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1000 results found for “protein-a, a/g”
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Name :
PSG1 HumanDescription:
Pregnancy Specific Beta-1-Glycoprotein 1 Human Recombinant
Pregnancy Specific Beta-1-Glycoprotein 1, PSBG1, B1G1, Fetal Liver Non-Specific Cross-Reactive Antigen 1/2, Pregnancy-Specific Beta-1 Glycoprotein C/D, CD66 Antigen-Like Family Member F, PS-Beta-C/D, PS-Beta-G-1, FL-NCA-1/2, PSBG-1, PSGGA, PSG95, SP1, Pregnancy-Specific Beta-1-Glycoprotein 1, Pregnancy-Specific B-1 Glycoprotein, Pregnancy-Specific Glycoprotein 1, CD66f Antigen, DHFRP2, PSGIIA, CD66f, PBG1, PSG1.
Product # :
PRO-1966Price :
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Shipped with Ice Packs
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Description
PSG1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (35-419) and having a molecular mass of 45.9 kDa.PSG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PSG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Pregnancy Specific Beta-1-Glycoprotein 1 (PSG1) is a member of a subgroup of transcription factors which are phosphorylated upon binding to promoter sequences. PSGs belong to the carcinoembryonic antigen (CEA) family and function as early biochemical markers of syncytiotrophoblast formation. Furthermore, PSG1 is assumed to mediate placental vascular morphogenesis by enhancing VEGF-A production and endothelial tube formation. PSG1 is a major product of the syncytiotrophoblast, reaching concentrations of 100- 290 mg/l at term in the serum of pregnant women.
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Synonyms
Pregnancy Specific Beta-1-Glycoprotein 1, PSBG1, B1G1, Fetal Liver Non-Specific Cross-Reactive Antigen 1/2, Pregnancy-Specific Beta-1 Glycoprotein C/D, CD66 Antigen-Like Family Member F, PS-Beta-C/D, PS-Beta-G-1, FL-NCA-1/2, PSBG-1, PSGGA, PSG95, SP1, Pregnancy-Specific Beta-1-Glycoprotein 1, Pregnancy-Specific B-1 Glycoprotein, Pregnancy-Specific Glycoprotein 1, CD66f Antigen, DHFRP2, PSGIIA, CD66f, PBG1, PSG1.
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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 MGSQVTIEAE PTKVSEGKDV LLLVHNLPQN LTGYIWYKGQ MRDLYHYITS YVVDGEIIIY GPAYSGRETA YSNASLLIQN VTREDAGSYT LHIIKGDDGT RGVTGRFTFT LHLETPKPSI SSSNLNPRET MEAVSLTCDP ETPDASYLWW MNGQSLPMTH SLKLSETNRT LFLLGVTKYT AGPYECEIRN PVSASRSDPV TLNLLPKLPK PYITINNLNP RENKDVLNFT CEPKSENYTY IWWLNGQSLP VSPRVKRPIE NRILILPSVT RNETGPYQCE IRDRYGGIRS DPVTLNVLYG PDLPRIYPSF TYYRSGEVLY LSCSADSNPP AQYSWTINEK FQLPGQKLFI RHITTKHSGL YVCSVRNSAT GKESSKSMTV EVSGKWIP.
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 :
BMP3 HumanDescription:
Bone Morphogenetic protein-3 Human Recombinant
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
Product # :
CYT-937Price :
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Shipped at Room temp
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Description
BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.More Info
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Introduction
Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.
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Synonyms
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
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Background
Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration
Abstract:
Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.
Production of BMP-3 Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.
Potential Therapeutic Applications:
BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.
Conclusion:
BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.
What is the molecular weight/Mw of BMP3 Protein?
BMP3 Protein has a total Mw of 24.8kDa.
What is the source or expression system of BMP3 Protein?
Escherichia Coli.
What is the Purity of BMP3 Protein?
BMP3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP3 Protein?
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.
What is the amino acid sequence of BMP3 Protein?
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
What applications can BMP3 Protein be used in?
BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP3 Protein?
The endotoxin level is minimal, BMP3 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 :
APIP HumanDescription:
APAF1 interacting protein Human Recombinant
APAF1 interacting protein, CGI-29, APIP2, Mmrp19, APAF1-interacting protein, MTRu-1-P dehydratase, probable methylthioribulose-1-phosphate dehydratase, CGI29, EC 4.2.1.109, dJ179L10.2, MMRP19.
Product # :
PRO-1186Price :
Quantity :
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Shipped with Ice Packs
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Description
APIP Human Recombinant produced E. coli is a single polypeptide chain containing 266 amino acids (1-242) and having a molecular mass of 29.7kDa.APIP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The APIP solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
APIP catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). APIP has an anti-apoptotic function and inhibits muscle ischemic impairment. APIP inhibits the cytochrome c-dependent and APAF1-mediated cell death.
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Synonyms
APAF1 interacting protein, CGI-29, APIP2, Mmrp19, APAF1-interacting protein, MTRu-1-P dehydratase, probable methylthioribulose-1-phosphate dehydratase, CGI29, EC 4.2.1.109, dJ179L10.2, MMRP19.
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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 MGSHMSGCDA REGDCCSRRC GAQDKEHPRY LIPELCKQFY HLGWVTGTGG GISLKHGDEI YIAPSGVQKE RIQPEDMFVC DINEKDISGP SPSKKLKKSQ CTPLFMNAYT MRGAGAVIHT HSKAAVMATL LFPGREFKIT HQEMIKGIKK CTSGGYYRYD DMLVVPIIEN TPEEKDLKDR MAHAMNEYPD SCAVLVRRHG VYVWGETWEK AKTMCECYDY LFDIAVSMKK VGLDPSQLPV GENGIV
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 :
TPA (311-562) HumanDescription:
Tissue Plasminogen Activator (311-562 a.a.) Human Recombinant
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
Product # :
ENZ-1023Price :
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Shipped with Ice Packs
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Description
TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 261 amino acids (311-562 a.a.) and having a molecular mass of 29.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).TPA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TPA protein solution (0.5mg/ml) contains 50mM MES (pH 5.0), 5mM CaCl2, 1mM DTT, 0.5M NaCl and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. -
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
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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
ADPIKGGLFA DIASHPWQAA IFAKHRRSPG ERFLCGGILI SSCWILSAAH CFQERFPPHH LTVILGRTYR VVPGEEEQKF EVEKYIVHKE FDDDTYDNDI ALLQLKSDSS RCAQESSVVR TVCLPPADLQ LPDWTECELS GYGKHEALSP FYSERLKEAH VRLYPSSRCT SQHLLNRTVT DNMLCAGDTR SGGPQANLHD ACQGDSGGPL VCLNDGRMTL VGIISWGLGC GQKDVPGVYT KVTNYLDWIR DNMRPHHHHH H.
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 :
Colloidal GoldDescription:
Colloidal Gold 40nM 2OD
Product # :
PRO-2830Price :
Quantity :
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Shipped with Ice Packs
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Description
Gold nanoparticles have one-of-a-kind properties turn them to ideal for detecting even the smallest amounts of biological molecules. These particles can be loaded with drugs or other therapeutic agents and then targeted to specific cells/tissues. Further to their diagnostic applications, gold nanoparticles may also take part in drug delivery and cancer therapy. Colloidal Gold is purified by proprietary chromatographic techniques.
Formulation
Colloidal Gold solution (6.7mg/ml) contains 50mM sodium citrate.
More Info
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Physical Appearance
Sterile Filtered red solution.
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Stability
Colloidal Gold should be stored at 4°C, DO NOT FREEZE.
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Background
Colloidal gold is liquid form colloid nanoparticles of gold in a water. The colloidal gold color is dependent of the particle size, below 100 nm gives a is deep purple red color due to the spherical nanoparticles. Colloid gold is crucial for research due to its unique properties such as electronic charge, Mw and optical properties. Colloid gold is used in biomedical devices, electron microscopy and nanotechnology.
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 :
HSA Recombinant, HEKDescription:
Human Serum Albumin Recombinant, HEK
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-967Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Serum Albumin produced in HEK cells is a glycosylated monomer, having a molecular weight range of 60-65kDa due to glycosylation.The HSA is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The HSA protein was lyophilized from 0.92mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
More Info
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Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood. -
Synonyms
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized HSA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HSA 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 HSA in sterile 1xPBS.
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 :
OMG HumanDescription:
Oligodendrocyte Myelin Glycoprotein Recombinant Human
Oligodendrocyte-myelin glycoprotein, OMG, OMGP.
Product # :
PRO-2343Price :
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Shipped with Ice Packs
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Description
OMG Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (25-418) and having a molecular mass of 45.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-100kDa).OMG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
OMG protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Oligodendrocyte-myelin glycoprotein (OMG) is a cell membrane protein which contains 8 leucine-rich repeats. The OMG protein is expressed on the surface of oligodendrocytes and on large projection neurons, including Purkinje cells of the cerebellum, pyramidal cells of the hippocampus, motoneurons of the brainstem and anterior horn cells of the spinal cord. The neurite outgrowth inhibitory activities of all three myelin-derived proteins are mediated by binding to a joint receptor complex consisting of the Nogo receptor and the p75 neurotrophin receptor.
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Synonyms
Oligodendrocyte-myelin glycoprotein, OMG, OMGP.
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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
ICPLQCICTE RHRHVDCSGR NLSTLPSGLQ ENIIHLNLSY NHFTDLHNQL TQYTNLRTLD ISNNRLESLP AHLPRSLWNM SAANNNIKLL DKSDTAYQWN LKYLDVSKNM LEKVVLIKNT LRSLEVLNLS SNKLWTVPTN MPSKLHIVDL SNNSLTQILP GTLINLTNLT HLYLHNNKFT FIPDQSFDQL FQLQEITLYN NRWSCDHKQN ITYLLKWMME TKAHVIGTPC STQISSLKEH NMYPTPSGFT SSLFTVSGMQ TVDTINSLSV VTQPKVTKIP KQYRTKETTF GATLSKDTTF TSTDKAFVPY PEDTSTETIN SHEAAAATLT IHLQDGMVTN TSLTSSTKSS PTPMTLSITS GMPNNFSEMP QQSTTLNLWR EETTTNVKTP LPSVEHHHHH H.
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 :
CSTA Human, HisDescription:
Cystatin A Human Recombinant, His tag
Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.
Product # :
PRO-504Price :
Quantity :
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Shipped with Ice Packs
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Description
CSTA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-98 a.a.) and having a molecular mass of 13.1kDa.CSTA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cystatin-A (1mg/ml) in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.
More Info
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Introduction
Cystatin-A is the intracellular inhibitor of cysteine proteinase cathepsin B (CatB) and belongs to family 1 of the cystatin superfamily of inhibitor proteins. CSTA is a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. It has been proposed that extracellular CatB together with other classes of proteinases are all subjected to a cascade-like manner of activation. CatB and its inhibitor Cystatin-A are involved in degradation of extracellular matrix proteins during tissue remodeling. CSTA is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Cystatin-A has been reported to be found in high concentrations in epithelial cells, polymorphonuclear leukocytes and lymphoid tissue. Stefins may be used as prognostic and diagnostic tools for cancer.
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Synonyms
Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.
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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 MIPGGLSEAK PATPEIQEIV DKVKPQLEEK TNETYGKLEA VQYKTQVVAG TNYYIKVRAG DNKYMHLKVF KSLPGQNEDL VLTGYQVDKN KDDELTGF.
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 :
Activin A Human PlantDescription:
Activin A Human Recombinant, Plant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-052Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in Tris HCl 0.05M buffer at pH 7.4.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Activin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin A 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 Activin A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.
What is the source or expression system of Activin A Protein?
Nicotinia
What is the Purity of Activin A Protein?
Activin A Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
The biological functionality of Activin-A Protein will be determined in the future.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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Serological Identification
The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.
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 :
PROSC HumanDescription:
Proline Synthetase Co-Transcribed Human Recombinant
Proline Synthetase Co-Transcribed Homolog (Bacterial), Proline Synthetase Co-Transcribed (Bacterial Homolog), Proline Synthase Co-Transcribed Bacterial Homolog Protein, Proline Synthetase Co-Transcribed Bacterial Homolog Protein, PROSC.
Product # :
PRO-481Price :
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Shipped with Ice Packs
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Description
PROSC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275) and having a molecular mass of 32.7 kDa.PROSC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PROSC solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Proline Synthetase Co-Transcribed (PROSC) is a member of the UPF0001 family.
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Synonyms
Proline Synthetase Co-Transcribed Homolog (Bacterial), Proline Synthetase Co-Transcribed (Bacterial Homolog), Proline Synthase Co-Transcribed Bacterial Homolog Protein, Proline Synthetase Co-Transcribed Bacterial Homolog Protein, PROSC.
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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 MGSMWRAGSM SAELGVGCAL RAVNERVQQA VARRPRDLPA IQPRLVAVSK TKPADMVIEA YGHGQRTFGE NYVQELLEKA SNPKILSLCP EIKWHFIGHL QKQNVNKLMA VPNLFMLETV DSVKLADKVN SSWQRKGSPE RLKVMVQINT SGEESKHGLP PSETIAIVEH INAKCPNLEF VGLMTIGSFG HDLSQGPNPD FQLLLSLREE LCKKLNIPAD QVELSMGMSA DFQHAVEVGS TNVRIGSTIF GERDYSKKPT PDKCAADVKA PLEVAQEH.
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 :
RND1 HumanDescription:
Rho Family GTPase 1 Human Recombinant
Rho family GTPase 1, GTP-binding protein, ras homolog gene family, member S, ARHS, RHOS, rho-related GTP-binding protein Rho6, RHO6, Rnd1, FLJ42294.
Product # :
PRO-893Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RND1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200) and having a molecular mass of 24.5 kDa.The RND1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RND1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
RND1 is a Rho-related GTPases that form a separate branch of the Rho family, since they are different in charge, size, and biochemical properties. RND1 is found in the activated GTP-bound form and performs as a negative regulator of actin assembly and of cell adhesion. RND1 assists in regulation of the organization of the actin cytoskeleton as a reaction to extracellular growth factors.
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Synonyms
Rho family GTPase 1, GTP-binding protein, ras homolog gene family, member S, ARHS, RHOS, rho-related GTP-binding protein Rho6, RHO6, Rnd1, FLJ42294.
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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 MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY TACLETEEQR VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV DSALKKWRTE ILDYCPSTRV LLIGCKTDLR TDLSTLMELS HQKQAPISYE QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF RTASMLCLNK PSPLPQKSPV
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 :
LRPAP1 MouseDescription:
Low Density Lipoprotein Receptor Related Protein Associated Protein 1 Mouse Recombinant
Low density lipoprotein-related protein-associated protein 1 (alpha-2-macroglobulin receptor-associated protein 1), A2MRAP, HBP44, RAP, A2RAP, Alpha-2-MRAP.
Product # :
PRO-2224Price :
Quantity :
Shipping Method :
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Description
LRPAP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (29-360 a.a) and having a molecular mass of 41.4kDa. LRPAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LRPAP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
LRPAP1 is a member of the alpha-2-MRAP family. LRPAP1 cooperates with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330. LRPAP1, located on the cell surface, creates a complex with the alpha 2 macroglobulin receptor light and heavy chains and has part in the pathogenesis of membrane glomerular nephritis.
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Synonyms
Low density lipoprotein-related protein-associated protein 1 (alpha-2-macroglobulin receptor-associated protein 1), A2MRAP, HBP44, RAP, A2RAP, Alpha-2-MRAP.
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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 MGSQPIAGHG GKYSREKNEP EMAAKRESGE EFRMEKLNQL WEKAKRLHLS PVRLAELHSD LKIQERDELN WKKLKVEGLD KDGEKEAKLI HNLNVILARY GLDGRKDAQM VHSNALNEDT QDELGDPRLE KLWHKAKTSG KFSSEELDKL WREFLHYKEK IQEYNVLLDT LSRAEEGYEN LLSPSDMAHI KSDTLISKHS ELKDRLRSIN QGLDRLRKVS HQGYGSTTEF EEPRVIDLWD LAQSANFTEK ELESFREELK HFEAKIEKHN HYQKQLEISH QKLKHVESIG DPEHISRNKE KYVLLEEKTK ELGYKVKKHL QDLSSRVSRA RHNEL.
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 :
GDF10 HumanDescription:
Growth differentiation factor 10 Human Recombinant
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
Product # :
CYT-659Price :
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- sds-page
Description
GDF10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (369-478 a.a.) and having a total molecular mass of 12.5 kDa. GDF10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDF10 solution (1mg/ml) contains 10mM Sodium citrate (pH 3.5), 1mM DTT, 40% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.
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Synonyms
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
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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
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
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Background
What is the molecular weight/Mw of GDF10 HUMAN Protein?
GDF10 HUMAN Protein has a total Mw of 12.5kDa.
What is the source or expression system of GDF10 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF10 HUMAN Protein?
GDF10 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF10 HUMAN Protein?
The biological functionality of GDF10 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF10 HUMAN Protein?
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
What applications can GDF10 HUMAN Protein be used in?
GDF10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF10 HUMAN Protein?
The endotoxin level is minimal, GDF10 HUMAN 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.
- View Data Sheet
Name :
CPPED1 HumanDescription:
Calcineurin-Like Phosphoesterase Domain Containing 1 Human Recombinant
CSTP1, Calcineurin-like phosphoesterase domain-containing protein 1, Complete S-transactivated protein 1, CPPED1.
Product # :
PRO-1500Price :
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Description
CPPED1 Human Recombinant produced in E. coli is a single polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 37.9kDa. CPPED1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CPPED1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CPPED1 which is a part of the metallophosphoesterase superfamily takes part in glucose uptake by adipocytes. CPPED1 binds two divalent metal cations and is transactivated by the great envelope protein of the hepatitis B virus.
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Synonyms
CSTP1, Calcineurin-like phosphoesterase domain-containing protein 1, Complete S-transactivated protein 1, CPPED1.
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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 MGSMSAAEAG GVFHRARGRT LAAFPAEKES EWKGPFYFIL GADPQFGLIK AWSTGDCDNG GDEWEQEIRL TEQAVQAINK LNPKPKFFVL CGDLIHAMPG KPWRTEQTED LKRVLRAVDR AIPLVLVSGN HDIGNTPTAE TVEEFCRTWG DDYFSFWVGG VLFLVLNSQF YENPSKCPSL KQAQDQWLDE QLSIARQRHC QHAIVFQHIP LFLESIDEDD DYYFNLSKST RKKLADKFIH AGVKVVFSGH YHRNAGGTYQ NLDMVVSSAI GCQLGRDPHG LRVVVVTAEK IVHRYYSLDE LSEKGIEDDL MDLIKKK.
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 :
VAV1 HumanDescription:
Vav 1 Guanine Nucleotide Exchange Factor Human Recombinant
Vav 1 Guanine Nucleotide Exchange Factor, VAV, Vav 1 Oncogene, Proto-Oncogene Vav.
Product # :
PRO-1764Price :
Quantity :
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Description
VAV1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (189-565a.a) and having a molecular mass of 46.8kDa.VAV1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VAV1 protein solution (0.25mg/ml) containing In 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Vav 1 Guanine Nucleotide Exchange Factor (VAV1), belongs to the VAV gene family. The VAV1 proteins are guanine nucleotide exchange factors (GEFs) for Rho family GTPases which activate pathways leading to actin cytoskeletal rearrangements and transcriptional alterations. VAV1 is essential in hematopoiesis, taking part in T-cell and B-cell development and activation. VAV1 has been identified as the specific binding partner of Nef proteins from HIV-1. In addition, VAV1 contains an SH2 domain, which could show its function as a substrate for tyrosine kinases. Expression of VAV1 is limited solely to cells of hematopoietic origin, as well as those of the erythroid, lymphoid and myeloid lineages. Among the diseases associated with VAV1 are cherubism, and hiv-1.
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Synonyms
Vav 1 Guanine Nucleotide Exchange Factor, VAV, Vav 1 Oncogene, Proto-Oncogene Vav.
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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 MGSMTEYDKR CCCLREIQQT EEKYTDTLGS IQQHFLKPLQ RFLKPQDIEI IFINIEDLLR VHTHFLKEMK EALGTPGAAN LYQVFIKYKE RFLVYGRYCS QVESASKHLD RVAAAREDVQ MKLEECSQRA NNGRFTLRDL LMVPMQRVLK YHLLLQELVK HTQEAMEKEN LRLALDAMRD LAQCVNEVKR DNETLRQITN FQLSIENLDQ SLAHYGRPKI DGELKITSVE RRSKMDRYAF LLDKALLICK RRGDSYDLKD FVNLHSFQVR DDSSGDRDNK KWSHMFLLIE DQGAQGYELF FKTRELKKKW MEQFEMAISN IYPENATANG HDFQMFSFEE TTSCKACQML LRGTFYQGYR CHRCRASAHK ECLGRVPPCG
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 :
TYRP1 HumanDescription:
Tyrosinase Related Protein 1 Human Recombinant
Tyrosinase Related Protein 1, Tyrosinase-Related Protein 1, Melanoma Antigen Gp75, Glycoprotein 75, DHICA Oxidase, Catalase B, CAS2, TRP1, TYRP, TRP, 5,6-Dihydroxyindole-2-Carboxylic Acid Oxidase, EC 1.14.18.1, EC 1.14.18.-, EC 1.14.18, B-PROTEIN, TRP-1, TYRRP, CATB, GP75, OCA3, 5,6-dihydroxyindole-2-carboxylic acid oxidase.
Product # :
PRO-2350Price :
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Description
TYRP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 462 amino acids (25-477a.a) and having a molecular mass of 52.5kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).TYRP1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TYRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TYRP1, also known as 5, 6-dihydroxyindole-2-carboxylic acid oxidase, is a melanosomal enzyme which is a member of the tyrosinase family and takes a significant part in the melanin biosynthetic pathway. TYRP1 is a melanocyte-specific gene which is involved in eumelanin synthesis. Furthermore, TYRP1 is implicated in the oxidation of 5,6-dihydroxyindole-2-carboxylic acid-DHICA into indole-5,6-quinone-2-carboxylic acid. TYRP1 is regulated by the microphthalmia-associatedtranscription factor-MITF.
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Synonyms
Tyrosinase Related Protein 1, Tyrosinase-Related Protein 1, Melanoma Antigen Gp75, Glycoprotein 75, DHICA Oxidase, Catalase B, CAS2, TRP1, TYRP, TRP, 5,6-Dihydroxyindole-2-Carboxylic Acid Oxidase, EC 1.14.18.1, EC 1.14.18.-, EC 1.14.18, B-PROTEIN, TRP-1, TYRRP, CATB, GP75, OCA3, 5,6-dihydroxyindole-2-carboxylic acid oxidase.
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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
ADLQFPRQCA TVEALRSGMC CPDLSPVSGP GTDRCGSSSG RGRCEAVTAD SRPHSPQYPH DGRDDREVWP LRFFNRTCHC NGNFSGHNCG TCRPGWRGAA CDQRVLIVRR NLLDLSKEEK NHFVRALDMA KRTTHPLFVI ATRRSEEILG PDGNTPQFEN ISIYNYFVWT HYYSVKKTFL GVGQESFGEV DFSHEGPAFL TWHRYHLLRL EKDMQEMLQE PSFSLPYWNF ATGKNVCDIC TDDLMGSRSN FDSTLISPNS VFSQWRVVCD SLEDYDTLGT LCNSTEDGPI RRNPAGNVAR PMVQRLPEPQ DVAQCLEVGL FDTPPFYSNS TNSFRNTVEG YSDPTGKYDP AVRSLHNLAH LFLNGTGGQT HLSPNDPIFV LLHTFTDAVF DEWLRRYNAD ISTFPLENAP IGHNRQYNMV PFWPPVTNTE MFVTAPDNLG YTYEIQWPSR EFSVPEHHHH HH.
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 :
RTN4R HumanDescription:
Reticulon 4 Receptor Human Recombinant
Reticulon 4 Receptor, Nogo-66 Receptor, Nogo Receptor, NOGOR, NGR , Reticulon-4 Receptor, UNQ330/PRO526.
Product # :
PRO-2353Price :
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Description
RTN4R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 429 amino acids (27-447 a.a.) and having a molecular mass of 46.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57 kDa). RTN4R is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RTN4R protein solution (0.5mg/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
Reticulon 4 Receptor, also known as RTN4R, plays a role as a receptor for RTN4, OMG and MAG. RTN4R is a glycosylphosphoinositol (GPI)-anchored protein which is a part from the Nogo recptor family. RTN4R is expressed mainly in neurons and their axons and is regulates axonal regeneration and plasticity in the adult central nervous system. RTN4R is a potential drug target for treating various neurological cases such as spinal cord injury, CNS lesions, stroke and Alzheimer's disease.
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Synonyms
Reticulon 4 Receptor, Nogo-66 Receptor, Nogo Receptor, NOGOR, NGR , Reticulon-4 Receptor, UNQ330/PRO526.
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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
CPGACVCYNE PKVTTSCPQQ GLQAVPVGIP AASQRIFLHG NRISHVPAAS FRACRNLTIL WLHSNVLARI DAAAFTGLAL LEQLDLSDNA QLRSVDPATF HGLGRLHTLH LDRCGLQELG PGLFRGLAAL QYLYLQDNAL QALPDDTFRD LGNLTHLFLH GNRISSVPER AFRGLHSLDR LLLHQNRVAH VHPHAFRDLG RLMTLYLFAN NLSALPTEAL APLRALQYLR LNDNPWVCDC RARPLWAWLQ KFRGSSSEVP CSLPQRLAGR DLKRLAANDL QGCAVATGPY HPIWTGRATD EEPLGLPKCC QPDAADKASV LEPGRPASAG NALKGRVPPG DSPPGNGSGP RHINDSPFGT LPGSAEPPLT AVRPEGSEPP GFPTSGPRRR PGCSRKNRTR SHCRLGQAGS GGGGTGDSEG SLEHHHHHH.
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 :
CRMP1 HumanDescription:
Collapsin Response Mediator Protein-1 Human Recombinant
Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, CRMP1, DPYSL1, DRP1.
Product # :
PRO-493Price :
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Description
CRMP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 597 amino acids (1-572 a.a) and having a molecular mass of 64.8kDa (Will appear as multiple bands on SDS-PAGE).CRMP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRMP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol, 1mM DTT and 0.2mM PMSF.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The X-ray crystal structure of murine CRMP1 was determined at 2.1 resolution and demonstrates that CRMP1 is a bilobed ‘lung-shaped’ protein forming a tetrameric assembly.
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Synonyms
Dihydropyrimidinase-related protein 1, DRP-1, Collapsin response mediator protein 1, CRMP-1, CRMP1, DPYSL1, DRP1.
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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 MGSEFMSYQG KKSIPHITSD RLLIKGGRII NDDQSLYADV YLEDGLIKQI GENLIVPGGV KTIEANGRMV IPGGIDVNTY LQKPSQGMTA ADDFFQGTRA ALVGGTTMII DHVVPEPGSS LLTSFEKWHE AADTKSCCDY SLHVDITSWY DGVREELEVL VQDKGVNSFQ VYMAYKDVYQ MSDSQLYEAF TFLKGLGAVI LVHAENGDLI AQEQKRILEM GITGPEGHAL SRPEELEAEA VFRAITIAGR INCPVYITKV MSKSAADIIA LARKKGPLVF GEPIAASLGT DGTHYWSKNW AKAAAFVTSP PLSPDPTTPD YLTSLLACGD LQVTGSGHCP YSTAQKAVGK DNFTLIPEGV NGIEERMTVV WDKAVATGKM DENQFVAVTS TNAAKIFNLY PRKGRIAVGS DADVVIWDPD KLKTITAKSH KSAVEYNIFE GMECHGSPLV VISQGKIVFE DGNINVNKGM GRFIPRKAFP EHLYQRVKIR NKVFGLQGVS RGMYDGPVYE VPATPKYATP APSAKSSPSK HQPPPIRNLH QSNFSLSGAQ IDDNNPRRTG HRIVAPPGGR SNITSLG.
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 :
HSPB11 HumanDescription:
Heat Shock Protein Family B Member 11 Human Recombinant
Heat shock protein beta-11, Hspb11, Placental protein 25, PP25, C1orf41, HSPC034, IFT25.
Product # :
HSP-046Price :
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Description
HSPB11 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa (Molecular weight on SDS-PAGE will appear higher).HSPB11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSPB11 protein (1mg/ml) solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HSPB11 is a component of IFT complex B composed of IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20. HSPB11 is detected in the placenta.
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Synonyms
Heat shock protein beta-11, Hspb11, Placental protein 25, PP25, C1orf41, HSPC034, IFT25.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
HSPB11 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRKIDLCLSS EGSEVILATS SDEKHPPENI IDGNPETFWT TTGMFPQEFI ICFHKHVRIE RLVIQSYFVQ TLKIEKSTSK EPVDFEQWIE KDLVHTEGQL QNEEIVAHDG SATYLRFIIV SAFDHFASVH SVSAEGTVVS NLSS.
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 :
CALB1 HumanDescription:
Calbindin-1 Human Recombinant
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, CALB1, CAB27, CALB, calbindin 1 28kDa.
Product # :
PRO-721Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CALB1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261 amino acids (1-261 a.a.) and having a molecular mass of 30kDa.The CALB1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CALB1 protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 10% glycerol and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Calbindin 1 (CALB1) is a calcium binding protein that is a member of the troponin C superfamily. CALB1 plays a vital role in calcium regulation (including calcium transport and uptake, calcification of bone and teeth) and calcium associated signaling in neurons and transiently in embryological development. CALB1 also has a role in protecting neurons from apoptotic cell death. CALB1 buffers cytosolic calcium and may stimulate a membrane Ca2+-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. The biological function of CALB1 seems to be tied to the redox state of its five cysteine residues.
CALB1 has 4 active calcium-binding domains, and 2 modified domains that seemingly have lost their calcium-binding ability. CALB1 is expressed in neural tissues. In the brain, the CALB1 synthesis is independent of vitamin-D-derived hormones.
Disregulation of the CALB1 is associated with epilepsy, amyotrophic lateral sclerosis, Huntington's disease. The neurons in brains of Huntington disease patients are calbindin-depleted. -
Synonyms
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, CALB1, CAB27, CALB, calbindin 1 28kDa.
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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
MAESHLQSSL ITASQFFEIW LHFDADGSGY LEGKELQNLI QELQQARKKA GLELSPEMKT FVDQYGQRDD GKIGIVELAH VLPTEENFLL LFRCQQLKSC EEFMKTWRKY DTDHSGFIET EELKNFLKDL LEKANKTVDD TKLAEYTDLM LKLFDSNNDG KLELTEMARL LPVQENFLLK FQGIKMCGKE FNKAFELYDQ DGNGYIDENE LDALLKDLCE KNKQDLDINN ITTYKKNIMA LSDGGKLYRT DLALILCAGD N.
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 :
RPL26 HumanDescription:
Ribosomal Protein L26 Human Recombinant
L26, Ribosomal Protein L26, 60S Ribosomal Protein L26.
Product # :
PRO-1538Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RPL26 Human Recombinant produced in E. coli is a single polypeptide chain containing 168 amino acids (1-145) and having a molecular mass of 19.6kDa. RPL26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPL26 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Ribosomal Protein L26 (RPL26) is a ribosomal protein which is a component of the 60S subunit (the large subunit of the ribosome). RPL26 is a part of the L24P family of ribosomal proteins which is located in the cytoplasm. There are numerous processed pseudogenes of RPL26 dispersed through the genome as usual for genes encoding ribosomal proteins.
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Synonyms
L26, Ribosomal Protein L26, 60S Ribosomal Protein L26.
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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 MGSMKFNPFV TSDRSKNRKR HFNAPSHIRR KIMSSPLSKE LRQKYNVRSM PIRKDDEVQV VRGHYKGQQI GKVVQVYRKK YVIYIERVQR EKANGTTVHV GIHPSKVVIT RLKLDKDRKK ILERKAKSRQ VGKEKGKYKE ETIEKMQE.
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 :
ARL6 HumanDescription:
ADP-Ribosylation Factor-Like 6 Human Recombinant
ADP-ribosylation factor-like 6, Bardet-Biedl syndrome 3 protein, BBS3, RP55, MGC32934.
Product # :
PRO-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARL6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-186a.a) and having a molecular mass of 23.2kDa.ARL6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARL6 protein solution (0.5mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.2M NaCl and 5mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ARL6 is a member of the ARF family of GTP-binding proteins. ARL6 has a vital part in modulating membrane trafficking and cytoskeletal functions. Mutation in ARL6 is the source of Bardet-Biedl syndrome (BBS3) which is a pleiotropic genetic disorder that causes obesity, photoreceptor degeneration, polydactyly, hypogenitalism, renal abnor-malities and developmental delay.
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Synonyms
ADP-ribosylation factor-like 6, Bardet-Biedl syndrome 3 protein, BBS3, RP55, MGC32934.
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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 MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ IQTVKT.
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 :
PCMTD1 HumanDescription:
Protein-L-Isoaspartate O-Methyltransferase 1 Human Recombinant
Protein-L-isoaspartate O-methyltransferase domain-containing protein 1, PCMTD1.
Product # :
PRO-1809Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PCMTD1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 243 amino acids (1-220) and having a molecular mass of 27kDa. PCMTD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PCMTD1 solution (0.25mg/ml) contains 20mM Tris-HCl (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Protein-L-Isoaspartate O-Methyltransferase 1, also known as PCMTD1, is a part of the methyltransferase superfamily and is situated in the cytoplasm.
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Synonyms
Protein-L-isoaspartate O-methyltransferase domain-containing protein 1, PCMTD1.
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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 MGSMGGAVSA GEDNDDLIDN LKEAQYIRTE RVEQAFRAID RGDYYLEGYR DNAYKDLAWK HGNIHLSAPC IYSEVMEALK LQPGLSFLNL GSGTGYLSTM VGLILGPFGI NHGIELHSDV VEYAKEKLES FIKNSDSFDK FEFCEPAFVV GNCLQIASDS HQYDRIYCGA GVQKDHENYM KILLKVGGIL VMPIEDQLTQ IMRTGQNTWE SKNILAVSFA PLV.
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 :
PFDN4 HumanDescription:
Prefoldin Subunit 4 Recombinant Human
Prefoldin Subunit 4, PFD4, C1, Prefoldin 4, Protein C-1.
Product # :
PRO-092Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PFDN4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-134.a.a) and having a molecular mass of 17.4kDa. PFDN4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFDN4 protein solution (1mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH7.5), 50mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
PFDN4 belongs to the prefoldin beta subunit family. PFDN4 is a heterohexameric chaperone protein that can capture unfolded actin and is a possible transcription factor. Six prefoldin polypeptides, prefoldin 1-6, are known.
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Synonyms
Prefoldin Subunit 4, PFD4, C1, Prefoldin 4, Protein C-1.
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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 MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI EVKKKQLQNL EDACDDIMLA DDDCLMIPYQ IGDVFISHSQ EETQEMLEEA KKNLQEEIDA LESRVESIQR VLADLKVQLY AKFGSNINLE ADES
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.