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744 results found for “NANOG”
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Name :
SNCA Delta-NAC HumanDescription:
Alpha Synuclein Delta-NAC Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-161Price :
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Shipping Method :
Shipped with Ice Packs
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Description
A-Synuclein Delta-NAC Human Recombinant which is a deletion mutant of the a-synuclein that lacks the NAC region (amino acid 61-95), produced in E.Coli is a single, non-glycosylated polypeptide chain of 111 amino acids having a molecular mass of 11.9kDa (molecular size on SDS-PAGE will appear higher), with 6 amino acids added as a linker. The Recombinant Human a-Synuclein Delta-NAC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA Delta-NAC protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK GTEIWMKKDQ LGKNEEGAPQ EGILEDMPVD PDNEAYEMPS EEGYQDYEPE 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 :
NT-proBNP CanineDescription:
NT-Pro-B-type Natriuretic Protein Canine Recombinant
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
Product # :
CYT-1223Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NT-proBNP Canine produced in E.coli is a single, non-glycosylated polypeptide chain (1-85 a.a) containing 101 a.a and having a molecular mass of 10,545 Dalton. NT-proBNP is fused with a 16 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NT-proBNP was lyophilized from 10mM potassium phosphate, pH 7.4 and 150 mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NT-proBNP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NT-Pro B-type Natriuretic Protein 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 NT-proBNP in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
N-terminal pro-brain natriuretic peptide, or NT-proBNP, has emerged as a significant biomarker in cardiovascular medicine, providing crucial insights into heart function and aiding in the diagnosis and management of heart-related conditions. This peptide, released in response to cardiac stress, reflects the heart's intricate signaling mechanisms and physiological responses. The study of NT-proBNP, especially in its recombinant form, has not only deepened our understanding of heart diseases but has also led to the development of advanced diagnostic tools and potential therapeutic interventions. This research delves into the world of NT-proBNP Recombinant Protein, exploring its biochemical intricacies, physiological roles, and its profound impact on cardiovascular healthcare.
Structural and Molecular Complexity of NT-proBNP:
NT-proBNP, derived from proBNP through enzymatic cleavage, is a stable peptide fragment. It acts as a precursor to the biologically active B-type natriuretic peptide (BNP) hormone. Understanding the molecular structure and processing of NT-proBNP is essential for unraveling the regulatory mechanisms governing its release and its significance in cardiovascular physiology.
Physiological Significance in Heart Function:
BNP and its precursor, NT-proBNP, play pivotal roles in cardiac homeostasis. They are secreted by ventricular myocardial cells in response to increased wall stress, primarily due to volume and pressure overload. Elevated levels of NT-proBNP serve as a sensitive indicator of heart failure, reflecting the heart's struggle to maintain effective circulation. Monitoring NT-proBNP levels aids clinicians in diagnosing heart failure, assessing its severity, and guiding therapeutic strategies, ultimately improving patient outcomes.
Diagnostic Applications and Clinical Relevance:
NT-proBNP assays, often utilizing recombinant NT-proBNP proteins, have become cornerstones in cardiovascular diagnostics. Elevated levels of NT-proBNP are indicative of heart failure, providing vital information for early intervention and personalized treatment plans. Moreover, the peptide's utility extends to predicting cardiovascular events, aiding in risk stratification among individuals with or at risk of heart diseases. The incorporation of NT-proBNP testing into clinical practice has significantly enhanced the accuracy and timeliness of cardiovascular disease diagnosis.
Potential Therapeutic Implications:
Research into NT-proBNP’s regulatory pathways has opened avenues for therapeutic interventions. Targeted therapies aimed at modulating the BNP system are under investigation, offering potential strategies for managing heart failure and related conditions. By understanding the complex interplay between NT-proBNP, its receptor systems, and cardiac function, researchers are exploring novel therapies to optimize cardiovascular health.
NT-proBNP Recombinant Protein, with its intricate involvement in cardiac physiology and its applications in diagnostics and potential therapeutics, stands as a beacon of hope in the realm of cardiovascular medicine. Its role as a diagnostic marker not only aids in early disease detection but also empowers clinicians to tailor treatments, improving patient outcomes and quality of life. As research continues to unravel the complexities of NT-proBNP, it holds the promise of not only enhancing our understanding of heart diseases but also shaping the future of cardiovascular healthcare. This research underscores the vital role of NT-proBNP in cardiovascular medicine, emphasizing its potential to transform the landscape of heart disease diagnosis and treatment.
What is the molecular weight / Mw of NT-proBNP Canine?
NT-proBNP Canine has a total Mw of 10,545 Da.
What is the source or expression system of NT-proBNP Canine?
Escherichia Coli.
What is the Purity of NT-proBNP Canine?
NT-proBNP Canine is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of NT-proBNP Canine?
The biological functionality of NT-proBNP Canine will be determined in the future.
What is the amino acid sequence of NT-proBNP Canine?
NT-proBNP Canine Protein is composed from 16 amino acids.
What applications can NT-proBNP Canine be used in?
NT-proBNP Canine can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for NT-proBNP Canine?
The endotoxin level is minimal, NT-proBNP Canine 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 :
BGN MouseDescription:
Biglycan Mouse Recombinant
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
Product # :
PRO-2537Price :
Quantity :
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Shipped with Ice Packs
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Description
BGN produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 574 amino acids (38-369 a.a.) and having a molecular mass of 64.6kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). BGN is expressed with a 242 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
The BGN 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
Biglycan (BGN) is a small cellular or pericellular matrix proteoglycan which takes part in assembly of collagen fibrils and muscle regeneration. BGN is closely correlated in structure to two other small proteoglycans, decorin and fibromodulin. BGN interacts with several proteins involved in muscular dystrophy, including alpha-dystroglycan, alpha- and gamma-sarcoglycan and collagen VI. BGN is also critical for the assembly of the dystrophin-associated protein complex.
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Synonyms
BGN, DSPG1, MRLS, PG-S1, PGI, SEMDX, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, Biglycan Proteoglycan, MRLS.
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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
ADPDEEASGS DTTSGVPDLD SVTPTFSAMC PFGCHCHLRV VQCSDLGLKT VPKEISPDTT LLDLQNNDIS ELRKDDFKGL QHLYALVLVN NKISKIHEKA FSPLRKLQKL YISKNHLVEI PPNLPSSLVE LRIHDNRIRK VPKGVFSGLR NMNCIEMGGN PLENSGFEPG AFDGLKLNYL
RISEAKLTGI PKDLPETLNE LHLDHNKIQA IELEDLLRYS KLYRLGLGHN QIRMIENGSL SFLPTLRELH LDNNKLSRVP AGLPDLKLLQ VVYLHSNNIT KVGINDFCPM GFGVKRAYYN GISLFNNPVP YWEVQPATFR CVTDRLAIQF GNYKKLEPKS CDKTHTCPPC PAPELLGGPS
VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH 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.
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Name :
OPG MouseDescription:
Osteoprotegerin Mouse Recombinant
Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.
Product # :
CYT-956Price :
Quantity :
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Shipped with Ice Packs
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Description
OPG Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 388 amino acids (22-401a.a.) and having a molecular mass of 44.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).OPG is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
OPG protein solution (0.25mg/ml) containing 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
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.
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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
ETLPPKYLHY DPETGHQLLC DKCAPGTYLK QHCTVRRKTL CVPCPDHSYT DSWHTSDECV YCSPVCKELQ SVKQECNRTH NRVCECEEGR YLEIEFCLKH RSCPPGSGVV QAGTPERNTV CKKCPDGFFS GETSSKAPCI KHTNCSTFGL LLIQKGNATH DNVCSGNREA TQKCGIDVTL CEEAFFRFAV PTKIIPNWLS VLVDSLPGTK VNAESVERIK RRHSSQEQTF QLLKLWKHQN RDQEMVKKII QDIDLCESSV QRHLGHSNLT TEQLLALMES LPGKKISPEE IERTRKTCKS SEQLLKLLSL WRIKNGDQDT LKGLMYALKH LKTSHFPKTV THSLRKTMRF LHSFTMYRLY QKLFLEMIGN QVQSVKISCL LEHHHHHH.
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 :
NAFDescription:
Nafarelin Acetate
Product # :
HOR-248Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Nafarelin is a decapeptide containing 9 amino acids Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.Nafarelin is purified by proprietary chromatographic techniques.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Nafarelin acetate is a synthetic analog of the naturally occurring gonadotropin-releasing hormone (GnRH). Nafarelin stimulates the release of the pituitary gonadotropins, LH and FSH, resulting in a temporary increase of ovarian steroidogenesis.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Nafarelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NAF 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 Nafarelin in sterile 18MΩ-cm H2O not less than 100 µg/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 :
NAA50 HumanDescription:
N Alpha-Acetyltransferase 50, NatE Catalytic Subunit Human Recombinant
N-alpha-acetyltransferase 50, N-acetyltransferase 13, N-acetyltransferase 5, hNAT5, N-acetyltransferase san homolog, hSAN, NatE catalytic subunit, NAA50, MAK3, NAT13, NAT5, SAN.
Product # :
ENZ-424Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NAA50 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (1-169) and having a molecular mass of 21.9kDa.NAA50 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NAA50 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
N-alpha-acetyltransferase 50 (NAA50) consists of 169 amino acid cytoplasmic protein belonging to the acetyltransferase family and GNAT subfamily. NAA50 is a likely catalytic component of the ARD1A-NARG1 complex which displays alpha acetyltransferase activity. NAA50 has also been shown to interact with MAK10 and is encoded by a gene that maps to human chromosome 3q13.2.
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Synonyms
N-alpha-acetyltransferase 50, N-acetyltransferase 13, N-acetyltransferase 5, hNAT5, N-acetyltransferase san homolog, hSAN, NatE catalytic subunit, NAA50, MAK3, NAT13, NAT5, SAN.
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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 MGSHMKGSRI ELGDVTPHNI KQLKRLNQVI FPVSYNDKFY KDVLEVGELA KLAYFNDIAV GAVCCRVDHS QNQKRLYIMT LGCLAPYRRL GIGTKMLNHV LNICEKDGTF DNIYLHVQIS NESAIDFYRK FGFEIIETKK NYYKRIEPAD AHVLQKNLKV
PSGQNADVQK TDN.
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 :
NUDC HumanDescription:
NudC Nuclear Distribution Protein Human Recombinant
Nuclear Distribution C Dynein Complex Regulator, NudC Nuclear Distribution Protein, Nuclear Distribution Protein C Homolog, Nuclear Distribution Gene C Homolog, Nuclear Distribution C Homolog, Nuclear Migration Protein NudC, NPD011, HNUDC, MNUDC, NUDC.
Product # :
PRO-2347Price :
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Shipping Method :
Shipped with Ice Packs
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Description
NUDC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-331 a.a) and having a molecular mass of 40.6kDa. NUDC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NUDC protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Nuclear distribution gene C homolog (NUDC) is a nuclear distribution protein. The NUDC protein has a key role in mitosis and cytokinesis. NUDC is involved in spindle formation during mitosis and in microtubule organization during cytokinesis. NUDC is required for correct formation of mitotic spindles and chromosome separation during mitosis, as well as cell proliferation. NUDC also has a role in neurogenesis and neuronal migration.
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Synonyms
Nuclear Distribution C Dynein Complex Regulator, NudC Nuclear Distribution Protein, Nuclear Distribution Protein C Homolog, Nuclear Distribution Gene C Homolog, Nuclear Distribution C Homolog, Nuclear Migration Protein NudC, NPD011, HNUDC, MNUDC, NUDC.
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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 MGSMGGEQEE ERFDGMLLAM AQQHEGGVQE LVNTFFSFLR RKTDFFIGGE EGMAEKLITQ TFSHHNQLAQ KTRREKRARQ EAERREKAER AARLAKEAKS ETSGPQIKEL TDEEAERLQL EIDQKKDAEN HEAQLKNGSL DSPGKQDTEE DEEEDEKDKG KLKPNLGNGA DLPNYRWTQT LSELDLAVPF CVNFRLKGKD MVVDIQRRHL RVGLKGQPAI IDGELYNEVK VEESSWLIED GKVVTVHLEK INKMEWWSRL VSSDPEINTK KINPENSKLS DLDSETRSMV EKMMYDQRQK SMGLPTSDEQ KKQEILKKFM DQHPEMDFSK AKFN.
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 :
DNAJC27 HumanDescription:
DnaJ (Hsp40) Homolog, Subfamily C, Member 27 Human Recombinant
DnaJ homolog subfamily C member 27, DnaJ (Hsp40) Homolog, Subfamily C, Member 27, DNAJC27, Rab and DnaJ domain-containing protein, RABJS, RBJ, dnaJ homolog subfamily C member 27 isoform 1.
Product # :
HSP-060Price :
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Shipping Method :
Shipped with Ice Packs
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Description
DNAJC27 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273 a.a.) and having a molecular mass of 33.2kDa. DNAJC27 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DNAJC27 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DnaJ (Hsp40) Homolog, Subfamily C, Member 27 (DNAJC27) which contains one J domain is a part of the small GTPase superfamily. DNAJC27 is a GTPase which activates the MEK/ERK pathway and induces cell transformation when overexpressed.
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Synonyms
DnaJ homolog subfamily C member 27, DnaJ (Hsp40) Homolog, Subfamily C, Member 27, DNAJC27, Rab and DnaJ domain-containing protein, RABJS, RBJ, dnaJ homolog subfamily C member 27 isoform 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
MGSSHHHHHH SSGLVPRGSH MGSMEANMPK RKEPGRSLRI KVISMGNAEV GKSCIIKRYC EKRFVSKYLA TIGIDYGVTK VHVRDREIKV NIFDMAGHPF FYEVRNEFYK DTQGVILVYD VGQKDSFDAL DAWLAEMKQE LGPHGNMENI IFVVCANKID CTKHRCVDES EGRLWAESKG FLYFETSAQT GEGINEMFQT FYISIVDLCE NGGKRPTTNS SASFTKEQAD AIRRIRNSKD SWDMLGVKPG ASRDEVNKAY RKLAVLLHPD KCVAPGSEDA FKAVVNARTA LLKNIK.
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 :
CANT1 HumanDescription:
Calcium Activated Nucleotidase 1 Human Recombinant
Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.
Product # :
PRO-1010Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CANT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (63-401 a.a.) and having a molecular mass of 40.5kDa. CANT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CANT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.
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Synonyms
Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.
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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 MGSHMRPAPG RPPTHNAHNW RLGQAPANWY NDTYPLSPPQ RTPAGIRYRI AVIADLDTES RAQEENTWFS YLKKGYLTLS DSGDKVAVEW DKDHGVLESH LAEKGRGMEL SDLIVFNGKL YSVDDRTGVV YQIEGSKAVP WVILSDGDGT VEKGFKAEWL AVKDERLYVG GLGKEWTTTT GDVVNENPEW VKVVGYKGSV DHENWVSNYN ALRAAAGIQP PGYLIHESAC WSDTLQRWFF LPRRASQERY SEKDDERKGA NLLLSASPDF GDIAVSHVGA VVPTHGFSSF KFIPNTDDQI IVALKSEEDS GRVASYIMAF TLDGRFLLPE TKIGSVKYEG IEFI.
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 :
HMGN3 HumanDescription:
High Mobility Group Nucleosomal Binding Domain 3 Human Recombinant
High Mobility Group Nucleosomal Binding Domain 3, TRIP7, TR-Interacting Protein 7, High Mobility Group Nucleosome-Binding Domain-Containing Protein 3, Thyroid Hormone Receptor Interacting Protein 7, Thyroid Receptor-Interacting Protein 7, Thyroid Hormone Receptor Interactor 7, PNAS-24, PNAS-25, TRIP-7, High mobility group nucleosome-binding domain-containing protein 3.
Product # :
PRO-2068Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HMGN3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77 a.a) and having a molecular mass of 10.8 kDa. HMGN3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMGN3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH7.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
High Mobility Group Nucleosomal Binding Domain 3 (HMGN3), binds thyroid hormone receptor beta, however it occurs only in the presence of thyroid hormone. Thyroid hormone receptors are hormone-dependent transcription factors which regulate expression of a variety of particular target genes. HMGN3 is considered to reduce the compactness of the chromatin fiber in nucleosomes, in that way enhancing transcription from chromatin templates.
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Synonyms
High Mobility Group Nucleosomal Binding Domain 3, TRIP7, TR-Interacting Protein 7, High Mobility Group Nucleosome-Binding Domain-Containing Protein 3, Thyroid Hormone Receptor Interacting Protein 7, Thyroid Receptor-Interacting Protein 7, Thyroid Hormone Receptor Interactor 7, PNAS-24, PNAS-25, TRIP-7, High mobility group nucleosome-binding domain-containing protein 3.
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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 MGSMPKRKSP ENTEGKDGSK VTKQEPTRRS ARLSAKPAPP KPEPKPRKTS AKKEPGAKIS RGAKGKKEEK QEAGKEGTEN.
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 :
CHRNA3 HumanDescription:
Cholinergic Receptor Nicotinic Alpha 3 Human Recombinant
Cholinergic Receptor, Nicotinic, Alpha 3 (Neuronal), Cholinergic Receptor, Nicotinic, Alpha Polypeptide 3, NACHRA3, LNCR2, PAOD2, Neuronal Nicotinic Acetylcholine Receptor, Alpha3 Subunit, Neuronal Acetylcholine Receptor Subunit Alpha-3, Acetylcholine Receptor, Alpha 3 (Neuronal), Nicotinic, Neuronal acetylcholine receptor subunit alpha-3.
Product # :
PRO-2216Price :
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Description
CHRNA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (32-240 a.a) and having a molecular mass of 27kDa. CHRNA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHRNA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Cholinergic Receptor Nicotinic Alpha 3, also known as CHRNA3 is part of the nicotinic acetylcholine receptor family. Proteins of this family form pentameric complexes comprised of both alpha & beta subunits. Furthermore, CHRNA3 is ligand-gated ions channel which prticipates in neurotransmission. CHRNA3 has been associated with an increased risk of smoking initiation as well as an increased susceptibility to lung cancer.
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Synonyms
Cholinergic Receptor, Nicotinic, Alpha 3 (Neuronal), Cholinergic Receptor, Nicotinic, Alpha Polypeptide 3, NACHRA3, LNCR2, PAOD2, Neuronal Nicotinic Acetylcholine Receptor, Alpha3 Subunit, Neuronal Acetylcholine Receptor Subunit Alpha-3, Acetylcholine Receptor, Alpha 3 (Neuronal), Nicotinic, Neuronal acetylcholine receptor subunit alpha-3.
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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 MGSSEAEHRL FERLFEDYNE IIRPVANVSD PVIIHFEVSM SQLVKVDEVN QIMETNLWLK QIWNDYKLKW NPSDYGGAEF MRVPAQKIWK PDIVLYNNAV GDFQVDDKTK ALLKYTGEVT WIPPAIFKSS CKIDVTYFPF DYQNCTMKFG SWSYDKAKID LVLIGSSMNL KDYWESGEWA IIKAPGYKHD IKYNCCEEIY PDITYSLYIR RL.
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 :
NFNB E.ColiDescription:
Dihydropteridine Reductase E.Coli Recombinant
DPRA, NFSB, NFSI, NTR.
Product # :
ENZ-423Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NFNB Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular mass of 26 kDa. The NFNB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.05M NaCl & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NFNB demonstrates the capability to reduce quinines. NFNB enzyme activates prodrugs in antibody directed enzyme prodrug therapy. NFNB reduces nitrofurazone, quinones and anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.
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Synonyms
DPRA, NFSB, NFSI, NTR.
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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 MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN ATLPKSRLPQ NITLTEV.
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 :
ATG3 HumanDescription:
Autophagy Related 3 Human Recombinant
APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.
Product # :
PRO-1987Price :
Quantity :
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Description
ATG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a) and having a molecular mass of 38.3kDa. ATG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATG3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.
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Synonyms
APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.
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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 MGSMQNVINT VKGKALEVAE YLTPVLKESK FKETGVITPE EFVAAGDHLV HHCPTWQWAT GEELKVKAYL PTGKQFLVTK NVPCYKRCKQ MEYSDELEAI IEEDDGDGGW VDTYHNTGIT GITEAVKEIT LENKDNIRLQ DCSALCEEEE DEDEGEAADM EEYEESGLLE TDEATLDTRK IVEACKAKTD AGGEDAILQT RTYDLYITYD KYYQTPRLWL FGYDEQRQPL TVEHMYEDIS QDHVKKTVTI ENHPHLPPPP MCSVHPCRHA EVMKKIIETV AEGGGELGVH MYLLIFLKFV QAVIPTIEYD YTRHFTM.
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 :
NusA E.ColiDescription:
Transcription Termination/Antitermination L Factor E.Coli Recombinant
Transcription elongation protein nusA, N utilization substance protein A, L factor, nusA, ECK3158, JW3158, b3169, Transcription Termination/Antitermination L Factor.
Product # :
PRO-623Price :
Quantity :
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Shipped with Ice Packs
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Description
NusA Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 495 amino acids (1-495a.a.) and having a molecular mass of 54 kDa.
Source
Escherichia Coli.
Formulation
NusA protein solution contains 1x PBS pH-7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NusA is an important player in both prevention and enhancement of transcriptional termination. NusA is important both in Rho-dependent and intrinsic termination, as well as in lambda and other phage antitermination systems. The NusA gene was first identified by isolation of the nusAl mutation, which limits bacteriophage-l growth by preventing the antitermination activity of the l N protein. NusA plays a role in transcriptional antitermination in the cell. It has been shown to specifically aid in read-through of the RNA polymerase genes rpoB and rpoC, as well as in successful synthesis of the ribosomal RNA genes. Additionally to its anti-termination role, NusA is needed for both Rho-dependent and intrinsic transcriptional termination. NusA is obligatory for Rho-dependent termination in lambda phage and in the cell. NusA plays a role in intrinsic termination and the inhibition of RNA elongation. However NusA interacts with all three subunits of RNA polymerase, its termination activity primarily depends on its interaction with the carboxy-terminus of RpoA. NusA induces conformational change in RNA polymerase & prevents RNA interaction with RpoA. This binding sequentially activates NusA, allowing it to bind RNA and promote formation of hairpins at intrinsic termination sites. NusA binds Rho, and participates with sigma70 for binding to the core RNA polymerase complex. NusA does not compete with NusG for binding to either Rho or the polymerase, despite modulating the same process as NusG in both cases.
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Synonyms
Transcription elongation protein nusA, N utilization substance protein A, L factor, nusA, ECK3158, JW3158, b3169, Transcription Termination/Antitermination L Factor.
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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
MNKEILAVVE AVSNEKALPR EKIFEALESA LATATKKKYE QEIDVRVQID RKSGDFDTFRRWLVVDEVTQ PTKEITLEAA RYEDESLNLG DYVEDQIESV TFDRITTQTA KQVIVQKVREAERAMVVDQF REHEGEIITG VVKKVNRDNI SLDLGNNAEA VILREDMLPR ENFRPGDRVR GVLYSVRPEA RGAQLFVTRS KPEMLIELFR IEVPEIGEEV IEIKAAARDP GSRAKIAVKT NDKRIDPVGA CVGMRGARVQ AVSTELGGER IDIVLWDDNP AQFVINAMAP ADVASIVVDE DKHTMDIAVE AGNLAQAIGR NGQNVRLASQ LSGWELNVMT DDLQAKHQA EAHAAIDTFT KYLDIDEDFA TVLVEEGFST LEELAYVPMK ELLEIEGLDE PTVEALRERA KNALATIAQA QEESLGDNKP ADDLLNLEGV DRDLAFKLAA RGVCTLEDLA EQGIDDLADI EGLTDEKAGA LIMAARNICW FGDEA.
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 :
LAG-1 HumanDescription:
LAG-1 Human Recombinant (CCL4L1)
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
Product # :
CHM-018Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LAG-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa.The CCL4L1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAG-1 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using human CCR5 transfected murine BaF3 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.More Info
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Introduction
CCL4L1 (C-C motif chemokine 4-like) is a member of to intercrine beta (chemokine CC) family. The CCL4L1 protein is similar to CCL4 which inhibits HIV replication in peripheral blood monocytes which express CCR5.
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Synonyms
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LAG-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4L1 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 LAG-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN.
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 :
GNG11 HumanDescription:
Guanine Nucleotide Binding Protein Gamma 11 Human Recombinant
GNGT11, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11, GNG11.
Product # :
PRO-1854Price :
Quantity :
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Description
GNG11 Human Recombinant produced in E. coli is. a single polypeptide chain containing 93 amino acids (1-70) and having a molecular mass of 10.6kDa. GNG11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GNG11 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.
More Info
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Introduction
Guanine Nucleotide Binding Protein Gamma 11 (GNG11) which belongs to the guanine nucleotide-binding protein (G protein) gamma family encodes a lipid-anchored, cell membrane protein. G proteins act as a modulator or transducer in various transmembrane signaling systems. GNG11 is also subject to carboxyl-terminal processing.
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Synonyms
GNGT11, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11, GNG11.
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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 MGSMPALHIE DLPEKEKLKM EVEQLRKEVK LQRQQVSKCS EEIKNYIEER SGEDPLVKGI PEDKNPFKEK GSC.
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 :
Visfatin HumanDescription:
Visfatin Human Recombinant
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Product # :
CYT-318Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 466 amino acids. The total molecular mass is 52.6kDa (calculated). The Visfatin is purified by Flag-affinity chromatography.
Source
Escherichia Coli.
Formulation
Visfatin was lyophilized with no additives.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The activity is determined by its ability to induce IL-6, IL-1 beta and TNF alpha production from human PBMCs at 100ng/ml.More Info
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Introduction
Excess adiposity is the most important risk in the development of type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-a, and IL-6, that modulate sensitivity and appear to play an important role in the pathogenesis, diabetes, dyslipidemia, inflammation, and atherosclerosis. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
Visfatin exerts mimetic effects that are dose-dependent and quantitatively similar to stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its mimetic effects, visfatin was as effective in reducing hyperglycemia in deficient diabetic mice. Visfatin was also found to be bound to and activate receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin did not compete for binding to the receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes. -
Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Visfatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Visfatin 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
Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with 20 mM HCl at a concentration of 0.1 mg/mL, which can be further diluted into other aqueous solutions. Wait several minutes for full reconstitution and solubility.
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Amino Acid Sequence
MPPNTSKVYS YFECREKKTE NSKLRKVKYE ETVFYGLQYI LNKYLKGKVV TKEKIQEAKD VYKEHFQDDV FNEKGWNYIL EKYDGHLPIE IKAVPEGFVI PRGNVLFTVE NTDPECYWLT NWIETILVQS WYPITVATNS REQKKILAKY LLETSGNLDG LEYKLHDFGY RGVSSQETAG IGASAHLVNF KGTDTVAGLA LIKKYYGTKD PVPGYSVPAA EHSTITAWGK DHEKDAFEHI VTQFSSVPVS VVSDSYDIYN ACEKIWGEDL RHLIVSRSTQ APLIIRPDSG NPLDTVLKVL EILGKKFPVT ENSKGYKLLP PYLRVIQGDG VDINTLQEIV EGMKQKMWSI ENIAFGSGGG LLQKLTRDLL NCSFKCSYVV TNGLGINVFK DPVADPNKRS KKGRLSLHRT PAGNFVTLEE GKGDLEEYGQ DLLHTVFKNG KVTKSYSFDE IRKNAQLNIE LEAAHH.
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Background
About Visfatin Human
Visfatin is a cytokine expressed in visceral fat that was originally isolated as a secreted
element that synergized with stem cell factors and IL-7. One of its main functions is to
enhance the development of B cell precursors.The cytokine is also known as the “Pre-B Cell Colony-Enhancing Factor (PBEF).” It has been
identified in vertebrates, including mice and humans, and it’s being studied due to its link
to inflammatory conditions, beta cell function, and cardiovascular disease.
What’s the Function of Visfatin Human Recombinant?Visfatin human recombinant is produced in E. Coli. It’s a single, non-glycosylated,
polypeptide chain that contains 466 amino acids, it’s purified by FLAG-affinity
chromatography, and it contains a total molecular mass of 52.6 kDa.
What Are the Main Applications of Visfatin Human Recombinant?The cytokine is being researched because of its involvement in glucose homeostasis,
dysregulation in biosynthesis and signal transduction, and the pathogenesis of diabetes.
Visfatin human recombinant is tailored exclusively for laboratory research, ensuring
experts can get further answers regarding the cytokine’s involvement in different
processes, including pathogenesis, diabetes, inflammation, dyslipidemia, and
atherosclerosis.Findings can also help during the identification of high-risk people for cardiovascular
disease and diabetes.
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 :
BASP1 HumanDescription:
Brain Abundant Membrane Attached Signal Protein 1 Human Recombinant
CAP-23, CAP23, NAP-22, NAP22, Brain acid soluble protein 1, BASP1, BASP1 Human, 22 kDa neuronal tissue-enriched acidic protein, Neuronal axonal membrane protein NAP-22.
Product # :
PRO-1355Price :
Quantity :
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Shipped with Ice Packs
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Description
BASP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-227) and having a molecular mass of 25 kDa (Molecular size on SDS-PAGE will appear higher). BASP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BASP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Brain Abundant Membrane Attached Signal Protein 1 (BASP1) is a membrane bound protein with numerous transient phosphorylation positions and PEST motifs. Preservation of proteins with PEST sequences amongst diverse species supports their functional significance. PEST sequences take place in proteins with high turnover rates. Immunological attributes of this protein are species specific. BASP1 undergoes N-terminal myristoylation.
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Synonyms
CAP-23, CAP23, NAP-22, NAP22, Brain acid soluble protein 1, BASP1, BASP1 Human, 22 kDa neuronal tissue-enriched acidic protein, Neuronal axonal membrane protein NAP-22.
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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 MGSMGGKLSK KKKGYNVNDE KAKEKDKKAE GAATEEEGTP KESEPQAAAE PAEAKEGKEK PDQDAEGKAE EKEGEKDAAA AKEEAPKAEP EKTEGAAEAK AEPPKAPEQE QAAPGPAAGG EAPKAAEAAA APAESAAPAA GEEPSKEEGE PKKTEAPAAP AAQETKSDGA PASDSKPGSS EAAPSSKETP AATEAPSSTP KAQGPAASAE EPKPVEAPAA NSDQTVTVKE.
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 :
SNCA NACP112 HumanDescription:
Alpha Synuclein NACP112 Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-162Price :
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Shipped with Ice Packs
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Description
A-Synuclein NACP112 Human Recombinant which is an alternatively spliced (103-129) form of a-Synuclein, produced in E.Coli is a single, non-glycosylated polypeptide chain of 112 amino acids having a molecular mass of 11.3kDa. The Recombinant Human a-Synuclein NACP112 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA NACP112 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKEGYQDYEP EA.
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 :
b NGF Human, HEKDescription:
beta Nerve Growth Factor Human Recombinant, HEK
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Product # :
CYT-079Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BNGF Human Recombinant produced in HEK293 is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.
Source
HEK293 cells.
Formulation
The b-NGF was lyophilized from 1mg/ml in 20mM PB and 0.25M NaCl pH-7.5.
Purity
Greater than 97% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.
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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
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Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized b-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution b-NGF 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 b-NGF in sterile distilled pyrogen free water at a concentration of 0.25mg/ml.
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Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 26.5kDa.
What is the source or expression system of B NGF Protein?
HEK293 cells.
What is the Purity of B NGF Protein?
B NGF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of B NGF Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.
What is the amino acid sequence of B NGF Protein?
B NGF Protein is composed from 118 amino acids.
What applications can B NGF Protein be used in?
B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for B NGF Protein?
The endotoxin level is minimal, B NGF 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 :
EREG HumanDescription:
Epiregulin Human Recombinant
EREG, Epiregulin, ER.
Product # :
CYT-609Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
- purity
- biological activity
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Description
Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.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
EREG, Epiregulin, ER.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epiregulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epiregulin 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 Epiregulin 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
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 5.6kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.
What is the amino acid sequence of EREG Protein?
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
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 :
HMGN1 HumanDescription:
High-Mobility Group Nucleosome Binding Domain 1 Human Recombinant
HMG14, GC104230, High-Mobility Group Nucleosome Binding Domain 1.
Product # :
PRO-821Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
HMGN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids (1-100 a.a.) and having a molecular mass of 11.7 kDa. HMGN1 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
HMGN1 protein solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl, 0.1mM PMSF & 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
HMGN1 binds to the inner side of the nucleosomal DNA therefore changing the interaction between the DNA and the histone octamer. HMGN1 participates in the development which maintains transcribable genes in an exceptional chromatin conformation. HMGN1 inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2.
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Synonyms
HMG14, GC104230, High-Mobility Group Nucleosome Binding Domain 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
MPKRKVSSAE GAAKEEPKRR SARLSAKPPA KVEAKPKKAA AKDKSSDKKV QTKGKRGAKG KQAEVANQET KEDLPAENGE TKTEESPASD EAGEKEAKSD LEHHHHHH.
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 :
HP-NAPDescription:
Neutrophil-activating protein A Helicobacter Pylori Recombinant
DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.
Product # :
PRO-2035Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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Description
HP-NAP Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Ala144) containing 154 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 18.2kDa.
Source
Escherichia Coli.
Formulation
HP-NAP was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.
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Synonyms
DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. HP-NAP 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
MKHHHHHHASMKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV TVTYADDQLA KLQKSIWMLQ AHLA.
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 :
DNAJC12 HumanDescription:
DnaJ (Hsp40) Homolog, Subfamily C, Member 12 Human Recombinant
DnaJ homolog subfamily C member 12, J domain-containing protein 1, DNAJC12, JDP1, RP11-57G10.2.
Product # :
HSP-053Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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- purity
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Description
DNAJC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (1-198) and having a molecular mass of 26kDa (Molecular weight on SDS-PAGE will appear higher).DNAJC12 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DNAJC12 solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 2mM DTT and 100mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DnaJ (Hsp40) Homolog, Subfamily C, Member 12 (DNAJC12) belongs to the DnaJ/Hsp40 family. DnaJ/Hsp40 family members are linked with complex assembly, protein folding, and export. DnaJ/Hsp40 proteins are extremely conserved throughout evolution and function as co-chaperones regulating protein folding, transport, translational initiation and gene expression. DnaJC12 has a role in protein folding and export and is believed to be involved in estrogen control and the development of breast cancer. DNAJC12 is expressed at high levels in the brain, heart, and testis, and at reduced levels in the kidney and stomach.
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Synonyms
DnaJ homolog subfamily C member 12, J domain-containing protein 1, DNAJC12, JDP1, RP11-57G10.2.
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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 MGSHMDAILN YRSEDTEDYY TLLGCDELSS VEQILAEFKV RALECHPDKH PENPKAVETF QKLQKAKEIL TNEESRARYD HWRRSQMSMP FQQWEALNDS VKTSMHWVVR GKKDLMLEES DKTHTTKMEN EECNEQRERK KEELASTAEK TEQKEPKPLE KSVSPQNSDS SGFADVNGWH LRFRWSKDAP SELLRKFRNY EI.
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.