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1000 results found for “hcg”
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Description:
Hepatoma-Derived Growth Factor (32-285 a.a) Human Recombinant
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.
Product # :
CYT-294Price :
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Shipped with Ice Packs
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Description
HGF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (32-285 a.a.) and having a molecular mass of 29.8kDa. HGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HGF protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
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Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.
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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
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.
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Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein has a total Mw of 29.8kDa.
What is the source or expression system of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
Escherichia Coli.
What is the Purity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
What is the molecular weight/Mw of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein has a total Mw of 29.8kDa. What is the source or expression system of HGF (32-285) HUMAN Protein? Escherichia Coli. What is the Purity of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE. What is the Biological Activity of HGF (32-285) HUMAN Protein? The biological functionality of HGF (32-285) HUMAN Protein will be determined in the future. What is the amino acid sequence of HGF (32-285) HUMAN Protein? MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET. What applications can HGF (32-285) HUMAN Protein be used in? HGF (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for HGF (32-285) HUMAN Protein? The endotoxin level is minimal, HGF (32-285) HUMAN Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.
What applications can HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein be used in?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ATG4B HumanDescription:
ATG4 Autophagy Related 4 Homolog B Human Recombinant
Cysteine protease ATG4B, AUT-like 1 cysteine endopeptidasem, Autophagin-1, Autophagy-related cysteine endopeptidase 1, Autophagy-related protein 4 homolog B, hAPG4B, ATG4B, APG4B, AUTL1, KIAA0943.
Product # :
PRO-1048Price :
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Shipped with Ice Packs
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Description
ATG4B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-393 a.a.) and having a molecular mass of 45.4kDa.ATG4B is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATG4B protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cysteine protease ATG4B (ATG4B) belongs to the autophagin protein family. Autophagy is the manner by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is vital for cell homeostasis and cell remodeling during differentiation, metamorphosis, non-apoptotic cell death, and aging. ATG4B is a cysteine protease necessary for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is then transformed to a smaller form (form II). Form II, with an exposed C-terminal glycine, is deemed to be the phosphatidylethanolamine (PE)-conjugated form, and is capable of binding to autophagosomes. Reduced levels of autophagy are seen in some malignant tumors; therefore autophagy may have a role in controlling the unregulated cell growth linked to cancer.
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Synonyms
Cysteine protease ATG4B, AUT-like 1 cysteine endopeptidasem, Autophagin-1, Autophagy-related cysteine endopeptidase 1, Autophagy-related protein 4 homolog B, hAPG4B, ATG4B, APG4B, AUTL1, KIAA0943.
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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
MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRKNFPA IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFS VLNAFIDRKD SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR RLCRTSVPCA GATAFPADSD RHCNGFPAGA EVTNRPSPWR PLVLLIPLRL GLTDINEAYV ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVEPTD GCFIPDESFH CQHPPCRMSI AELDPSIAVG FFCKTEDDFN DWCQQVKKLS LLGGALPMFE LVEQQPSHLA CPDVLNLSLD SSDVERLERF FDSEDEDFEI LSLLEHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BGN HumanDescription:
Biglycan Human Recombinant
DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.
Product # :
PRO-1382Price :
Quantity :
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Shipped with Ice Packs
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Description
BGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (38-368a.a) and having a molecular mass of 39.5kDa. BGN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
BGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
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
DSPG1, PG-S1, PGI, SLRR1A, Biglycan, Bone/cartilage proteoglycan I, BGN.
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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 MDEEASGADT SGVLDPDSVT PTYSAMCPFG CHCHLRVVQC SDLGLKSVPK EISPDTTLLD LQNNDISELR KDDFKGLQHL YALVLVNNKI SKIHEKAFSP LRKLQKLYIS KNHLVEIPPN LPSSLVELRI HDNRIRKVPK GVFSGLRNMN CIEMGGNPLE NSGFEPGAFD GLKLNYLRIS EAKLTGIPKD LPETLNELHL DHNKIQAIEL EDLLRYSKLY RLGLGHNQIR MIENGSLSFL PTLRELHLDN NKLARVPSGL PDLKLLQVVY LHSNNITKVG VNDFCPMGFG VKRAYYNGIS LFNNPVPYWE VQPATFRCVT DRLAIQFGNY KK.
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 :
CCNI HumanDescription:
Cyclin-I Human Recombinant
Cyclin-I, CCNI, CYC1, CYI.
Product # :
PKA-318Price :
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Shipped with Ice Packs
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Description
CCNI Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (1-377 a.a) and having a molecular mass of 44.9kDa.CCNI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCNI protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CCN1 is a part of the extremely conserved cyclin family, whose members are characterized by a remarkable periodicity in protein abundance through the cell cycle. Cyclins which function as regulators of CDK kinases, shows the highest similarity with cyclin G. Different cyclins display diverse expression and degradation patterns which contribute to the chronological coordination of every mitotic event. The transcript of CCN1was found to be expressed continually during cell cycle progression.
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Synonyms
Cyclin-I, CCNI, CYC1, CYI.
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Physical Appearance
Sterile Filtered clear 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 MGSMKFPGPL ENQRLSFLLE KAITREAQMW KVNVRKMPSN QNVSPSQRDE VIQWLAKLKY QFNLYPETFA LASSLLDRFL ATVKAHPKYL SCIAISCFFL AAKTVEEDER IPVLKVLARD SFCGCSSSEI LRMERIILDK LNWDLHTATP LDFLHIFHAI AVSTRPQLLF SLPKLSPSQH LAVLTKQLLH CMACNQLLQF RGSMLALAMV SLEMEKLIPD WLSLTIELLQ KAQMDSSQLI HCRELVAHHL STLQSSLPLN SVYVYRPLKH TLVTCDKGVF RLHPSSVPGP DFSKDNSKPE VPVRGTAAFY HHLPAASGCK QTSTKRKVEE MEVDDFYDGI KRLYNEDNVS ENVGSVCGTD LSRQEGHASP CPPLQPVSVM.
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 :
IRGM HumanDescription:
Immunity-Related GTPase Family, M Human Recombinant
Immunity-related GTPase family M protein, Immunity-related GTPase family M protein1, LPS-stimulated RAW 264.7 macrophage protein 47 homolog, LRG-47, IRGM, IFI1, IRGM1, LRG47.
Product # :
PRO-1302Price :
Quantity :
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Shipped with Ice Packs
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Description
IRGM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (23-181) and having a molecular mass of 20.1 kDa. IRGM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IRGM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Immunity-related GTPase family M protein (IRGM) is essential for clearance of severe protozoan and bacterial infections. IRGM belongs to the p47 immunity-related GTPase family. IRGM serves in innate immune response possibly via regulation of autophagy. IRGM regulates proinflammatory cytokine production and inhibit endotoxemia upon infection and also has a part in macrophages adhesion and motility. Polymorphisms which modify the natural expression of the IRGM gene are associated with a susceptibility to Crohn's disease and tuberculosis.
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Synonyms
Immunity-related GTPase family M protein, Immunity-related GTPase family M protein1, LPS-stimulated RAW 264.7 macrophage protein 47 homolog, LRG-47, IRGM, IFI1, IRGM1, LRG47.
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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 MKETLKIVSR TPVNITMAGD SGNGMSTFIS ALRNTGHEGK ASPPTELVKA TQRCASYFSS HFSNVVLWDL PGTGSATTTL ENYLMEMQFN RYDFIMVASA QFSMNHVMLA KTAEDMGKKF YIVWTKLDMD LSTGALPEVQ LLQIRENVLE NLQKERVCEY.
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 :
PLAC8 HumanDescription:
Placenta-Specific 8 Human Recombinant
Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.
Product # :
PRO-1725Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PLAC8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa.PLAC8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLAC8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0),0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Placenta-Specific 8 (PLAC8) is a member of the cornifelin family. The PLAC8 protein is expressed at high levels in the plasmacytoid dendritic cells, spleen, lymph nodes, peripheral blood leukocytes, and bone marrow.
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Synonyms
Placenta-Specific 8, C15, Onzin, Placenta-Specific Gene 8 Protein, Protein C15.
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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 MGSMQAQAPV VVVTQPGVGP GPAPQNSNWQ TGMCDCFSDC GVCLCGTFCF PCLGCQVAAD MNECCLCGTS VAMRTLYRTR YGIPGSICDD YMATLCCPHC TLCQIKRDIN RRRAMRTF.
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 :
GDA Human, HisDescription:
Guanine Deaminase Human Recombinant, His Tag
CYPIN, GUANASE, NEDASIN, Guanine aminase, Guanine aminohydrolase, GAH, p51-nedasin.
Product # :
ENZ-682Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GDA Human Recombinant produced in E. coli is a single polypeptide chain containing 477 amino acids (1-454) and having a molecular mass of 53kDa. GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDA solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl,10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.
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Synonyms
CYPIN, GUANASE, NEDASIN, Guanine aminase, Guanine aminohydrolase, GAH, p51-nedasin.
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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 MGSMCAAQMP PLAHIFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE ASQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHASQ YSFAGSSIDL PLLEWLTKYT FPAEHRFQNI DFAEEVYTRV VRRTLKNGTT TACYFATIHT DSSLLLADIT DKFGQRAFVG KVCMDLNDTF PEYKETTEES IKETERFVSE MLQKNYSRVK PIVTPRFSLS CSETLMGELG NIAKTRDLHI QSHISENRDE VEAVKNLYPS YKNYTSVYDK NNLLTNKTVM AHGCYLSAEE LNVFHERGAS IAHCPNSNLS LSSGFLNVLE VLKHEVKIGL GTDVAGGYSY SMLDAIRRAV MVSNILLINK VNEKSLTLKE VFRLATLGGS QALGLDGEIG NFEVGKEFDA ILINPKASDS PIDLFYGDFF GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.
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 :
GMNN HumanDescription:
Geminin Human Recombinant
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
Product # :
PRO-579Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Geminin Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.7 kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris pH 8, 100mM NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.
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Synonyms
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNPS MKQKQEEIKE NIKNSSVPRR TLKMIQPSAS GSLVGRENEL SAGLSKRKHR NDHLTSTTSS PGVIVPESSE NKNLGGVTQE SFDLMIKENP SSQYWKEVAE KRRKALYEAL KENEKLHKEI EQKDNEIARL KKENKELAEV AEHVQYMAEL IERLNGEPLD NFESLDNQEF DSEEETVEDS LVEDSEIGTC AEGTVSSSTD
AKPCI.
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 :
LIPG HumanDescription:
Lipase Endothelial Human Recombinant
LIPG, Lipase Endothelial, EDL, EL, Endothelial Cell-Derived Lipase, EC 3.1.1.3, PRO719, Endothelial Lipase, Lipoprotein Lipase H, EC 3.1.1.
Product # :
ENZ-785Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LIPG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (21-340) and having a molecular mass of 38kDa.LIPG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LIPG solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lipase Endothelial (LIPG) has extensive phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. The LIPG protein is considered a member of the TG lipase family through its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. In addition, the LIPG has triglyceride lipase activities. LIPG hydrolyzes HDLs more efficiently than other lipoproteins.
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Synonyms
LIPG, Lipase Endothelial, EDL, EL, Endothelial Cell-Derived Lipase, EC 3.1.1.3, PRO719, Endothelial Lipase, Lipoprotein Lipase H, EC 3.1.1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. 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 MGSSPVPFGP EGRLEDKLHK PKATQTEVKP SVRFNLRTSK DPEHEGCYLS VGHSQPLEDC SFNMTAKTFF IIHGWTMSGI FENWLHKLVS ALHTREKDAN VVVVDWLPLA HQLYTDAVNN TRVVGHSIAR MLDWLQEKDD FSLGNVHLIG YSLGAHVAGY AGNFVKGTVG RITGLDPAGP MFEGADIHKR LSPDDADFVD VLHTYTRSFG LSIGIQMPVG HIDIYPNGGD FQPGCGLNDV LGSIAYGTIT EVVKCEHERA VHLFVDSLVN QDKPSFAFQC TDSNRFKKGI CLSCRKNRCN SIGYNAKKMR NKRNSKMYLK TRA.
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 :
UQCRH HumanDescription:
Ubiquinol-Cytochrome C Reductase Hinge Protein Human Recombinant
Cytochrome c1 non-heme 11 kDa protein, Ubiquinol-cytochrome c reductase complex 11 kDa protein, UQCRH, Ubiquinol-Cytochrome C Reductase Hinge Protein, Complex III Subunit VIII, Complex III Subunit 6, Mitochondrial Hinge Protein, Ubiquinol-Cytochrome C Reductase, QCR6, UQCR8, Cytochrome B-C1 Complex Subunit 6 Mitochondrial, Ubiquinol-Cytochrome C Reductase Complex III Subunit VIII.
Product # :
PRO-1798Price :
Quantity :
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Description
UQCRH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (14-91 a.a) and having a molecular mass of 11.6kDa.UQCRH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UQCRH protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ubiquinol-Cytochrome C Reductase Hinge Protein (UQCRH) is a member of the UQCRH/QCR6 family. UQCRH is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The UQCRH protein mediates formation of the complex between cytochromes c and c1.
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Synonyms
Cytochrome c1 non-heme 11 kDa protein, Ubiquinol-cytochrome c reductase complex 11 kDa protein, UQCRH, Ubiquinol-Cytochrome C Reductase Hinge Protein, Complex III Subunit VIII, Complex III Subunit 6, Mitochondrial Hinge Protein, Ubiquinol-Cytochrome C Reductase, QCR6, UQCR8, Cytochrome B-C1 Complex Subunit 6 Mitochondrial, Ubiquinol-Cytochrome C Reductase Complex III Subunit VIII.
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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 MGSGDPEEEE EEEEELVDPL TTVREQCEQL EKCVKARERL ELCDERVSSR SHTEEDCTEE LFDFLHARDH CVAHKLFNNL 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.
- View Data Sheet
Name :
GDF15 Human, HisDescription:
Growth and Differentiation Factor 15 Human Recombinant, His Tag
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Product # :
CYT-691Price :
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Description
Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
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Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
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Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.
What is the source or expression system of GDF15 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 HUMAN, HIS Protein?
The biological functionality of GDF15 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
What applications can GDF15 HUMAN, HIS Protein be used in?
GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and
Lateral Flow.
What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Prolactin Human, PEGDescription:
Prolactin Pegylated Human Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-1063Price :
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Description
Prolactin Human Recombinant Pegylated produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids + an additional Ala at n-terminal. Pegylated Prolactin is mono-pegylated having a molecular mass of ~ 39 kDa, however under non-denaturing conditions it behaves as 220 kDa protein due to its increased hydrodynamic volume. The Pegylated Prolactin protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Human Prolactin was tested for its biological functionality in-vitro by inducing proliferation of Nb2 cells or Baf/3 cells that were stably transfected with Human Prolactin receptors, though its activity is lower than human Prolactin. However, it is anticipated that its biological activity in vivo will be higher than human Prolactin due to prolonged persistence in circulation.
Citations
More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Prolactin is secreted when eating, nursing, mating, estrogen treatment and during ovulation. Prolactin's primary role is to promote and maintain lactation but also plays a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin in sterile 0.4% NaHCO3 pH-8-9, 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.
- View Data Sheet
Name :
CNTF Human, HisDescription:
Ciliary Neurotrophic Factor Human Recombinant, His Tag
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-573Price :
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Description
Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 1-200) containing a total of 220 amino acids and having a molecular mass of 25kDa. The CNTF protein is fused to a 20 aa His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNTF protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8 and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
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Physical Appearance
Sterile Filtered colorless 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 MAFTEHSPLT PHRRDLCSRS IWLARKIRSDLTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
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Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The biological functionality of CNTF Protein will be determined in the future.
What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSDLTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CEA Human, HisDescription:
Carcinoembryonic Antigen Human Recombinant, His Tag
Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.
Product # :
PRO-2407Price :
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Description
CEA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 659 amino acids (35-685a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-150kDa). CEA is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CEA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed. -
Synonyms
Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.
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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
KLTIESTPFN VAEGKEVLLL VHNLPQHLFG YSWYKGERVD GNRQIIGYVI GTQQATPGPA YSGREIIYPN ASLLIQNIIQ NDTGFYTLHV IKSDLVNEEA TGQFRVYPEL PKPSISSNNS KPVEDKDAVA FTCEPETQDA TYLWWVNNQS LPVSPRLQLS NGNRTLTLFN VTRNDTASYK CETQNPVSAR RSDSVILNVL YGPDAPTISP LNTSYRSGEN LNLSCHAASN PPAQYSWFVN GTFQQSTQEL FIPNITVNNS GSYTCQAHNS DTGLNRTTVT TITVYAEPPK PFITSNNSNP VEDEDAVALT CEPEIQNTTY LWWVNNQSLP VSPRLQLSND NRTLTLLSVT RNDVGPYECG IQNKLSVDHS DPVILNVLYG PDDPTISPSY TYYRPGVNLS LSCHAASNPP AQYSWLIDGN IQQHTQELFI SNITEKNSGL YTCQANNSAS GHSRTTVKTI TVSAELPKPS ISSNNSKPVE DKDAVAFTCE PEAQNTTYLW WVNGQSLPVS PRLQLSNGNR TLTLFNVTRN DARAYVCGIQ NSVSANRSDP VTLDVLYGPD TPIISPPDSS YLSGANLNLS CHSASNPSPQ YSWRINGIPQ QHTQVLFIAK ITPNNNGTYA CFVSNLATGR NNSIVKSITV SASGTSPGLS ALEHHHHHH.
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 :
CCN1 HumanDescription:
Cysteine-Rich Angiogenic Inducer 61 Human Recombinant
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Product # :
CYT-164Price :
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Shipped at Room temp
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Description
CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2m filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.Citations
More Info
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Introduction
CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
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Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 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 CYR61 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
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD -
Background
Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis
Abstract:
Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.Introduction:
Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.Production and Characterization:
Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.Role in Angiogenesis:
CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.Therapeutic Implications:
The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.Conclusion:
Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 39.5kDa.
What is the source or expression system of CCN1 Protein?
Escherichia Coli.
What is the Purity of CCN1 Protein?
CCN1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCN1 Protein?
The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.
What is the amino acid sequence of CCN1 Protein?
TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD
What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Activin-A Human ActiveDescription:
Activin-A Human Recombinant, Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-145Price :
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Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
Citations
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.
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 :
TRH HumanDescription:
Thyrotropin Releasing Hormone Human
Thyroliberin, TRH, MGC125964, MGC125965, Protirelin, TRF.
Product # :
HOR-264Price :
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Description
Thyrotropin Releasing Hormone Human C16H22N6O4 has a molecular mass of 362.4 Dalton.The TRH is purified by proprietary chromatographic techniques.
Formulation
The TRH was lyophilized with no additives.
Purity
Greater than 98.2% as determined by analysis by RP-HPLC.
Citations
More Info
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Introduction
Thyrotropin-releasing hormone (TRH), also called thyrotropin-releasing factor (TRF), thyroliberin or protirelin, is a tripeptide hormonethat stimulates the release of thyroid-stimulating hormoneand prolactinby the anterior pituitary.
TRH is produced by the hypothalamus, near the paraventricular nucleus.
It travels across the median eminenceto the pituitary via the hypophyseal portal system. It is released from cells called thyrotropes.
In addition to the brain, TRH can also be detected in other areas of the body including the gastrointestinal systemand pancreatic islets.
Protirelin stimulates the secretion of pituitary thyroid stimulating hormone from the anterior pituitary and has been shown that protirelin increases secretion of prolactin. Protirelin is identified as 5-oxo-L-prolyl-L-histidyl-L-proline amide. It is a synthetic tripeptide that is believed to be structurally identical to the naturally-occurring thyrotropin-releasing hormone produced by the hypothalamus. -
Synonyms
Thyroliberin, TRH, MGC125964, MGC125965, Protirelin, TRF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protirelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRH 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 Thyroliberin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Pyr-His-Pro-NH2.
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Background
What is the molecular weight/Mw of TRH HUMAN Protein?
TRH HUMAN Protein has a total Mw of 0.36kDa.
What is the Purity of TRH HUMAN Protein?
TRH HUMAN Protein is >98.2% pure as determined by SDS-PAGE.
What is the Biological Activity of TRH HUMAN Protein?
The biological functionality of TRH HUMAN Protein will be determined in the future.
What is the amino acid sequence of TRH HUMAN Protein?
Pyr-His-Pro-NH2.
What applications can TRH HUMAN Protein be used in?
TRH HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TRH HUMAN Protein?
The endotoxin level is minimal, TRH HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HBsAg preS1Description:
Hepatitis B Surface Antigen, preS1 Recombinant
Product # :
HBS-871Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The E.Coli derived Recombinant Hepatitis B Surface Antigen preS1 is a single non-glycosylated polypeptide chain containing 119 amino acids and having a molecular weight of 12.6 kDa.
Source
Escherichia Coli.
Formulation
HBsAg protein was lyophilized from 0.2μm filtered (1mg/ml) solution in 20mM PB, pH 7.4, and 50mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Citations
More Info
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Introduction
Hepatitis B virus (HBV) is a human pathogen, causing serious liver disease. The HBV surface protein antigens (HBsAg) are comprised of three carboxyl co terminal HBs proteins termed large (LHBs), middle (MHBs) and small (SHBs, also called major) protein. LHBs and MHBs also share the highly hydrophobic, repetitive, membrane spanning S domain. In addition, LHBs has a 119 amino acid region called preS1.
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Stability
This lyophilized HBsAg preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
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Solubility
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MGGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGAN
SNNPDWDFNPNKDHWPEAHQVGAGAFGPGFTPPHGGLLGWSP
QAQGILTTVPVAPPPASTNRQSGRQPTPISPPLRDSHPQA. -
Purification Method
HBsAg protein was purified by proprietary chromatographic technique.
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 :
HBsAg preS2Description:
Hepatitis B Surface Antigen, preS2 Recombinant
Product # :
HBS-874Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Hepatitis B Surface Antigen preS2 is approximately 5.7 kDa, a single non-glycosylated polypeptide chain containing 55 amino acids. Purified by proprietary chromatographic technique.
Source
E.coli.
Formulation
HBsAg protein was lyophilized from 0.2μm filtered (1mg/ml) solution in 20mM PB, pH 7.4 and 50mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Hepatitis B virus (HBV) is a human pathogen, causing serious liver disease. The HBV surface protein antigens (HBsAg) are comprised of three carboxyl co terminal HBs proteins termed large (LHBs), middle (MHBs) and small (SHBs, also called major) protein. LHBs and MHBs also share the highly hydrophobic, repetitive, membrane spanning S domain. In addition, MHBs has a 55 amino acid region called preS2.
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Stability
This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
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Solubility
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQWNSTTFHQALLDPKVRGLYFPAGGSSSGTVNPVPTTASP ISSIFSRTGDPAPN.
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 :
GAGE12F HumanDescription:
G Antigen 12F Human Recombinant
G Antigen 12F, GAGE-12F, G Antigen 12F/G/I.
Product # :
PRO-1736Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GAGE12F Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-117aa) and having a molecular mass of 15.4kDa.GAGE12F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GAGE12F protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GAGE12F is a member of the GAGE multigene family expressed in a large range of tumors whereas in normal tissues, his expression is restricted to germ cells. These genes are organized in clustered repeats, and have a high degree of forecasted sequence identity, however differ by scattered single nucleotide substitution. Their sequences contain either the antigenic peptide YYWPRPRRY or YRPRPRRY which is recognized by cytotoxic T-cells.
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Synonyms
G Antigen 12F, GAGE-12F, G Antigen 12F/G/I.
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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 MGSMSWRGRS TYYWPRPRRY VQPPEMIGPM RPEQFSDEVE PATPEEGEPA TQRQDPAAAQ EGEDEGASAG QGPKPEAHSQ EQGHPQTGCE CEDGPDGQEM DPPNPEEVKT PEEGEKQSQC
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 :
POGLUT1 HumanDescription:
Protein O-Glucosyltransferase 1 Human Recombinant
POGLUT1, C3orf9, CLP46, hCLP46, KDELCL1, KTELC1, Protein O-glucosyltransferase 1, CAP10-like 46 kDa protein, KTEL motif-containing protein 1, Myelodysplastic syndromes relative protein, O-glucosyltransferase Rumi homolog, hRumi, Protein O-xylosyltransferase, MDSRP.
Product # :
ENZ-956Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
POGLUT1 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 377 amino acids (24-392a.a) and having a molecular mass of 44.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). POGLUT1 is fused to a 8 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The POGLUT1 solution (0.25mg/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
POGLUT1 is a homologue of Rumi from Drosophila, an endoplasmic reticulum (ER)-retaining glucosyltransferase which catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to EGF repeats on the consensus sequence C-X-S-X-P-C. POGLUT1 positively regulates Notch signaling without affecting Notch ligand binding.
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Synonyms
POGLUT1, C3orf9, CLP46, hCLP46, KDELCL1, KTELC1, Protein O-glucosyltransferase 1, CAP10-like 46 kDa protein, KTEL motif-containing protein 1, Myelodysplastic syndromes relative protein, O-glucosyltransferase Rumi homolog, hRumi, Protein O-xylosyltransferase, MDSRP.
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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
RQKESGSKWK VFIDQINRSL ENYEPCSSQN CSCYHGVIEE DLTPFRGGIS RKMMAEVVRR KLGTHYQITK NRLYRENDCM FPSRCSGVEH FILEVIGRLP DMEMVINVRD YPQVPKWMEP AIPVFSFSKT SEYHDIMYPA WTFWEGGPAV WPIYPTGLGR WDLFREDLVR SAAQWPWKKK NSTAYFRGSR TSPERDPLIL LSRKNPKLVD AEYTKNQAWK SMKDTLGKPA AKDVHLVDHC KYKYLFNFRG VAASFRFKHL FLCGSLVFHV GDEWLEFFYP QLKPWVHYIP VKTDLSNVQE LLQFVKANDD VAQEIAERGS QFIRNHLQMD DITCYWENLL SEYSKFLSYN VTRRKGYDQI IPKMLKTELL 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.
- View Data Sheet
Name :
LRG1 Human, Sf9Description:
Leucine-Rich Alpha-2-Glycoprotein 1 Human Recombinant, Sf9
Leucine Rich Alpha-2-Glycoprotein 1, Leucine-Rich Alpha-2-Glycoprotein, 1300008B03Rik, 2310031E04Rik, HMFT1766, Leucine-rich alpha-2-glycoprotein, LRG1, LRG.
Product # :
PRO-2530Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LRG1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 321 amino acids (36-347a.a.) and having a molecular mass of 35.4kDa. LRG1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LRG1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
LRG1 belongs to the leucine-rich repeat (LRR) family of proteins, which have been shown to be involved in protein-protein interaction, signal transduction, cell adhesion and development. The LRG1 is expressed during granulocyte differentiation.
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Synonyms
Leucine Rich Alpha-2-Glycoprotein 1, Leucine-Rich Alpha-2-Glycoprotein, 1300008B03Rik, 2310031E04Rik, HMFT1766, Leucine-rich alpha-2-glycoprotein, LRG1, LRG.
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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
ADPVTLSPKD CQVFRSDHGS SISCQPPAEI PGYLPADTVH LAVEFFNLTH LPANLLQGAS KLQELHLSSN GLESLSPEFL RPVPQLRVLD LTRNALTGLP PGLFQASATL DTLVLKENQL EVLEVSWLHG LKALGHLDLS GNRLRKLPPG LLANFTLLRT LDLGENQLET LPPDLLRGPL QLERLHLEGN KLQVLGKDLL LPQPDLRYLF LNGNKLARVA AGAFQGLRQL DMLDLSNNSL ASVPEGLWAS LGQPNWDMRD GFDISGNPWI CDQNLSDLYR WLQAQKDKMF SQNDTRCAGP EAVKGQTLLA VAKSQHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
RGS14 HumanDescription:
Regulator of G-Protein Signaling 14 Human Recombinant
Regulator of G-protein signaling 14, RGS14.
Product # :
PRO-1151Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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.
- View Data Sheet
Name :
Thyroglobulin Human, BiotinDescription:
Thyroglobulin Human, Biotinylated
Thyroglobulin, TGN, AITD3, TG.
Product # :
PRO-2563Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).
Source
Native, Isolated from human thyroid glands.
Formulation
Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease. -
Synonyms
Thyroglobulin, TGN, AITD3, TG.
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Physical Appearance
Sterile Filtered solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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.