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1000 results found for “mitochondrial ribosomal protein”
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Name :
CRP RatDescription:
C-Reactive Protein Rat Recombinant
Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.
Product # :
PRO-1421Price :
Quantity :
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Shipped with Ice Packs
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Description
CRP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 217 amino acids (20-230 a.a.) and having a molecular mass of 24.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).CRP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CRP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
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Synonyms
Ptx1, C-reactive protein, Pentraxin 1, C-Reactive Protein Pentraxin-Related.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
HEDMSKQAFV FPGVSATAYV SLEAESKKPL EAFTVCLYAH ADVSRSFSIF SYATKTSFNE ILLFWTRGQG FSIAVGGPEI LFSASEIPEV PTHICATWES ATGIVELWLD GKPRVRKSLQ KGYIVGTNAS IILGQEQDSY GGGFDANQSL VGDIGDVNMW DFVLSPEQIN AVYVGRVFSP NVLNWRALKY ETHGDVFIKP QLWPLTDCCE SHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RNP/Sm BovineDescription:
Bovine RNP/Sm Ribonucleoprotein Complex
Product # :
PRO-2556Price :
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Description
RNP/Sm Bovine is purified from bovine tissues by proprietary protein-chemical techniques.
Source
Bovine tissues.
Formulation
RNP/Sm Bovine is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
U-snRNPs which are a pivotal part of spliceosomes, are created between small non-coding nuclear RNAs and a protein moiety. Whereas the 7 Sm proteins are conserved, the RNP antigens are exclusive for each U-snRNP subclass.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. Immunodot test with positive/negative samples.
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Applications
Western blot with anti-RNP/Sm autoantibody positive sample.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AUH HumanDescription:
AU RNA Binding Protein/Enoyl-CoA Hydratase Human Recombinant
Methylglutaconyl-CoA hydratase, mitochondrial, AU-specific RNA-binding enoyl-CoA hydratase, AU-binding protein/enoyl-CoA hydratase, AUH.
Product # :
ENZ-046Price :
Quantity :
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Shipped with Ice Packs
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Description
AUH Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 293 amino acids (68-339 a.a.) and having a molecular mass of 31.4kDa. The AUH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AUH solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Mitochondrial methylglutaconyl-CoA hydratase (AUH) is involved in the amino acid degradation pathway by catalyzing the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA and water. AUH Human is expressed as a single mRNA species of 1.8 kb, and translated as a 40kDa precursor protein which is consequently processed to a 32kDa mature form. AUH has a very low enoyl-CoA hydratase activity. The AUH protein binds to the AU-rich element (ARE), which is a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. AU-rich elements are involved in directing RNA to rapid degradation and deadenylation. In addition, AUH is homologous to enol-CoA hydratase, which is an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is therefore a bifunctional chimera between RNA binding and metabolic enzyme activity.
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Synonyms
Methylglutaconyl-CoA hydratase, mitochondrial, AU-specific RNA-binding enoyl-CoA hydratase, AU-binding protein/enoyl-CoA hydratase, AUH.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSEMKTEDE LRVRHLEEEN RGIVVLGINR AYGKNSLSKN LIKMLSKAVD ALKSDKKVRT IIIRSEVPGI FCAGADLKER AKMSSSEVGP FVSKIRAVIN DIANLPVPTI AAIDGLALGG GLELALACDI RVAASSAKMG LVETKLAIIP GGGGTQRLPR AIGMSLAKEL IFSARVLDGK EAKAVGLISH VLEQNQEGDA AYRKALDLAR EFLPQGPVAM RVAKLAINQG MEVDLVTGLA IEEACYAQTI PTKDRLEGLL AFKEKRPPRY KGE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LIF Human, HisDescription:
Leukemia Inhibitory Factor Human Recombinant, His tag
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-1082Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 23-202) containing 189 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 20.9kDa (calculated).
Source
Escherichia Coli.
Formulation
LIF filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 20 mM Tris buffer, 20 mM NaCl and 5% w/v trehalose, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHAS PLPITPVNAT CAIRHPCHNN LMNQIRSQLA QLNGSANALF ILYYTAQGEP FPNNLDKLCG PNVTDFPPFH ANGTEKAKLV ELYRIVVYLG TSLGNITRDQ KILNPSALSL HSKLNATADI LRGLLSNVLC RLCSKYHVGH VDVTYGPDTS GKDVFQKKKL GCQLLGKYKQ IIAVLAQAF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RBM11 HumanDescription:
RNA Binding Motif Protein 11 Human Recombinant
Splicing regulator RBM11, RNA-binding motif protein 11, RBM11.
Product # :
PRO-1802Price :
Quantity :
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Shipped with Ice Packs
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Description
RBM11 Human Recombinant produced in E. coli is a single polypeptide chain containing 304 amino acids (1-281) and having a molecular mass of 34.6kDa. RBM11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RBM11 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
RNA Binding Motif Protein 11 (RBM11) which contains 1 RNA recognition motif is a part of the RBM family. The RBM gene family encodes proteins with an RNA binding motif which participate in the modulation of apoptosis. RBM11 is expressed in testis, kidney, spleen, brain, spinal cord and mammary gland and can be found as 2 isoforms produced by alternative splicing.
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Synonyms
Splicing regulator RBM11, RNA-binding motif protein 11, RBM11.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFPAQEE ADRTVFVGNL EARVREEILY ELFLQAGPLT KVTICKDREG KPKSFGFVCF KHPESVSYAI ALLNGIRLYG RPINVQYRFG SSRSSEPANQ SFESCVKINS HNYRNEEMLV GRSSFPMQYF PINNTSLPQE YFLFQKMQWH VYNPVLQLPY YEMTAPLPNS ASVSSSLNHV PDLEAGPSSY KWTHQQPSDS DLYQMTAPLP NSASVSSSLN HVPDLEAGPS SYKWTHQQPS DSDLYQMNKR KRQKQTSDSD SSTDNNRGNE CSQKFRKSKK KKRY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BMP 4 HumanDescription:
Bone Morphogenetic Protein-4 Human Recombinant
BMP4, ZYME, BMP2B, BMP2B1.
Product # :
CYT-361Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
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Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
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Background
What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant
As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.
Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.
Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!
How Does Bone Morphogenetic Protein-4 (BMP-4) Work?
Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.
The Role of BMP-4
This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.
However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:
- Embryonic development
- Wound healing
- Bone remodeling
- Immune response modulation
- Tissue repair
- Cardiac development and function
What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?
To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.
As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.
More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:
- Cancer therapy
- Development of engineered tissues and organs
- Bone regeneration for the treatment of osteoporosis and nonunion fractures
- Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
- Promotion of tissue repair and regeneration
Final Thoughts BMP-4
Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.
However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 13kDa.
What is the source or expression system of BMP4 Protein?
Escherichia Coli.
What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP4 Protein?
The biological functionality of BMP4 Protein will be determined in the future.
What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RAP1B HumanDescription:
RAP1B, Member RAS Oncogene Family Human Recombinant
RAP1B, member of RAS oncogene family, DKFZp586H0723, K-REV, RAL1B, GTP-binding protein smg p21B, Ras family small GTP binding protein RAP1B, RAS-related protein RAP1B, small GTP binding protein.
Product # :
PRO-083Price :
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Shipped with Ice Packs
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Description
RAP1B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181.a.a) and having a molecular mass of 22.6kDa. RAP1B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RAP1B protein solution (0.25mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
RAP1B is a member of a superfamily of RAS-like small GTP-binding proteins which takes part in cell signaling. RAP1B owns an intrinsic GTPase activity and is universally expressed in mammalian tissues. The alleged effector domain of Ras proteins, whose integrity is required for cell transformation as well as interaction with the putative effector protein GAP, is conserved in both Rap 1 proteins.
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Synonyms
RAP1B, member of RAS oncogene family, DKFZp586H0723, K-REV, RAL1B, GTP-binding protein smg p21B, Ras family small GTP binding protein RAP1B, RAS-related protein RAP1B, small GTP binding protein.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ CMLEILDTAG TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL EDERVVGKEQ GQNLARQWNN CAFLESSAKS KINVNEIFYD
LVRQINRKTP VPGKARKKSS C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RRAS HumanDescription:
Related RAS Viral (r-ras) Oncogene Homolog Human Recombinant
Ras-Related Protein R-Ras, p23, RRAS.
Product # :
PRO-808Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RRAS Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 235 amino acids (1-215 a.a.) and having a molecular mass of 25.3 kDa. RRAS protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
RRAS Human solution (0.5mg/1ml) containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
RRAS belongs to the Ras family which functions in signal transduction pathways. RRAS interacts with RASSF5, NCK1, Bcl-2, ARAF and RALGDS. RRAS binds GTP and GDP, and it has intrinsic GTPase activity. RRAS regulates the organization of the actin cytoskeleton
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Synonyms
Ras-Related Protein R-Ras, p23, RRAS.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSGAASGTG RGRPRGGGPG PGDPPPSETH KLVVVGGGGV GKSALTIQFI QSYFVSDYDP TIEDSYTKIC SVDGIPARLD ILDTAGQEEF GAMREQYMRA GHGFLLVFAI NDRQSFNEVG KLFTQILRVK DRDDFPVVLV GNKADLESQR QVPRSEASAF GASHHVAYFE ASAKLRLNVD EAFEQLVRAV RKYQEQELPP SPPSAPRKKG GGCPC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NAP1L1 HumanDescription:
Nucleosome Assembly Protein 1-Like 1 Human Recombinant
Nucleosome assembly protein 1-like 1, NRP, hNRP, NAP1L, NAP1, NAP-1-related protein, HSP22-like protein interacting protein, MGC23410, MGC8688.
Product # :
PRO-985Price :
Quantity :
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Shipped with Ice Packs
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Description
NAP1L1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (1-388 a.a.) and having a molecular mass of 47.2kDa.NAP1L1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NAP1L1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NAP1L1 is a member of the nucleosome assembly protein (NAP) family. NAP1L1 protein plays a part in DNA replication, modulating chromatin formation and regulation of cell proliferation.
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Synonyms
Nucleosome assembly protein 1-like 1, NRP, hNRP, NAP1L, NAP1, NAP-1-related protein, HSP22-like protein interacting protein, MGC23410, MGC8688.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MADIDNKEQS ELDQDLDDVE EVEEEETGEE TKLKARQLTV QMMQNPQILA ALQERLDGLV ETPTGYIESL PRVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI INAIYEPTEE ECEWKPDEED EISEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL LSDMVQEHDE PILKHLKDIK VKFSDAGQPM SFVLEFHFEP NEYFTNEVLT KTYRMRSEPD DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF FAPPEVPESG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE ADEEGEEEGD EENDPDYDPK KDQNPAEC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SIRT2 HumanDescription:
Sirtuin 2 Human Recombinant
Sirtuin 2, SIR2L2, SIR2-like protein 2, NAD-dependent deacetylase sirtuin-2, Silent Information Regulator 2.
Product # :
PRO-033Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIRT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352a.a.) and having a molecular mass of 41.7kDa.SIRT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SIRT2 protein solution (0.25mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 2mM DTT, 200mM NaCl, 0.5mM EDTA and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SIRT2 belongs to the sirtuin family of proteins, homologs to the yeast Sir2 protein. Proteins of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes and take part in various processes, including transcriptional regulation, cell cycle progression, DNA-damage repair and aging. SIRT2 is a NAD-dependent deacetylase, which deacetylates the 'Lys-40' of alpha-tubulin.
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Synonyms
Sirtuin 2, SIR2L2, SIR2-like protein 2, NAD-dependent deacetylase sirtuin-2, Silent Information Regulator 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDFLRNLFSQ TLSLGSQKER LLDELTLEGV ARYMQSERCR RVICLVGAGI STSAGIPDFR SPSTGLYDNL EKYHLPYPEA IFEISYFKKH PEPFFALAKE LYPGQFKPTI CHYFMRLLKD KGLLLRCYTQ NIDTLERIAG LEQEDLVEAH GTFYTSHCVS ASCRHEYPLS WMKEKIFSEV TPKCEDCQSL VKPDIVFFGE SLPARFFSCM QSDFLKVDLL LVMGTSLQVQ PFASLISKAP LSTPRLLINK EKAGQSDPFL GMIMGLGGGM DFDSKKAYRD VAWLGECDQG CLALAELLGW KKELEDLVRR EHASIDAQSG AGVPNPSTSA SPKKSPPPAK DEARTTEREK PQ
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MIS12 HumanDescription:
MIS12 Human Recombinant
hMis12, KNTC2AP, MTW1, Protein MIS12 homolog.
Product # :
PRO-022Price :
Quantity :
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Shipped with Ice Packs
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Description
MIS12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-205 a.a.) and having a molecular mass of 26.5kDa. MIS12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIS12 protein solution (1mg/ml) containing 20mM Tris-HCl buffer, (pH 8.0) ,2M Urea and10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein MIS12 Belongs to the mis12 family. MIS12 is an element of the MIS12 complex, which is necessary for kinetochore formation during mitosis and normal chromosome alignment and segregation. The MIS12 complex which comprised of MIS12,DSN1 , NSL1 and PMF-1. MIS12 is section of a network of complexes that supply microtubule attachment and generates pulling forces from depolymerization.
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Synonyms
hMis12, KNTC2AP, MTW1, Protein MIS12 homolog.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSVDPMT YEAQFFGFTP QTCMLRIYIA FQDYLFEVMQ AVEQVILKKL DGIPDCDISP VQIRKCTEKF LCFMKGHFDN LFSKMEQLFL QLILRIPSNI LLPEDKCKET PYSEEDFQHL QKEIEQLQEK YKTELCTKQA LLAELEEQKI VQAKLKQTLT FFDELHNVGR DHGTSDFRES LVSLVQNSRK LQNIRDNVEK ESKRLKIS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
C6ORF108 HumanDescription:
Chromosome 6 Open Reading Frame 108 Human Recombinant
c-Myc-responsive protein Rcl, RCL,putative c-Myc-responsive.
Product # :
PRO-249Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
C6ORF108 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 194 amino acids (1-174 a.a.) and having a molecular mass of 21.2kDa.C6ORF108 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C6ORF108 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
C6ORF108 is stimulated by c-Myc protein that is a transcription factor that is involved in the regulation of cell proliferation, differentiation, and apoptosis. C6ORF108 functions in rat in cellular proliferation and c-Myc-mediated transformation. C6ORF108 catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5''-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5''-monophosphates comprising purine bases are favored to those comprising of pyrimidine bases.
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Synonyms
c-Myc-responsive protein Rcl, RCL,putative c-Myc-responsive.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAAMVPGRS ESWERGEPGR PALYFCGSIR GGREDRTLYE RIVSRLRRFG TVLTEHVAAA ELGARGEEAA
GGDRLIHEQD LEWLQQADVV VAEVTQPSLG VGYELGRAVA FNKRILCLFR PQSGRVLSAM IRGAADGSRF QVWDYEEGEV EALLDRYFEA
DPPGQVAASP DPTT.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ARF4 HumanDescription:
ADP-Ribosylation Factor 4 Human Recombinant
ADP-ribosylation factor 4, ARF4, ARF2.
Product # :
PRO-066Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARF4 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 204 amino acids (1-180 a.a.) and having a molecular mass of 23kDa. The ARF4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARF4 solution (0.5 mg/ml) in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
ARF4 belongs to the ARF gene family whose members encode small guanine nucleotide-binding proteins which stimulate the ADP-ribosyltransferase activity of cholera toxin and have a role in vesicular trafficking and as activators of phospholipase D. The ARF proteins include five ARF proteins and eleven ARF-like proteins and constitute one family of the RAS superfamily. They are classified as class I, class II and class III; the ARF4 gene is a class II member. The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains 6 exons and 5 introns. The ARF4 gene is the most divergent member of the human ARFs.
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Synonyms
ADP-ribosylation factor 4, ARF4, ARF2.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGLTIS SLFSRLFGKK QMRILMVGLD AAGKTTILYK LKLGEIVTTI PTIGFNVETV EYKNICFTVW DVGGQDRIRP LWKHYFQNTQ GLIFVVDSND RERIQEVADE LQKMLLVDEL RDAVLLLFAN KQDLPNAMAI SEMTDKLGLQ SLRNRTWYVQ ATCATQGTGL YEGLDWLSNE LSKR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
C12ORF5 HumanDescription:
Chromosome 12 Open Reading Frame 5 Human
Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.
Product # :
PRO-1791Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TIGAR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids and having a molecular mass of 30.1kDa. The TIGAR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TIGAR was Lyophilized from a 0.2 µm filtered concentrated solution in 20mM Tris-HCl, pH8.5, 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
TIGAR is a p53-inducible enzyme which catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is an influential activator of 6-phosphofructose-1 kinase (the rate limiting enzyme of glycolysis). By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing through the pentose phosphate pathway, the main cellular source for NADPH.
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Synonyms
Fructose-2,6-bisphosphatase TIGAR, TP53-induced glycolysis and apoptosis regulator, TIGAR, C12orf5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TIGAR stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TIGAR should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized TIGAR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MARFALTVVR HGETRFNKEK IIQGQGVDEP LSETGFKQAA AAGIFLNNVK FTHAFSSDLM RTKQTMHGIL ERSKFCKDMT VKYDSRLRER KYGVVEGKAL SELRAMAKAA REECPVFTPP GGETLDQVKM RGIDFFEFLC QLILKEADQK EQFSQGSPSN CLETSLAEIF PLGKNHSSKV NSDSGIPGLA ASVLVVSHGA YMRSLFDYFL TDLKCSLPAT LSRSELMSVT PNTGMSLFII NFEEGREVKP TVQCICMNLQ DHLNGLTETR
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
RBP4 Human, HisDescription:
Retinol Binding Protein-4 Human Recombinant, His tag
Retinol Binding Protein 4 plasma, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
Product # :
CYT-555Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RBP-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 183 amino acids fragment (19-201) corresponding to the mature Retinol Binding Protein, having a total molecular mass of 25.57kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The RBP4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RBP4 protein solution is supplied in 10mM Tris, 50mM NaCl, 1mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Retinol binding protein 4(RBP4) belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. This protein was found to be expressed and secreted by adipose tissue, and was strongly associated with insulin resistance. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli.
RBP4 delivers retinol from the liver to the peripheral tissues. In plasma, the rbp-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli. -
Synonyms
Retinol Binding Protein 4 plasma, RBP-4, RBP4, Plasma retinol-binding protein, PRBP, RBP.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Protein A/GDescription:
Protein A/G Recombinant
Product # :
PRO-646Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The recombinant Protein A/G consists of 5 IgG-binding regions of protein A and 2 of protein G, which corresponds to the Protein A and G domains that are included in the recombinant sequence. Cell wall binding region, cell membrane binding region and albumin binding region have been removed from the recombinant Protein A/G to ensure the maximum specific IgG binding. The Protein A portion is from Staphylococcus aureus segments E, D, A, B and C. The Protein G portion is from Streptococcus segments C1 and C3. The fusion protein has a predicted molecular mass of 47.7kDa and containing 429 amino acids.
Source
Escherichia coli.
Formulation
Lyophilized white Powder containing no additives.
Purity
>97% as determined by SDS-PAGE and RP-HPLC.
More Info
-
Introduction
Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG. -
Stability
After reconstitution, aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNURF HumanDescription:
SNRPN Upstream Reading Frame Human Recombinant
SNRPN Upstream Reading Frame Protein.
Product # :
PRO-1849Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SNURF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (1-71) and having a molecular mass of 10.8 kDa. SNURF is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The SNURF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
SNURF is an extremely basic protein restricted to the nucleus. The evolutionarily reserved open reading frame is located on a bicistronic transcript which has a downstream ORF encoding the small nuclear ribonucleoprotein polypeptide N. The first three exons of the transcript are exploited by the upstream coding region which is known as an imprinting center. The full-length nature of these transcripts is yet to be determined but multiple transcription initiation sites have been identified and large scale alternative splicing takes place in the 5' untranslated region. An alternate exon which substitutes for exon 4 and leads to a truncated, monocistronic transcript was identified. Deletion or alternative splicing produced by a translocation event in the 5' UTR or coding region of this gene results in Prader-Willi syndrome or Angelman syndrome because of parental imprint switch failure.
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Synonyms
SNRPN Upstream Reading Frame Protein.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMERARDR LHLRRTTEQH VPEVEVQVKR RRTASLSNQE CQLYPRRSQQ QQVPVVDFQA ELRQAFLAET PRGG
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAP1LC3B2 HumanDescription:
Microtubule-Associated Protein 1 Light Chain 3 Beta 2 Human Recombinant
Microtubule-associated proteins 1A/1B light chain 3 beta 2, Microtubule-associated proteins 1A/1B light chain 3B-like, MAP1LC3B2, ATG8G.
Product # :
PRO-215Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAP1LC3B2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-120 a.a.) and having a molecular mass of 16.2kDa.MAP1LC3B2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAP1LC3B2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Microtubule-associated proteins 1A/1B light chain 3 beta 2 (MAP1LC3B2) is a member of the MAP1LC3 family. MAP1LC3B2 is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and essential for neurogenesis. The MAP1LC3B2 protein is possibly involved in formation of autophagosomal vacuoles (autophagosomes). MAP1LC3B2 is expressed primarily in the heart, testis, brain and skeletal muscle.
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Synonyms
Microtubule-associated proteins 1A/1B light chain 3 beta 2, Microtubule-associated proteins 1A/1B light chain 3B-like, MAP1LC3B2, ATG8G.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVCASQETFG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PEX26 HumanDescription:
Peroxisomal Biogenesis Factor 26 Human Recombinant
PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.
Product # :
PRO-1544Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PEX26 Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-246) and having a molecular mass of 29.3kDa. PEX26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PEX26 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Peroxisomal Biogenesis Factor 26 (PEX26) which is a part of the peroxin-26 gene family is probably required for protein import into peroxisomes. PEX26 attaches PEX1 and PEX6 to peroxisome membranes to form heteromeric AAA ATPase complexes needed for the import of proteins into peroxisomes. Deficiencies in this gene are the cause of peroxisome biogenesis disorder complementation group 8. PBD is a group of peroxisomal disorders evolving from a failure of protein import into the peroxisomal membrane or matrix.
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Synonyms
PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKSDSST SAAPLRGLGG PLRSSEPVRA VPARAPAVDL LEEAADLLVV HLDFRAALET CERAWQSLAN HAVAEEPAGT SLEVKCSLCV VGIQALAEMD RWQEVLSWVL QYYQVPEKLP PKVLELCILL YSKMQEPGAV LDVVGAWLQD PANQNLPEYG ALAEFHVQRV LLPLGCLSEA EELVVGSAAF GEERRLDVLQ AIHTARQQQK QEHSGSEEAQ KPNLEGSVSH KFLSLPMLVR QLWDSAVSH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
METRN MouseDescription:
Meteorin Mouse Recombinant
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Product # :
PRO-2241Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
METRN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
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Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NAIF1 HumanDescription:
Nuclear Apoptosis Inducing Factor 1 Human Recombinant
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
Product # :
PRO-1978Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.
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Synonyms
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MYBPC3 HumanDescription:
Myosin Binding Protein C, Cardiac Human Recombinant
Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.
Product # :
PRO-2292Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MYBPC3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Phe271) containing 281 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 29.6kDa.
Source
Escherichia Coli.
Formulation
MYBPC3 was filtered (0.4µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Myosin Binding Protein C, Cardiac (MYBPC3) is the cardiac isoform of myosin-binding protein C expressed exclusively in heart muscle. Myosin-binding protein C is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. Regulatory phosphorylation of the cardiac isoform in vivo by cAMP-dependent protein kinase upon adrenergic stimulation may be associated with modulation of cardiac contraction. MYBPC3 gene mutations are one of the causes of familial hypertrophic cardiomyopathy. In vitro MYBPC3 binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. MYBPC3 may modulate muscle contraction or it may have a more structural role.
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Synonyms
Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. MYBPC3 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASMPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS ASNKYGLATE GTRHTLTVRE VGPADQGSYA VIAGSSKVKF DLKVIEAEKA EPMLAPAPAP AEATGAPGEA PAPAAELGES APSPKGSSSA ALNGPTPGAP DDPIGLFVMR PQDGEVTVGG SITFSARVAG ASLLKPPVVK WFKGKWVDLS SKVGQHLQLH DSYDRASKVY LFELHITDAQ PAFTGSYRCE VSTKDKFDCS NFNLTVHEAM GTGDLDLLSA F.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BCAT2 HumanDescription:
Branched Chain Amino-Acid Transaminase 2 Human Recombinant
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
Product # :
ENZ-606Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
BCAT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (28-392) and having a molecular mass of 43.9kDa.BCAT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCAT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 10% glycerol, 0.2M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Branched Chain Amino-Acid Transaminase 2 (BCAT2) is a member of the class-IV pyridoxal-phosphate-dependent aminotransferase family. BCAT2 is a branched chain aminotransferase found in mitochondria. BCAT2 forms a dimer which catalyzes the first step in the production of the branched chain amino acids leucine, isoleucine, and valine. In addition, BCAT2 may actn as a transporter of branched chain alpha-keto acids.
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Synonyms
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMASSSF KAADLQLEMT QKPHKKPGPG EPLVFGKTFT DHMLMVEWND KGWGQPRIQP FQNLTLHPAS SSLHYSLQLF EGMKAFKGKD QQVRLFRPWL NMDRMLRSAM RLCLPSFDKL ELLECIRRLI EVDKDWVPDA AGTSLYVRPV LIGNEPSLGV SQPTRALLFV ILCPVGAYFP GGSVTPVSLL ADPAFIRAWV GGVGNYKLGG NYGPTVLVQQ EALKRGCEQV LWLYGPDHQL TEVGTMNIFV YWTHEDGVLE LVTPPLNGVI LPGVVRQSLL DMAQTWGEFR VVERTITMKQ LLRALEEGRV REVFGSGTAC QVCPVHRILY KDRNLHIPTM ENGPELILRF QKELKEIQYG IRAHEWMFPV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
RCN3 HumanDescription:
Reticulocalbin 3 Human Recombinant
Reticulocalbin-3, EF-hand calcium-binding protein RLP49, RCN3, RLP49.
Product # :
PRO-1049Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RCN3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 333 amino acids (21-328 a.a) and having a molecular mass of 37.9kDa.RCN3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RCN3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Reticulocalbin 3 (RCN3) belongs to the CREC (cab45/reticulocalbin/ ERC45/calumenin) family. RCN3 contains 5 Arg-Xaa-Xaa-Arg motifs, which function as target sequences of SPCs (subtilisin-like proprotein convertases), which is a family of serine endoproteases that proteolytically activate proproteins. The synthesis of PACE4 is induced by association and coexpression with RCN3.
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Synonyms
Reticulocalbin-3, EF-hand calcium-binding protein RLP49, RCN3, RLP49.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKPSPD AGPHGQGRVH QAAPLSDAPH DDAHGNFQYD HEAFLGREVA KEFDQLTPEE SQARLGRIVD RMDRAGDGDG WVSLAELRAW IAHTQQRHIR DSVSAAWDTY DTDRDGRVGW EELRNATYGH YAPGEEFHDV EDAETYKKML ARDERRFRVA DQDGDSMATR EELTAFLHPE EFPHMRDIVI AETLEDLDRN KDGYVQVEEY IADLYSAEPG EEEPAWVQTE RQQFRDFRDL NKDGHLDGSE VGHWVLPPAQ DQPLVEANHL LHESDTDKDG RLSKAEILGN WNMFVGSQAT NYGEDLTRHH DEL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.