- 12 months
-
-
- ACTR2 (Actin-Related Protein 2 (ACTR2))
-
Alternative Name
- ACTR2
-
Background
- Actin-related protein 2 (Actin-like protein 2),FUNCTION: ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9000076). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9000076). Seems to contact the pointed end of the daughter actin filament (PubMed:9000076). In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation (PubMed:29058690). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:17220302, PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947). {ECO:0000269|PubMed:17220302, ECO:0000269|PubMed:29058690, ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:9000076}.
-
Molecular Weight
- 44.8 kDa
-
UniProt
- P61160
-
Pathways
- RTK Signaling, Regulation of Actin Filament Polymerization
Target
-