GEMIN5 Protein (AA 1-1502) (Strep Tag)

Catalog No. ABIN3136298

Product Details

Target: GEMIN5 (Gem (Nuclear Organelle) Associated Protein 5 (GEMIN5))

Protein Type: Recombinant

Protein Characteristics: AA 1-1502

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This GEMIN5 protein is labelled with Strep Tag.

Application: ELISA, Western Blotting (WB), SDS-PAGE (SDS)

Sequence: MKPEPRTLPP SPNWYCSRCS DAAPGGIFGF AARTSVFLVR VGPGAGASPG APPFRVVGEL VGHTERVSGF TFSHHPGQYN LCATSSDDGT VKVWDVETKT VVTEHTLHQH TISALHWSPT VKDLIVSGDE KGVVFCYWLN RNDSQHLFTE PRTIFCLTCS PHHENLVAIG YKDGIVVIID ISKKGEVIHR LRGHDDEIHS IAWCPLSGED CLSISQEENS EEPDIPNGKL IAETPITKGC YLATGSKDQT IRIWSCSRGR GVMVLKLPFL KRRSGGVDPT VKERLWLTLH WPKNQPTQLV SSCFGGELLL WDLTQSWRRK YTLFSTSAEG HNHSRIVFNL CSLKTEDGKQ LLLSTSMDRD VKCWDMATLE CCWTLPSLGG FAYSLAFSPV DVGSLAIGVG DGMIRVWNTL SIKNNYDVKN FWQGVKSKVT ALCWHPNKEG CLAFGTDDGK VGLYDTCSNK PPQISSTYHK KTVYRLAWGP PVPPMSLGGE GDRPSLTLYS CGGEGVVLQH NPWKLSGEAF DINKLVRDTN SIRYKLPVHT EISWKGDGKV LALGNEDGSI EIFQVPNLRL LCTIQQHHKL VNAIVWHHEH GSRPELSCLL ASGSNNAVIY VHNLKAVLES NPESPITITE PYRTLSGHTA KITSLAWSPH HDGRLVSACY DGTAQVWDAL REEPLFNFRG HRGRLLCVAW SPVDPECIYS GADDFCVYRW LTSMQDHSRP PQGKKCIELE KKRLSQFKPK LKKKKKPTLR LPVKQDSSVG NEDESVKENS GPAENGLSDQ DGEEEAQEPE LPPSPVVCVE PVSCTDICSG FEKSKVTVSS KATSLKKEPA KEKPEALLKK RKARSMLPLS TSLDHRSKEE LHRDCLVLAT ATHAKAELNE DVSADLEERF HLGLFTDRAT LYRMMETEGK GHLESGHPEL FHQLMLWKGD LKGVLQAAAE RGELTDSLVA VAPVAGYSVW LWAVEAFAKQ LCFQDQYVKA ASYLLSIHKV YEAVELLKSN HLYREAIAVA KARLRPEDPV LKELYLSWGS ILERDGHYAI AAKCYLGATS AYDAAKVLAR KGDAASLRTA AELAAIAGEH ELAASLALRC AQELLLMKNW VGAQEALGLH ESLQGQRLVF CLLELLCRHL EEKQPLEVRG PSSIYHQWAT GSEGTLVQRV TGVWRSAFSV DTPEQCQAAL QKLQDVKYPS ATSNTPFRQL LLHVCHDLTL AMLSQQAAAW EEAVPALLQA VVRSYTSGNF TLMQEIYSAF LPGGCDHLRD KLGDLSPAMA AYKSLEAFCI YGQLYEVWWS LCGPGPESSV WVLSAESTVS DKQSKPEDSA SAEDMEQPPG PGPRLSAESE RLLSACKELF SERHASLQTS QRTVAEVQET LAEMIRQHQK SQLCKATTNG PSRDEPSRDE PSQEAERAPS QPPSPTEERN APVSLPELTR RLTEANERIA EFPESVKAWP FPDVLECCLV LLHIGSQCPD AVDPEMQQQA QELLHKYGHT RAYRRHCQSR HT
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case 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 by multi-step, protein-specific process to ensure correct folding and modification.
• These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

The big advantage of ordering our made-to-order 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 in several dilutions and is measured against its specific reference buffer.
• We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

Purification: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Purity: ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin Level: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Grade: Crystallography grade

Application Details

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

Handling

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: Unlimited (if stored properly)

Target Details

Target: GEMIN5 (Gem (Nuclear Organelle) Associated Protein 5 (GEMIN5))

Alternative Name: Gemin5 (GEMIN5 Products)

Synonyms: GEMIN-5 Protein, AA407055 Protein, AA407208 Protein, AI451603 Protein, BB194447 Protein, C330013N08 Protein, gem nuclear organelle associated protein 5 Protein, gem (nuclear organelle) associated protein 5 Protein, GEMIN5 Protein, Gemin5 Protein

Background: Gem-associated protein 5 (Gemin5),FUNCTION: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN5 recognizes and delivers the small nuclear RNAs (snRNAs) to the SMN complex. Binds to the 7-methylguanosine cap of RNA molecules (By similarity). Binds to the 3'-UTR of SMN1 mRNA and regulates its translation, does not affect mRNA stability (PubMed:25911097). May play a role in the regulation of protein synthesis via its interaction with ribosomes (By similarity). {ECO:0000250|UniProtKB:Q8TEQ6, ECO:0000269|PubMed:25911097}.

Molecular Weight: 166.6 kDa

UniProt: Q8BX17

Pathways: Ribonucleoprotein Complex Subunit Organization