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1000 results found for “LHRH”
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Name :
MRRF HumanDescription:
Mitochondrial Ribosome Recycling Factor Human Recombinant
MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.
Product # :
PRO-1299Price :
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Description
MRRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (56-262 a.a.) and having a molecular mass of 25.1kDa.MRRF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MRRF protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
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Introduction
Mitochondrial Ribosome Recycling Factor (MRRF) is a member of the RRF family. MRRF attaches to the large ribosomal subunit in the cleft which has a peptidyl transferase center. MRRF controls the release of ribosome from messenger RNA at the termination of protein biosynthesis. Also, it may intensify the efficacy of translation by recycling ribosome from one round of translation to another.
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Synonyms
MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.
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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 MATKKAKAKG KGQSQTRVNI NAALVEDIIN LEEVNEEMKS VIEALKDNFN KTLNIRTSPG SLDKIAVVTA DGKLALNQIS QISMKSPQLI LVNMASFPEC TAAAIKAIRE SGMNLNPEVE GTLIRVPIPQ VTREHREMLV KLAKQNTNKA KDSLRKVRTN SMNKLKKSKD TVSEDTIRLI EKQISQMADD TVAELDRHLA VKTKELLG.
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 :
SDR16C5 HumanDescription:
Short Chain Dehydrogenase/Reductase Family 16C, Member 5 Human Recombinant
RDH#2, RDH-E2, RDHE2, Epidermal retinol dehydrogenase 2, EPHD-2, Retinal short-chain dehydrogenase reductase 2, retSDR2, Short-chain dehydrogenase/reductase family 16C member 5, SDR16C5.
Product # :
PRO-1385Price :
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Description
SDR16C5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (32-269 a.a.) and having a molecular mass of 28.3kDa. SDR16C5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SDR16C5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
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Introduction
Short chain dehydrogenase/reductase family 16C, member5 (SDR16C5) is active in the oxidative direction as well as in the reductive one. SDR16C5 oxidizes all-trans-retinol in all-trans-retinaldehyde. No activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH.
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Synonyms
RDH#2, RDH-E2, RDHE2, Epidermal retinol dehydrogenase 2, EPHD-2, Retinal short-chain dehydrogenase reductase 2, retSDR2, Short-chain dehydrogenase/reductase family 16C member 5, SDR16C5.
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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 MGSPKPRKNV AGEIVLITGA GSGLGRLLAL QFARLGSVLV LWDINKEGNE ETCKMAREAG ATRVHAYTCD CSQKEGVYRV ADQVKKEVGD VSILINNAGI VTGKKFLDCP DELMEKSFDV NFKAHLWTYK AFLPAMIAND HGHLVCISSS AGLSGVNGLA DYCASKFAAF GFAESVFVET FVQKQKGIKT TIVCPFFIKT GMFEGCTTGC PSLLPILEPK YAVEKIVEAI LQEKMYLYMP K.
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 :
HRPDescription:
Horseradish Peroxidase
Horseradish Peroxidase, HRP, EC 1.11.1.7.
Product # :
ENZ-321Price :
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Description
HRP consists of the basic isoenzyme having a molecular weight of 44 kDa.The Horseradish Peroxidase is purified by affinity chromatography, which results in an enzyme of high specific activity and purity.
Source
Root extracts of horseradish.
Purity
(A403/A275) = RZ: 3.0.
Biological Activity
276 U/mg (25°C, guaiacol as the hydrogen donor, pH-7 and H2O2 as substrates).
Citations
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Introduction
The enzyme horseradish peroxidase, found in horseradish, is used extensively in molecular biologyand in antibody amplification and detection, among other things. For example, "In recent years the technique of marking neurons with the enzyme horseradish peroxidase (HRP) has become a major tool. In its brief history, this method has probably been used by more neurobiologists than have used the Golgi stainsince its discovery in 1870." Horseradish peroxidase is also highly used in techniques such as Western blottingand ELISAs.
HRP is widely used as an enzymatic label in immunoassays. Usually, the enzyme is coupled to antibodies, lectins or haptens. Coupling to antibodies etc. may be performed through the carbohydrate side chains of the HRP. -
Synonyms
Horseradish Peroxidase, HRP, EC 1.11.1.7.
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Physical Appearance
Sterile Filtered red-brown lyophilized powder.
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Stability
Lyophilized HRP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HRP should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized HRP in sterile 18MΩ-cm H2O not less than 100 µg/ml.
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 :
SH3GL3 HumanDescription:
SH3-Domain GRB2-Like 3 Human Recombinant
SH3-Domain GRB2-Like 3, SH3 Domain-Containing GRB2-Like Protein 3, SH3 Domain Protein 2C, Endophilin-3, EEN-B2, SH3D2C, CNSA3, Endophilin-A3, HsT19371, SH3P13, EEN-2B-L3.
Product # :
PRO-2159Price :
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Description
SH3GL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 370 amino acids (1-347 a.a) and having a molecular mass of 41.7kDa. SH3GL3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SH3GL3 protein solution (1mg/ml) containing PBS (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SH3-Domain GRB2-Like 3, also known as SH3GL3, is a part of the endophilin family. SH3GL3 contains 1 BAR domain and 1 SH3 domain and takes part in endocytosis. SH3GL3 is a protein coding gene which drafts proteins with high curvature to membranes.
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Synonyms
SH3-Domain GRB2-Like 3, SH3 Domain-Containing GRB2-Like Protein 3, SH3 Domain Protein 2C, Endophilin-3, EEN-B2, SH3D2C, CNSA3, Endophilin-A3, HsT19371, SH3P13, EEN-2B-L3.
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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 MGSMSVAGLK KQFHKASQLF SEKISGAEGT KLDDEFLDME RKIDVTNKVV AEILSKTTEY LQPNPAYRAK LGMLNTVSKI RGQVKTTGYP QTEGLLGDCM LKYGKELGED STFGNALIEV GESMKLMAEV KDSLDINVKQ TFIDPLQLLQ DKDLKEIGHH LKKLEGRRLD YDYKKKRVGK IPDEEVRQAV EKFEESKELA ERSMFNFLEN DVEQVSQLAV FIEAALDYHR QSTEILQELQ SKLQMRISAA SSVPRREYKP RPVKRSSSEL NGVSTTSVVK TTGSNIPMDQ PCCRGLYDFE PENQGELGFK EGDIITLTNQ IDENWYEGMI HGESGFFPIN YVEVIVPLPQ.
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 :
SRGN HumanDescription:
Serglycin Human Recombinant
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
Product # :
PRO-965Price :
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Description
SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.
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Synonyms
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
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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 MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.
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 :
BLVRB HumanDescription:
Biliverdin Reductase B Human Recombinant
FLR, BVRB, SDR43U1, MGC117413, BLVRB, Flavin reductase, FR, NADPH-dependent diaphorase, NADPH-flavin reductase, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, Green heme-binding protein, GHBP.
Product # :
ENZ-387Price :
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Description
BLVRB Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids having a molecular mass of 22.1 kDa.The BLVRB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl buffer pH 8.5, 10% glycerol, and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.
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Synonyms
FLR, BVRB, SDR43U1, MGC117413, BLVRB, Flavin reductase, FR, NADPH-dependent diaphorase, NADPH-flavin reductase, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, Green heme-binding protein, GHBP.
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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
MAVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV VVGDVLQAAD VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA HGVDKVVACT SAFLLWDPTK VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD LGHFMLRCLT TDEYDGHSTY PSHQYQ.
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 7 Human, HisDescription:
Bone Morphogenetic Protein-7 Human Recombinant, His Tag
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
Product # :
CYT-629Price :
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Description
BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
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Synonyms
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
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Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK
Abstract:
Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.8kDa.
What is the source or expression system of BMP7 Protein?
Escherichia Coli.
What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.
What is the amino acid sequence of BMP7 Protein?
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 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 :
LCN2 Human, PichiaDescription:
Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant, Pichia
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
Product # :
ENZ-064Price :
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Shipped at Room temp
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Description
Neutrophil Gelatinase Associated Lipocalin Human Recombinant is expressed in Pichia pastoris having a molecular weight of approximately 21kDa.The LCN2 is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
LCN2 was lyophilized from 0.02M NH4HCO3.
Purity
Greater than 96% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke. -
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LCN2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCN2 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 LCN2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
YWHAQ HumanDescription:
Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta Human Recombinant
14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.
Product # :
PKA-254Price :
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Description
YWHAQ Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-245) and having a molecular mass of 27 kDa. YWHAQ is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YWHAQ solution containing 20mM Tris 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, ?, ?, ?, ?, ?, ? and ? that have been identified in mammals. The 14-3-3 tau, a subtype of the 14-3-3 family of proteins, was found in T Cells, brain and testes. This 14-3-3 tau is upregulated in patients with amyotrophic lateral sclerosis.
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Synonyms
14-3-3 theta, 14-3-3 tau, 14-3-3 T-cell, HS1, YWHAQ, 1C5, 14-3-3 Tau, Tyr-3/Trp- 5 Monooxygenase Activation Protein Theta.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
YWHAQ 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
MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWRVISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLKMKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYEILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN.
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 :
RP9 HumanDescription:
Retinitis Pigmentosa 9 Human Recombinant
Retinitis pigmentosa 9 protein, Pim-1-associated protein, PAP-1, RP9.
Product # :
PRO-1314Price :
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Description
RP9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-155 a.a.) and having a molecular mass of 20.7kDa.RP9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RP9 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Retinitis pigmentosa 9 (RP9) is assumed to be a target protein for the PIM1 kinase. The RP9 protein may have some roles in B-cell proliferation in association with PIM1. RP9 can be bound and phosphorylated by the protooncogene PIM1 product, a serine/threonine protein kinase. RP9 localizes in nuclear speckles containing the splicing factors, and has a part in pre-mRNA splicing. RP9 gene mutations result in autosomal dominant retinitis pigmentosa-9.
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Synonyms
Retinitis pigmentosa 9 protein, Pim-1-associated protein, PAP-1, RP9.
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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 MGSMSSRPGR EDVGAAGARR PREPPEQELQ RRREQKRRRH DAQQLQQLKH LESFYEKPPP GLIKEDETKP EDCIPDVPGN EHAREFLAHA PTKGLWMPLG KEVKVMQCWR CKRYGHRTGD KECPFFIKGN QKLEQFRVAH EDPMYDIIRD NKRHEKDV.
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 :
LFA 3 HumanDescription:
Lymphocyte Function Associated Antigen-3 Human Recombinant , Fusion Protein
CD58, LFA-3, Ag3, Surface glycoprotein LFA-3.
Product # :
CYT-423Price :
Quantity :
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Shipped at Room temp
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Description
Lymphocyte Function-Associated Antigen-3 Fusion Protein Recombinant Human is produced by recombinant DNA technology in a Chinese Hamster Ovary (CHO) mammalian cell expression system. The molecular weight is 91.4 kDa. Recombinant LFA3 is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary.
Formulation
Each mg of CD58 contains 0.8mg sucrose, 0.3mg glycine, 0.25mg sodium citrate dihydrate, and 4µg citric acid monohydrate.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
LFA-3 is ligand of the t-lymphocyte cd2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and dependent interactions of t-lymphocytes with target cells and antigen- presenting cells and the t-lymphocyte rosetting with erythrocytes. In addition, the lfa-3/cd2 interaction may prime response by both the cd2+ and lfa-3+ cells.
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Synonyms
CD58, LFA-3, Ag3, Surface glycoprotein LFA-3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LFA3 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human LFA-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 LFA-3 Human in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
Holo Transferrin HumanDescription:
Holo Transferrin Human Recombinant
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Product # :
PRO-2844Price :
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Shipped at Room temp
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Description
Human Holo Transferrin Recombinant produced in HEK Cells is a glycosylated polypeptide containing 679 amino acids and having a Mw of of 76 kDa.
Source
HEK Cells
Formulation
The protein was lyophilized from 1x PBS pH-7.4.
Purity
Protein is >98% pure as determined by 10% PAGE (coomassie staining).
Biological Activity
The activity of Recombinant Holo Transferrin was determined by the proliferation assay using MDCK cells stimulated with recombinant human Holo Transferrin. The protein was found biologically activesds-page, activity
Citations
More Info
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Introduction
Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.
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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Holo Transferrin recombinant between 2-8°C, do not freeze.
Upon reconstitution Holo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Holo Transferrin recombinant in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VPDKTVRWCA VSEHEATKCQ SFRDHMKSVI PSDGPSVACV KKASYLDCIR AIAANEADAV TLDAGLVYDA YLAPNNLKPV VAEFYGSKED PQTFYYAVAV VKKDSGFQMN QLRGKKSCHT GLGRSAGWNI PIGLLYCDLP EPRKPLEKAV ANFFSGSCAP CADGTDFPQL CQLCPGCGCS TLNQYFGYSG AFKCLKDGAG DVAFVKHSTI FENLANKADR DQYELLCLDN TRKPVDEYKD CHLAQVPSHT VVARSMGGKE DLIWELLNQA QEHFGKDKSK EFQLFSSPHG KDLLFKDSAH GFLKVPPRMD AKMYLGYEYV TAIRNLREGT CPEAPTDECK PVKWCALSHH ERLKCDEWSV NSVGKIECVS AETTEDCIAK IMNGEADAMS LDGGFVYIAG KCGLVPVLAE NYNKSDNCED TPEAGYFAVA VVKKSASDLT WDNLKGKKSC HTAVGRTAGW NIPMGLLYNK INHCRFDEFF SEGCAPGSKK DSSLCKLCMG SGLNLCEPNN KEGYYGYTGA FRCLVEKGDV AFVKHQTVPQ NTGGKNPDPW AKNLNEKDYE LLCLDGTRKP VEEYANCHLA RAPNHAVVTR KDKEACVHKI LRQQQHLFGS NVTDCSGNFC LFRSETKDLL FRDDTVCLAK LHDRNTYEKY LGEEYVKAVG NLRKCSTSSL LEACTFRRP.
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 :
HMGA2 HumanDescription:
High Mobility Group AT-Hook 2 Human Recombinant
High Mobility Group AT-Hook 2, HMGIC, High-Mobility Group (Nonhistone Chromosomal) Protein Isoform I-C, High Mobility Group AT-Hook Protein, BABL, HMGI-C, LIPO, STQTL9, High Mobility Group Protein HMGI-C, HMGA2.
Product # :
PRO-1469Price :
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Description
HMGA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (1-109 a.a) and having a molecular mass of 12.8kDa.HMGA2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMGA2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 250mM Imidazole.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
High Mobility Group AT-Hook 2 (HMGA2) is a member of the non-histone chromosomal high mobility group (HMG) family. HMG proteins perform as architectural factors and are necessary components of the enhancesome. Thisprotein contains structural DNA-binding domains and may function as a transcriptional regulating factor. In addition, identification ofthe deletion, amplification, and rearrangement of this gene that are associated with myxoid liposarcoma proposes arole in adipogenesis and mesenchymal differentiation. A gene knock out study of the mouse counterpartdemonstrated that this gene is implicated in diet-induced obesit.Among the Diseases associated with HMGA2 are diffuse lipomatosis, and 12q14 microdeletion syndrome.
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Synonyms
High Mobility Group AT-Hook 2, HMGIC, High-Mobility Group (Nonhistone Chromosomal) Protein Isoform I-C, High Mobility Group AT-Hook Protein, BABL, HMGI-C, LIPO, STQTL9, High Mobility Group Protein HMGI-C, HMGA2.
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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
MSARGEGAGQ PSTSAQGQPA APAPQKRGRG RPRKQQQEPT GEPSPKRPRG RPKGSKNKSP SKAAQKKAEA TGEKRPRGRP RKWPQQVVQK KPAQEETEET SSQESAEEDL EHHHHHH.
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 :
THG1L HumanDescription:
tRNA-Histidine Guanylyltransferase 1-Like Human Recombinant
tRNA-histidine guanylyltransferase 1-like (S. cerevisiae), Interphase cytoplasmic foci protein 45, probable tRNA(His) guanylyltransferase, induced by high glucose-1, FLJ11601, FLJ20546, ICF45, IHG-1, EC 2.7.7.79, EC 2.7.7.6.
Product # :
ENZ-639Price :
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Description
THG1L Human Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (30-298) and having a molecular mass of 34.0 kDa.THG1L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The THG1L solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Probable tRNA (His) guanylyltransferase (THG1L) is a member of the tRNA (His) gyanylytransferase family. THG1L which is localized to the cytoplasm also found adjacent to the nuclear membrane and expressed in various tissues, including liver and lung. THG1L is expressed in a cell cycle-dependent manner and may be involved in cell cycle progression and cell proliferation. THG1L adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is vital for accurate recognition of the tRNA and for the fidelity of protein synthesis. Upon DNA damage, THG1L is phosphorylated, presumably by ATM or ATR.
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Synonyms
tRNA-histidine guanylyltransferase 1-like (S. cerevisiae), Interphase cytoplasmic foci protein 45, probable tRNA(His) guanylyltransferase, induced by high glucose-1, FLJ11601, FLJ20546, ICF45, IHG-1, EC 2.7.7.79, EC 2.7.7.6.
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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 MGSMAKSKFE YVRDFEADDT CLAHCWVVVR LDGRNFHRFA EKHNFAKPND SRALQLMTKC AQTVMEELED IVIAYGQSDE YSFVFKRKTN WFKRRASKFM THVASQFASS YVFYWRDYFE DQPLLYPPGF DGRVVVYPSN QTLKDYLSWR QADCHINNLY NTVFWALIQQ SGLTPVQAQG RLQGTLAADK NEILFSEFNI NYNNELPMYR KGTVLIWQKV DEVMTKEIKL PTEMEGKKMA VTRTRTKPVP LHCDIIGDAF WKEHPEILDE DS.
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 :
RGS14 HumanDescription:
Regulator of G-Protein Signaling 14 Human Recombinant
Regulator of G-protein signaling 14, RGS14.
Product # :
PRO-1151Price :
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Description
RGS14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 586 amino acids (1-566 a.a) and having a molecular mass of 63.6kDa.RGS14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RGS14 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH7.5, 10% glycerol, 1mM DTT and 200mM NaCl.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Regulator of G-protein signaling 14 (RGS14) is a member of the regulator of G protein signaling family. RGS14 contains one RGS domain, 2 Raf-like Ras-binding domains (RBDs) and one GoLoco motif. RGS14 reduces the signaling activity of G-proteins by binding, via its GoLoco domain, to specific types of activated, GTP-bound G alpha subunits. RGS14 is a scaffolding protein which integrates G protein and H-Ras/ERK/MAP kinase signaling pathways, thus making it suitably positioned to repress plasticity in CA2 neurons. Since RGS14 is highly enriched in CA2 pyramidal neurons, it has a role in inhibition of both synaptic plasticity at these synapses and hippocampal-based learning and memory.
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Synonyms
Regulator of G-protein signaling 14, RGS14.
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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 MPGKPKHLGV PNGRMVLAVS DGELSSTTGP QGQGEGRGSS LSIHSLPSGP SSPFPTEEQP VASWALSFER LLQDPLGLAY FTEFLKKEFS AENVTFWKAC ERFQQIPASD TQQLAQEARN IYQEFLSSQA LSPVNIDRQA WLGEEVLAEP RPDMFRAQQL QIFNLMKFDS YARFVKSPLY RECLLAEAEG RPLREPGSSR LGSPDATRKK PKLKPGKSLP LGVEELGQLP PVEGPGGRPL RKSFRRELGG TANAALRRES QGSLNSSASL DLGFLAFVSS KSESHRKSLG STEGESESRP GKYCCVYLPD GTASLALARP GLTIRDMLAG ICEKRGLSLP
DIKVYLVGNE QALVLDQDCT VLADQEVRLE NRITFELELT ALERVVRISA KPTKRLQEAL QPILEKHGLS PLEVVLHRPG EKQPLDLGKL VSSVAAQRLV LDTLPGVKIS KARDKSPCRS QGCPPRTQDK ATHPPPASPS SLVKVPSSAT GKRQTCDIEG LVELLNRVQS SGAHDQRGLL
RKEDLVLPEF LQLPAQGPSS EETPPQTKSA AQPIGGSLNS TTDSAL.
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 :
NHLH1 HumanDescription:
Nescient Helix Loop Helix 1 Human Recombinant
Nescient Helix Loop Helix 1, Class A Basic Helix-Loop-Helix Protein 35, Helix-Loop-Helix Protein 1, BHLHA35, NSCL1, HEN1.
Product # :
PRO-1547Price :
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Description
NHLH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-133) and having a molecular mass of 17.0kDa.NHLH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NHLH1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 40% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HLH (helix-loop-helix) proteins are a putative transcription factors family. Several HLH proteins take part in growth and development of an extensive range of tissues and species. NHLH1 functions as a DNA-binding protein and has a role in the regulation of cell-type determination in the developing nervous system.
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Synonyms
Nescient Helix Loop Helix 1, Class A Basic Helix-Loop-Helix Protein 35, Helix-Loop-Helix Protein 1, BHLHA35, NSCL1, HEN1.
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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 MGSMMLNSDT MELDLPPTHS ETESGFSDCG GGAGPDGAGP GGPGGGQARG PEPGEPGRKD LQHLSREERR RRRRATAKYR TAHATRERIR VEAFNLAFAE LRKLLPTLPP DKKLSKIEIL RLAICYISYL NHVLDV
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 :
EREG Human, HEKDescription:
Epiregulin Human Recombinant, HEK
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
Product # :
CYT-1206Price :
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Description
EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
Citations
More Info
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Introduction
"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."
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Synonyms
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
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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
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 32.6kDa.
What is the source or expression system of EREG Protein?
HEK293 cells.
What is the Purity of EREG Protein?
EREG Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.
What is the amino acid sequence of EREG Protein?
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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 :
RGS2 HumanDescription:
Regulator of G-Protein Signaling 2 Human Recombinant
Regulator of G-protein Signaling 2 24kDa, G0S8, G0/G1 switch regulatory protein 8, Cell growth-inhibiting gene 31 protein, RGS2.
Product # :
PRO-182Price :
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Description
RGS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-211a.a.) and having a molecular mass of 26.5 kDa. RGS2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RGS2 protein solution (0.25mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
RGS2 belongs to the RGS family which are regulatory molecules that act as GTPase activating proteins for G alpha subunits of heterotrimeric G proteins. RGS2 inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits and as a result driving them into their inactive GDP-bound form.
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Synonyms
Regulator of G-protein Signaling 2 24kDa, G0S8, G0/G1 switch regulatory protein 8, Cell growth-inhibiting gene 31 protein, RGS2.
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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 MQSAMFLAVQ HDCRPMDKSA GSGHKSEEKR EKMKRTLLKD WKTRLSYFLQ NSSTPGKPKT GKKSKQQAFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL MENNSYPRFL ESEFYQDLCK KPQITTEPHA T
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 :
SRR HumanDescription:
Serine Racemase Human Recombinant
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
Product # :
ENZ-232Price :
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Description
SRR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-340) and having a molecular mass of 39.1kDa.SRR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Serine racemase (SRR) is an enzyme which generates D-serine from L-serine. D-serine functions as a neuronal signaling molecule by activating NMDA receptors in the brain. Mammalian SRR is a pyridoxal 5'-phosphate dependent enzyme which catalyzes both the racemization of L-serine to D-serine and also the elimination of water from L-serine, producing pyruvate and ammonia. The SRR enzyme is physiologically stimulated by divalent cations (e.g., magnesium) and is allosterically activated by the magnesium/ATP complex.
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Synonyms
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
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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 MGSHMCAQYC ISFADVEKAH INIRDSIHLT PVLTSSILNQ LTGRNLFFKC ELFQKTGSFK IRGALNAVRS LVPDALERKP KAVVTHSSGN HGQALTYAAK LEGIPAYIVV PQTAPDCKKL AIQAYGASIV YCEPSDESRE NVAKRVTEET EGIMVHPNQE PAVIAGQGTI ALEVLNQVPL VDALVVPVGG GGMLAGIAIT VKALKPSVKV YAAEPSNADD CYQSKLKGKL MPNLYPPETI ADGVKSSIGL NTWPIIRDLV DDIFTVTEDE IKCATQLVWE RMKLLIEPTA GVGVAAVLSQ HFQTVSPEVK NICIVLSGGN VDLTSSITWV KQAERPASYQ SVSV.
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 :
NTHL1 HumanDescription:
Nth Endonuclease III-Like 1 Human Recombinant
Endonuclease III-like protein 1, NTHL1, NTH1, OCTS3.
Product # :
ENZ-172Price :
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Description
NTHL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 332 amino acids (1-312 a.a.) and having a molecular mass of 36.6kDa.NTHL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NTHL1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
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Introduction
Nth endonuclease III-like protein 1 (NTHL1) is one of the enzymes which act on a large number of oxidatively damaged DNA sites. NTHL1 has an apurinic and/or apyrimidinic endonuclease activity and a DNA N-glycosylase activity. NTHL1 acts on a damaged strand, 5' from the damaged site and incises damaged DNA at cytosines, thymines and guanines.
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Synonyms
Endonuclease III-like protein 1, NTHL1, NTH1, OCTS3.
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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 MCSPQESGMT ALSARMLTRS RSLGPGAGPR GCREEPGPLR RREAAAEARK SHSPVKRPRK AQRLRVAYEG SDSEKGEGAE PLKVPVWEPQ DWQQQLVNIR AMRNKKDAPV DHLGTEHCYD SSAPPKVRRY QVLLSLMLSS QTKDQVTAGA MQRLRARGLT VDSILQTDDA TLGKLIYPVG FWRSKVKYIK QTSAILQQHY GGDIPASVAE LVALPGVGPK MAHLAMAVAW GTVSGIAVDT HVHRIANRLR WTKKATKSPE ETRAALEEWL PRELWHEING LLVGFGQQTC LPVHPRCHAC LNQALCPAAQ GL.
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 :
CDH1 Human, Sf9Description:
E-Cadherin Human Recombinant, Sf9
Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-1.
Product # :
PRO-2265Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 694 amino acids (24-709a.a.) and having a molecular mass of 76.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70kDa). CDH1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CDH1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.
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Synonyms
Cadherin 1, Type 1, E-Cadherin, Cadherin 1, Type 1, E-Cadherin (Epithelial), Epithelial Cadherin, CAM 120/80, Uvomorulin, CDHE, UVO, Calcium-Dependent Adhesion Protein, Epithelial, Cadherin 1, E-Cadherin (Epithelial), Cell-CAM 120/80, CD324 Antigen, Arc-1, CD324, ECAD, LCAM, Cadherin-1.
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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
EPEPCHPGFD AESYTFTVPR RHLERGRVLG RVNFEDCTGR QRTAYFSLDT RFKVGTDGVI TVKRPLRFHN PQIHFLVYAW DSTYRKFSTK VTLNTVGHHH RPPPHQASVS GIQAELLTFP NSSPGLRRQK RDWVIPPISC PENEKGPFPK NLVQIKSNKD KEGKVFYSIT GQGADTPPVG VFIIERETGW LKVTEPLDRE RIATYTLFSH AVSSNGNAVE DPMEILITVT DQNDNKPEFT QEVFKGSVME GALPGTSVME VTATDADDDV NTYNAAIAYT ILSQDPELPD KNMFTINRNT GVISVVTTGL DRESFPTYTL VVQAADLQGE GLSTTATAVI TVTDTNDNPP IFNPTTYKGQ VPENEANVVI TTLKVTDADA PNTPAWEAVY TILNDDGGQF VVTTNPVNND GILKTAKGLD FEAKQQYILH VAVTNVVPFE VSLTTSTATV TVDVLDVNEA PIFVPPEKRV EVSEDFGVGQ EITSYTAQEP DTFMEQKITY RIWRDTANWL EINPDTGAIS TRAELDREDF EHVKNSTYTA LIIATDNGSP VATGTGTLLL ILSDVNDNAP IPEPRTIFFC ERNPKPQVIN IIDADLPPNT SPFTAELTHG ASANWTIQYN DPTQESIILK PKMALEVGDY KINLKLMDNQ NKDQVTTLEV SVCDCEGAAG VCRKAQPVEA GLQIPALEHH HHHH.
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 :
LPL HumanDescription:
Lipoprotein Lipase Human Recombinant
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
Product # :
ENZ-086Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human LPL produced in E.coli has a molecular mass of 51.61kDa containing 458 amino acid residues of the human LPL and fused to a 10 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
LPL was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 50mM Acetate buffer, pH=4.
Citations
More Info
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Introduction
LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.
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Synonyms
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
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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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product 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
MKHHHHHHAS ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ADQRRDFIDI ESKFALRTPE DTAEDTCHLI PGVAESVATC HFNHSSKTFM VIHGWTVTGM YESWVPKLVA ALYKREPDSN VIVVDWLSRA QEHYPVSAGY TKLVGQDVAR FINWMEEEFN YPLDNVHLLG YSLGAHAAGI AGSLTNKKVN RITGLDPAGP NFEYAEAPSR LSPDDADFVD VLHTFTRGSP GRSIGIQKPV GHVDIYPNGG TFQPGCNIGE AIRVIAERGL GDVDQLVKCS HERSIHLFID SLLNEENPSK AYRCSSKEAF EKGLCLSCRK NRCNNLGYEI SKVRAKRSSK MYLKTRSQMP YKVFHYQVKI HFSGTESETH TNQAFEISLY GTVAESENIP FTLPEVSTNK TYSFLIYTEV DIGELLMLKL KWKSDSYFSW SDWWSSPGFA IQKIRVKAGE TQKKVIFCSR EKVSHLQKGK APAVFVKCHD KSLNKKSG.
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 :
LRIG1 MouseDescription:
Leucine Rich Repeats And Immunoglobulin Like Domains 1 Mouse Recombinant
Leucine-rich repeats and immunoglobulin-like domains protein 1, LIG-1, Lrig1, LIG1, D6Bwg0781e, Img
Product # :
PRO-2656Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LRIG1 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 770 amino acids (35-796 a.a.) and having a molecular mass of 84.8kDa.LRIG1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LRIG1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Leucine Rich Repeats And Immunoglobulin Like Domains 1 or LRIG1 is a protein, acting as is a pan-negative regulator of EGFR signal transduction. When studied along with ErbB proteins and Met kinase, LRIG1 was found to have regulation activities such as ubiquitination and lysosomal degradation increment of the receptors. Therefore, LRIG1 acts as a suppressor for tumors via cell proliferation control via negative regulation of tyrosine kinase receptors that belongs to the EGF protein family. LRIG1 expression is downregulated in cancer, and acts a prognostic tool for cancer development.
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Synonyms
Leucine-rich repeats and immunoglobulin-like domains protein 1, LIG-1, Lrig1, LIG1, D6Bwg0781e, Img
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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
AQAGPRAPCA AACTCAGDSL DCSGRGLATL PRDLPSWTRS LNLSYNRLSE IDSAAFEDLT NLQEVYLNSN ELTAIPSLGA ASIGVVSLFL QHNKILSVDG SQLKSYLSLE VLDLSSNNIT EIRSSCFPNG LRIRELNLAS NRISILESGA FDGLSRSLLT LRLSKNRITQ LPVKAFKLPR LTQLDLNRNR IRLIEGLTFQ GLDSLEVLRL QRNNISRLTD GAFWGLSKMH VLHLEYNSLV EVNSGSLYGL TALHQLHLSN NSISRIQRDG WSFCQKLHEL ILSFNNLTRL DEESLAELSS LSILRLSHNA ISHIAEGAFK GLKSLRVLDL DHNEISGTIE DTSGAFTGLD NLSKLTLFGN KIKSVAKRAF SGLESLEHLN LGENAIRSVQ FDAFAKMKNL KELYISSESF LCDCQLKWLP PWLMGRMLQA FVTATCAHPE SLKGQSIFSV LPDSFVCDDF PKPQIITQPE TTMAVVGKDI RFTCSAASSS SSPMTFAWKK DNEVLANADM ENFAHVRAQD GEVMEYTTIL HLRHVTFGHE GRYQCIITNH FGSTYSHKAR LTVNVLPSFT KIPHDIAIRT GTTARLECAA TGHPNPQIAW QKDGGTDFPA ARERRMHVMP DDDVFFITDV KIDDMGVYSC TAQNSAGSVS ANATLTVLET PSLAVPLEDR VVTVGETVAF QCKATGSPTP RITWLKGGRP LSLTERHHFT PGNQLLVVQN VMIDDAGRYT CEMSNPLGTE RAHSQLSILP TPGCRKDGTT VGVEHHHHHH
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 :
RHOQ HumanDescription:
Ras Homolog Gene Family Member Q Human Recombinant
ARHQ, RASL7A, TC10, TC10A, Rho-related GTP-binding protein RhoQ, Ras-like protein TC10, Ras-like protein family member 7A, RHOQ.
Product # :
PRO-1451Price :
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Shipping Method :
Shipped with Ice Packs
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Description
RHOQ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202 a.a) and having a molecular mass of 24.7kDa. RHOQ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
RHOQ protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
RHOQ (rho-related GTP-binding protein RhoQ) is a small signaling G protein which cycles between an active GTP-bound and an inactive GDP-bound state. In the active state it binds to a diversity of effector proteins to regulate cellular responses. Ras-like protein belongs to the Rac subfamily of the Rho family of GTPases. RHOQ is involved in epithelial cell polarization processes. In addition, RHOQ plays a role in CFTR trafficking to the plasma membrane. RHOQ causes the formation of thin, actin-rich surface projections called filopodia.
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Synonyms
ARHQ, RASL7A, TC10, TC10A, Rho-related GTP-binding protein RhoQ, Ras-like protein TC10, Ras-like protein family member 7A, RHOQ.
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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 MGSMAHGPGA LMLKCVVVGD GAVGKTCLLM SYANDAFPEE YVPTVFDHYA VSVTVGGKQY LLGLYDTAGQ EDYDRLRPLS YPMTDVFLIC FSVVNPASFQ NVKEEWVPEL KEYAPNVPFL LIGTQIDLRD DPKTLARLND MKEKPICVEQ GQKLAKEIGA CCYVECSALT QKGLKTVFDE AIIAILTPKK HTVKKRIGSR CINCC.
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.