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1000 results found for “noggin”
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Name :
NCAM1 HumanDescription:
Neural Cell Adhesion Molecule 1 Human Recombinant
Neural cell adhesion molecule 1, Neural cell adhesion molecule 1 isoform3, N-CAM-1, NCAM-1, CD56, NCAM1, NCAM, MSK39
Product # :
PRO-2710Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NCAM1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 593 amino acids (20-603 a.a) and having a molecular mass of 65.7kDa.NCAM1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The NCAM1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Neural Cell Adhesion Molecule 1 (NCAM1) is apart of the immunoglobulin superfamily. NCAM1 bindsspecifically to neurite fasciculation, neuronneuron adhesion, outgrowth of neurites, and more. The polysialyation of NCAM1 reduces its adhesive property and increases its neurite outgrowth promoting features.NCAM1is mainly expressed in NK cells and a subset of T lymphocytes that mediate MHC-unrestricted cellmediated cytotoxicity. High expression of NCAM-1 differentiates NK cells as having an activated phenotype. During hematopoiesis, NCAM1plays a role as the prototypic marker of NK cells and also present on subset of CD4+, CD8+ and T cells. In cell adhesion, NCAM1 contributes to cell-cell adhesion during embryonic development.
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Synonyms
Neural cell adhesion molecule 1, Neural cell adhesion molecule 1 isoform3, N-CAM-1, NCAM-1, CD56, NCAM1, NCAM, MSK39
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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
ADPLQVDIVP SQGEISVGES KFFLCQVAGD AKDKDISWFS PNGEKLTPNQ QRISVVWNDD SSSTLTIYNA NIDDAGIYKC VVTGEDGSES EATVNVKIFQ KLMFKNAPTP QEFREGEDAV IVCDVVSSLP PTIIWKHKGR DVILKKDVRF IVLSNNYLQI RGIKKTDEGT YRCEGRILAR GEINFKDIQV IVNVPPTIQA RQNIVNATAN LGQSVTLVCD AEGFPEPTMS WTKDGEQIEQ EEDDEKYIFS DDSSQLTIKK VDKNDEAEYI CIAENKAGEQ DATIHLKVFA KPKITYVENQ TAMELEEQVT LTCEASGDPI PSITWRTSTR NISSEEKTLD GHMVVRSHAR VSSLTLKSIQ YTDAGEYICT ASNTIGQDSQ SMYLEVQYAP KLQGPVAVYT WEGNQVNITC EVFAYPSATI SWFRDGQLLP SSNYSNIKIY NTPSASYLEV TPDSENDFGN YNCTAVNRIG QESLEFILVQ ADTPSSPSID QVEPYSSTAQ VQFDEPEATG GVPILKYKAE WRAVGEEVWH SKWYDAKEAS MEGIVTIVGL KPETTYAVRL AALNGKGLGE ISAASEFKTQ PVHSPPPHHH HHH
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 :
NEDD8 HumanDescription:
Neural Precursor Cell Expressed Developmentally Down-Regulated 8 Human Recombinant
Nedd-8, FLJ43224, MGC104393, MGC125896, MGC125897, NEDD8, Ubiquitin-like protein Nedd8, Neddylin, Neural precursor cell expressed developmentally down-regulated protein 8.
Product # :
ENZ-396Price :
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Shipped with Ice Packs
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Description
NEDD8 Human Recombinant fused with 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (1-76 a.a.) and having a molecular mass of 12.8 kDa.The NEDD8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NEDD8 solution contains 20mM Tris pH 8.0, 50mM NaCl, 0.5mM DTT & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NEDD8 is part of the ubiquitin family. Human NEDD8 shares 60% amino acid sequence homology to ubiquitin. The NEDD8 system is essential for the regulation of protein degradation pathways involved in cell cycle progression, morphogenesis and tumorigenesis. NEDD8 is involved in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E-1 complex UbE1c- appbp1 and linkage to the E-2 enzyme UbE2m. Attachment of NEDD8 to cullins activates their associated E-3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.
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Synonyms
Nedd-8, FLJ43224, MGC104393, MGC125896, MGC125897, NEDD8, Ubiquitin-like protein Nedd8, Neddylin, Neural precursor cell expressed developmentally down-regulated protein 8.
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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
MHHHHHHMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYAQ SGLLAEITPD KAFQDKLYPF TWDAVRYNGK LIAYPIAVEA LSLIYNKDLL PNPPKTWEEI PALDKELKAK GKSALMFNLQ EPYFTWPLIA ADGGYAFKYE NGKYDIKDVG VDNAGAKAGL TFLVDLIKNK HMNADTDYSI AEAAFNKGET AMTINGPWAW SNIDTSKVNY GVTVLPTFKG QPSKPFVGVL SAGINAASPN KELAKEFLEN YLLTDEGLEA
VNKDKPLGAV ALKSYEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTNSSSNN NNNNNNNNLG IEGRGSHMAA AEAANCIMEV SCGQAESSEK PNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGILCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLHAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG
FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYVHALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR.
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 :
E Selectin HumanDescription:
E-selectin Human Recombinant
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
Product # :
PRO-380Price :
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Shipped with Ice Packs
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Description
E-Selectin Human Recombinant is expressed in E. coli containing amino acids 179-557 fused to an amino terminal hexahistidine tag, having a total molecular weight of 45.22 kDa.
Source
Escherichia Coli.
Formulation
E-Selectin is supplied in 1x PBS and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
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Introduction
E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
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Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
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Physical Appearance
Sterile Filtered liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
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 :
Quantity :
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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.
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.
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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
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 :
IHH MouseDescription:
Indian Hedgehog Mouse Recombinant
Indian hedgehog protein, IHH, HHG-2, BDA1.
Product # :
CYT-398Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IHH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0μg/ml corresponding to a specific activity of 100-334units/mg.
More Info
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Introduction
IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.
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Synonyms
Indian hedgehog protein, IHH, HHG-2, BDA1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH 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 IHH 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
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
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 :
OMP HumanDescription:
Olfactory Marker Protein Human Recombinant
Olfactory neuronal-specific protein, Olfactory marker protein, OMP.
Product # :
PRO-1412Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-163 a.a) and having a molecular mass of 21.3kDa. OMP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
OMP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Olfactory marker protein (OMP) which is expressed in the cytoplasm of olfactory chemosensory neurons in the nasal neuroepithelium, is associated in a unique way with the mature olfactory receptor neurons in numerous vertebrate species. OMP have a modulatory part in the odor detection/signal transduction cascade ant its expression is a sign of mature vertebrate olfactory receptor neurons (ORNs). OMP is also a potent enhancer of mitosis in fetal olfactory epithelial cells and it promotes an increase in uptake of tritiated thymidine in liver.
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Synonyms
Olfactory neuronal-specific protein, Olfactory marker protein, OMP.
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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 MGSMAEDRPQ QPQLDMPLVL DQGLTRQMRL RVESLKQRGE KRQDGEKLLQ PAESVYRLNF TQQQRLQFER WNVVLDKPGK VTITGTSQNW TPDLTNLMTR QLLDPTAIFW RKEDSDAIDW NEADALEFGE RLSDLAKIRK VMYFLVTFGE GVEPANLKAS VVFNQL.
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 :
BNIP1 HumanDescription:
BCL2/Adenovirus E1B 19kDa Interacting Protein 1 Human Recombinant
BCL2/Adenovirus E1B 19kDa Interacting Protein 1, NIP1, BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 1, Transformation-Related Gene 8 Protein, TRG-8, BCL2/Adenovirus E1B 19kD-Interacting Protein 1, Vesicle Transport Protein SEC20, SEC20L, SEC20, Vesicle transport protein SEC20.
Product # :
PRO-2150Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BNIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-199 a.a) and having a molecular mass of 25.2kDa. BNIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BNIP1 protein solution (1.0 mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
BNIP1 belongs to the of the BCL2/adenovirus E1B 19 kd-interacting protein (BNIP) family. BNIP1 interacts with the E1B 19 kDa protein, which defends cells from virally-induced cell death. In addition, BNIP1 interacts with E1B 19 kDa-like sequences of BCL2 which is an additional apoptotic protector. Adding up, BNIP1 is implicated in vesicle transport into the endoplasmic reticulum. Alternative splicing results of BNIP1 in four protein products with identical N- and C-termini have been found.
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Synonyms
BCL2/Adenovirus E1B 19kDa Interacting Protein 1, NIP1, BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 1, Transformation-Related Gene 8 Protein, TRG-8, BCL2/Adenovirus E1B 19kD-Interacting Protein 1, Vesicle Transport Protein SEC20, SEC20L, SEC20, Vesicle transport protein SEC20.
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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 MGSMAAPQDV HVRICNQEIV KFDLEVKALI QDIRDCSGPL SALTELNTKV KEKFQQLRHR IQDLEQLAKE QDKESEKQLL LQEVENHKKQ MLSNQASWRK ANLTCKIAID NLEKAELLQG GDLLRQRKTT KESLAQTSST ITESLMGISR MMAQQVQQSE EAMQSLVTSS RTILDANEEF KSMSGTIQLG RKLITKYNRR EL.
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 :
PFDN2 HumanDescription:
Prefoldin Subunit 2 Human Recombinant
Prefoldin subunit 2, PFDN2, PFD2.
Product # :
PRO-001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PFDN2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 18.8kDa. The PFDN2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFDN2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Prefoldin subunit 2 (PFDN2) belongs to the prefoldin beta subunit family. The PFDN2 protein is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold correctly. PFDN2 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. PFDN2 also binds to a nascent polypeptide chain and promotes folding in an setting in which there are many competing pathways for nonnative proteins.
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Synonyms
Prefoldin subunit 2, PFDN2, PFD2.
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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 MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS.
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 :
PFN1 RatDescription:
Profilin-1 Rat Recombinant
Profilin-1, Profilin I.
Product # :
PRO-2231Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PFN1 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 17.5kDa. PFN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PFN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Profilin-1 also known as Pfn1 is a ubiquitous actin monomer-binding protein which is a member of the profilin family. Pfn1 significantly enhances skin wound healing in-vitro as well as in-vivo which is mediated by purinergic receptors. Furthermore, Pfn1 is also active in endothelial cell migration and vessel sprouting. Pfn1 is considered to regulate actin polymerization in response to extracellular signals.
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Synonyms
Profilin-1, Profilin I.
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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 MGSHMAGWNA YIDSLMADGT CQDAAIVGYK DSPSVWAAVP GKTFVSITPA EVGVLVGKDR SSFFVNGLTL GGQKCSVIRD SLLQDGEFTM DLRTKSTGGA PTFNVTVTMT AKTLVLLMGK EGVHGGLINK KCYEMASHLR RSQY.
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 :
PLEKHF2 HumanDescription:
Pleckstrin Homology Domain Containing Family F Member 2 Human Recombinant
EAPF, PHAFIN2, ZFYVE18, Pleckstrin homology domain-containing family F member 2, PH domain-containing family F member 2, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, PH and FYVE domain-containing protein 2, Zinc finger FYVE domain-containing protein 18, PLEKHF2.
Product # :
PRO-1874Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PLEKHF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-249 a.a) and having a molecular mass of 30.2kDa. PLEKHF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLEKHF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Pleckstrin Homology Domain Containing Family F Member 2, also known as PLEKHF2, contains 1 FYVE-type zinc finger and 1 PH domain. PLEKHF2 takes part in early endosome fusion upstream of RAB5, regulates receptor trafficking and fluid-phase transport. PLEKHF2 increases cellular sensitivity to TNF-induced apoptosis.
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Synonyms
EAPF, PHAFIN2, ZFYVE18, Pleckstrin homology domain-containing family F member 2, PH domain-containing family F member 2, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, PH and FYVE domain-containing protein 2, Zinc finger FYVE domain-containing protein 18, PLEKHF2.
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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 MGSMVDRLAN SEANTRRISI VENCFGAAGQ PLTIPGRVLI GEGVLTKLCR KKPKARQFFL FNDILVYGNI VIQKKKYNKQ HIIPLENVTI DSIKDEGDLR NGWLIKTPTK SFAVYAATAT EKSEWMNHIN KCVTDLLSKS GKTPSNEHAA VWVPDSEATV CMRCQKAKFT PVNRRHHCRK CGFVVCGPCS EKRFLLPSQS SKPVRICDFC YDLLSAGDMA TCQPARSDSY SQSLKSPLND MSDDDDDDDS SD.
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 :
CDC37 Human, HisDescription:
Cell Division Cycle 37 Human Recombinant, His Tag
Cell Division Cycle 37 homolog, P50CDC37, CDC37, Hsp90 chaperone protein kinase-targeting subunit, CDC37 cell division cycle 37 homolog, hsp90 co-chaperone Cdc37, CDC37A.
Product # :
PRO-140Price :
Quantity :
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Description
CDC37, His Protein is a 45.71 kDa protein containing 388 amino acids fused to a 10 aa N-Terminal His-tag.
Source
E. coli
Formulation
CDC37, His Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in
20mM TRIS, 50mM NaCl, pH 7.5.More Info
-
Introduction
CDC37, His protein is extremely parallel to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. CDC37 is a molecular chaperone with a detailed role in cell signal transduction. CDC37 forms a complex with Hsp90 and several protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, and eIF2 alpha kinases CDC37 has a vital part in directing Hsp90 to its target kinases.
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Synonyms
Cell Division Cycle 37 homolog, P50CDC37, CDC37, Hsp90 chaperone protein kinase-targeting subunit, CDC37 cell division cycle 37 homolog, hsp90 co-chaperone Cdc37, CDC37A.
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Stability
Store lyophilized CDC37 His human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted CDC37 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
Add deionized water to prepare a working stock solution of 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV
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 :
Procalcitonin HumanDescription:
Procalcitonin Human Recombinant
Procalcitonin, PCT.
Product # :
HOR-304Price :
Quantity :
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Shipped at Room temp
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Description
Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids and having a molecular mass of 12.8 kDa.The Procalcitonin is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
-
Synonyms
Procalcitonin, PCT.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized procalcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution procalcitonin 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.
-
Solubility
It is recommended to reconstitute the lyophilized procalcitonin sterile 18MΩ-cm H2O at 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN.
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 :
MANF RatDescription:
Mesencephalic Astrocyte-Derived Neurotrophic Factor Rat Recombinant
Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.
Product # :
CYT-828Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MANF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18.2kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% 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 rat C6 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.More Info
-
Introduction
MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.
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Synonyms
Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MANF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MANF 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.
-
Solubility
It is recommended to reconstitute the lyophilized MANF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIEEELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDKQ IDLSTVDLKK LRVKELKKIL DDWGEMCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.
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 :
RAGE Human, Sf9Description:
Advanced Glycosylation End Product-Specific Receptor Human Recombinant, Sf9
Advanced Glycosylation End-Product Specific Receptor, Advanced Glycosylation End Product-Specific Receptor, RAGE, Receptor for Advanced Glycation End-Products Variant 20, Receptor for Advanced Glycosylation End Products, Receptor for Advanced Glycation End-Products, RAGE Isoform NtRAGE-Delta, RAGE Isoform SRAGE-Delta, SCARJ1.
Product # :
PRO-2645Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RAGE Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 561 amino acids (24-342 a.a) and having a molecular mass of 61.2kDa. RAGE is fused to a 242 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The RAGE solution (0.25mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by the ability of the binding activity in a functional ELISA. The ED50 range ≤15ug/ml.
More Info
-
Introduction
Advanced Glycosylation End Product-Specific Receptor or RAGE is an immunoglobulin, part of the immunoglobulin transmembrane proteins family. RAGE moderates interactions between advanced glycosylation end products, also known as AGE. These signaling has a crucial part in the regulation of TNFalpha,oxidative stress, endothelial dysfunction in type 2 diabetesproduction and expression. RAGE helps the translocation of ABPP (amyloid-beta peptide) through the membrane of cells to the intracellular area in the cortical neurons.
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Synonyms
Advanced Glycosylation End-Product Specific Receptor, Advanced Glycosylation End Product-Specific Receptor, RAGE, Receptor for Advanced Glycation End-Products Variant 20, Receptor for Advanced Glycosylation End Products, Receptor for Advanced Glycation End-Products, RAGE Isoform NtRAGE-Delta, RAGE Isoform SRAGE-Delta, SCARJ1.
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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.
-
Amino Acid Sequence
ADLQNITARI GEPLVLKCKG APKKPPQRLE WKLNTGRTEA WKVLSPQGGG PWDSVARVLP NGSLFLPAVG IQDEGIFRCQ AMNRNGKETK SNYRVRVYQI PGKPEIVDSA SELTAGVPNK VGTCVSEGSY PAGTLSWHLD GKPLVPNEKG VSVKEQTRRH PETGLFTLQS ELMVTPARGG DPRPTFSCSF SPGLPRHRAL RTAPIQPRVW EPVPLEEVQL VVEPEGGAVA PGGTVTLTCE VPAQPSPQIH WMKDGVPLPL PPSPVLILPE IGPQDQGTYS CVATHSSHGP QESRAVSISI IEPGEEGPTA GSVGGSGLGT LALEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEA HNHYTQKSLS LSPGKHHHHH 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 :
ZCCHC12 HumanDescription:
Zinc Finger, CCHC Domain Containing 12 Human Recombinant
PNMA7A, SIZN, SIZN1, Zinc finger CCHC domain-containing protein 12, Smad-interacting zinc finger protein 1, ZCCHC12.
Product # :
PRO-1982Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ZCCHC12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-402 a.a) and having a molecular mass of 47.8kDa. ZCCHC12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZCCHC12 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Zinc Finger, CCHC Domain Containing 12 (ZCCHC12) which holds 1 CCHC-type zinc finger is a part of the ZCCHC12 family. ZCCHC12 takes part in the bone morphogenetic protein (BMP)-signaling pathway as a transcriptional coactivator. BMP signaling is positively modulated as a result of the interaction between ZCCHC12 with SMAD1 and the association with CBP in the transcription complex.
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Synonyms
PNMA7A, SIZN, SIZN1, Zinc finger CCHC domain-containing protein 12, Smad-interacting zinc finger protein 1, ZCCHC12.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASIIAR VGNSRRLNAP LPPWAHSMLR SLGRSLGPIM ASMADRNMKL FSGRVVPAQG EETFENWLTQ VNGVLPDWNM SEEEKLKRLM KTLRGPAREV MRVLQATNPN LSVADFLRAM KLVFGESESS VTAHGKFFNT LQAQGEKASL YVIRLEVQLQ NAIQAGIIAE KDANRTRLQQ LLLGGELSRD LRLRLKDFLR MYANEQERLP NFLELIRMVR EEEDWDDAFI KRKRPKRSES MVERAVSPVA FQGSPPIVIG SADCNVIEID DTLDDSDEDV ILVESQDPPL PSWGAPPLRD RARPQDEVLV IDSPHNSRAQ FPSTSGGSGY KNNGPGEMRR ARKRKHTIRC SYCGEEGHSK ETCDNESDKA QVFENLIITL QELTHTEMER SRVAPGEYND FSEPL.
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
Description:
Human Follicle Stimulating Hormone
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
Product # :
HOR-249Price :
Quantity :
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Shipped at Room temp
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Description
FSH Human is a glycoprotein produced from urine of post-menopausal women and having a total molecular mass of 30,000 Dalton.FSH is a heterodimeric hormone consisting of 92 amino acids a chain and 111 amino acids b chain.The FSH is purified by proprietary chromatographic techniques.
Source
Urine of post-menopausal women.
Formulation
The FSH was lyophilized with no additives.
More Info
-
Introduction
Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproductionIn women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production.
In men, FSH enhances the production of androgen-binding proteinby the Sertoli cells of the testes and is critical for spermatogenesis.
In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle.
Like its partner, LH, FSH release at the pituitary gland is controlled by pulses of gonadotropin-releasing hormone(GnRH). Those pulses, in turn, are subject to the estrogen feed-back from the gonads. -
Synonyms
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH-beta 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 Follicle Stimulating Hormone in sterile pyrogen free water at 2,000IU/1ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of FOLLICLE STIMULATING HORMONE HUMAN Protein?
FOLLICLE STIMULATING HORMONE HUMAN Protein has a total Mw of 30kDa.
What is the source or expression system of FOLLICLE STIMULATING HORMONE HUMAN Protein?
Urine of post-menopausal women.
What is the Biological Activity of FOLLICLE STIMULATING HORMONE HUMAN Protein?
The biological functionality of FOLLICLE STIMULATING HORMONE HUMAN Protein will be determined in the future.
What is the amino acid sequence of FOLLICLE STIMULATING HORMONE HUMAN Protein?
FOLLICLE STIMULATING HORMONE HUMAN Protein is composed from 92 amino acids a chain and 111 amino acids b chain.
What applications can FOLLICLE STIMULATING HORMONE HUMAN Protein be used in?
FOLLICLE STIMULATING HORMONE HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLICLE STIMULATING HORMONE HUMAN Protein?
The endotoxin level is minimal, FOLLICLE STIMULATING HORMONE HUMAN Protein was purified using conventional chromatography techniques.
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Contaminants
Less than: 0.1% hCG, 0.5%TSH, 0.5% LH, 0.5%GH and 0.5%Prl.Free of HbsAg, antibodies to HIV and HCV.
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 :
Glucagon HumanDescription:
Glucagon Human Recombinant
GLP1, GLP2, GRPP.
Product # :
HOR-237Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton. The Glucagon is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of recombinant Glucagon was formulated with 100mg of lactose.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.More Info
-
Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract. -
Synonyms
GLP1, GLP2, GRPP.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Glucagon although stable at room temperature for 3 weeks, should be stored at 40C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
-
Solubility
It is recommended to reconstitute the lyophilized Glucagon sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.
-
Background
What is the molecular weight/Mw of GLUCAGON HUMAN Protein?
GLUCAGON HUMAN Protein has a total Mw of 3.48kDa.
What is the source or expression system of GLUCAGON HUMAN Protein?
Escherichia Coli.
What is the Purity of GLUCAGON HUMAN Protein?
GLUCAGON HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GLUCAGON HUMAN Protein?
The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.
What is the amino acid sequence of GLUCAGON HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.
What applications can GLUCAGON HUMAN Protein be used in?
GLUCAGON HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GLUCAGON HUMAN Protein?
The endotoxin level is minimal, GLUCAGON 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 :
ConglutinDescription:
Allergen Ara h 6.0101 Recombinant
Conglutin, Allergen Ara h 6.
Product # :
ALR-009Price :
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Shipped with Ice Packs
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Description
Recombinant Conglutin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 16,217 Dalton. Conglutin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Conglutin is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Conglutin, also known as Ara h 6.0101 is a part of the 2S albumin protein family. Conglutin along with Ara h 2.0201 are considered as some of the most potent elicitors of anaphylaxis. Both proteins hold multiple disulphide-bridged cysteine residues, resulting in a tightly coiled, heat-stable, protease resistant core structure. Conglutin causes an allergic reaction in human and binds to IgE.
-
Synonyms
Conglutin, Allergen Ara h 6.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
IL 1 beta HumanDescription:
Interleukin-1 beta Human Recombinant
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-208Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton.The IL-1 Beta is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-1 Beta was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Phosphate buffer pH=7.1 and 150mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.More Info
-
Introduction
Interleukin-1b is produced by activated macrophages, IL-1 Beta stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 Beta 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.
-
Solubility
It is recommended to reconstitute the lyophilized Interleukin-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Val-Arg-Ser.
-
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.631 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-1 beta Recombinant as a Reference Standard.
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 :
EGFPDescription:
Enhanced Green Fluorescent Protein Recombinant
Green fluorescent protein, GFP.
Product # :
PRO-1606Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant EGFP produced in E.coli cells is a single non-glycosylated protein containing 239 amino acid chain and having a molecular mass of 26.9kDa. EGFP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGFP 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.More Info
-
Introduction
GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.
-
Synonyms
Green fluorescent protein, GFP.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized EGFP although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution EGFP should be stored at 40C between 2-7 days and for future use below -180C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized EGFP in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK
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 :
CFD HumanDescription:
Complement Factor D Human
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
Product # :
PRO-2699Price :
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Description
Human Complement Factor D produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 24kDa.
Source
Human Plasma.
Formulation
CFD protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.
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Synonyms
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
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Physical Appearance
Sterile filtered solution.
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Stability
CFD Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
CTGF Human, HEKDescription:
Connective Tissue Growth Factor Human Recombinant , HEK
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.
Product # :
CYT-687Price :
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Description
The CTGF Human Recombinant produced in HEK293 cells, is 36kDa protein containing a total of 329 amino acid residues (aa 27-349) including a C-terminal 6×His tag.
Source
HEK293 cells.
Formulation
CTGF filtered (0.2µm) solution in 0.1M Citrate buffer pH 4.7 and 20% (w/v) glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia. -
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF.
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Physical Appearance
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
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.
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Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 36kDa.
What is the source or expression system of CTGF Protein?
HEK293 cells.
What is the Purity of CTGF Protein?
CTGF Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CTGF Protein?
The biological functionality of CTGF Protein will be determined in the future.
What is the amino acid sequence of CTGF Protein?
QNCSGPCRCP DEPAPRCPAG VSLVLDGCGC CRVCAKQLGE LCTERDPCDP HKGLFCHFGS PANRKIGVCT AKDGAPCIFG GTVYRSGESF QSSCKYQCTC LDGAVGCMPL CSMDVRLPSP DCPFPRRVKL PGKCCEEWVC DEPKDQTVVG PALAAYRLED TFGPDPTMIR ANCLVQTTEW SACSKTCGMG ISTRVTNDNA SCRLEKQSRL CMVRPCEADL EENIKKGKKC IRTPKISKPI KFELSGCTSM KTYRAKFCGV CTDGRCCTPH RTTTLPVEFK CPDGEVMKKN MMFIKTCACH YNCPGDNDIF ESLYYRKMYG DMA HHHHHH.
What applications can CTGF Protein be used in?
CTGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTGF Protein?
The endotoxin level is minimal, CTGF 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 :
CGB HumanDescription:
CGB Human Recombinant
CGB3, CGB5, CGB7, CGB8, hCGB, CG-beta, CGB.
Product # :
HOR-007Price :
Quantity :
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Shipped with Ice Packs
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Description
CGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (21-165 a.a.) and having a molecular mass of 17.9kDa. CGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CGB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycoprotein hormones are heterodimers consisting of a common alpha subunit and a unique beta subunit which confers biological specificity. CGB is a member of the glycoprotein hormone beta chain family and is the beta 3 subunit of (CG). CG is produced by the trophoblastic cells of the placenta and stimulates the ovaries. The beta subunit of CG is encoded by 6 genes which are arranged in tandem and inverted pairs on chromosome 19q13.3 and contiguous with the luteinizing hormone beta subunit gene.
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Synonyms
CGB3, CGB5, CGB7, CGB8, hCGB, CG-beta, CGB.
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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 MGSSKEPLRP RCRPINATLA VEKEGCPVCI TVNTTICAGY CPTMTRVLQG VLPALPQVVC NYRDVRFESI RLPGCPRGVN PVVSYAVALS CQCALCRRST TDCGGPKDHP LTCDDPRFQD SSSSKAPPPS LPSPSRLPGP SDTPILPQ.
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 HumanDescription:
Growth and Differentiation Factor 15 Human Recombinant
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-335Price :
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Shipping Method :
Shipped at Room temp
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Description
GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
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 White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
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Background
What is the molecular weight/Mw of GDF15 HUMAN Protein?
GDF15 HUMAN Protein has a total Mw of 24.8kDa.
What is the source or expression system of GDF15 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF15 HUMAN Protein?
GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 HUMAN Protein?
The biological functionality of GDF15 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF15 HUMAN Protein?
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
What applications can GDF15 HUMAN Protein be used in?
GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 HUMAN Protein?
The endotoxin level is minimal, GDF15 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.