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1000 results found for “protein c-ets”
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Name :
CTSE HumanDescription:
Cathepsin-E Human Recombinant
Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.
Product # :
ENZ-776Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (57-363 a.a) and having a molecular mass of 35.4kDa.CTSE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CTSE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-E also known as CTSE is a gastric aspartyl protease which functions as a disulfide-linked homodimer. CTSE belongs to the peptidase C1 family; furthermore it has specificity similar to pepsin A and cathepsin D. CTSE is an intracellular proteinase which does not seem to be involved in the digestion of dietary protein and is found in the uppermost concentration in the surface of epithelial mucus-producing cells of the stomach. CTSE is the first aspartic proteinaseexpressed in the fetal stomach and is discovered in more than half of gastric cancers. For that reason CTSE is anoncofetal antigen. In addition, transcript variants utilizing alternative polyadenylation signals and two transcript variantsencoding different isoforms exist for this gene.
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Synonyms
Cathepsin E, EC 3.4.23.34, CATE, Erythrocyte Membrane Aspartic Proteinase, Slow-Moving Proteinase, EC 3.4.23.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTESCSMD QSAKEPLINY LDMEYFGTIS IGSPPQNFTV IFDTGSSNLW VPSVYCTSPA CKTHSRFQPS QSSTYSQPGQ SFSIQYGTGS LSGIIGADQV SVEGLTVVGQ QFGESVTEPG QTFVDAEFDG ILGLGYPSLA VGGVTPVFDN MMAQNLVDLP MFSVYMSSNP EGGAGSELIF GGYDHSHFSG SLNWVPVTKQ AYWQIALDNM LWSVPTLTSC RMSPSPLTES PIPSAQLPTP YWTSWMECSS AAVAFKDLTS TLQLGPSGSW GMSSFDSFTQ SLTVGITVWD WPQQSPKEGP CVCACLSDRP
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 :
CEA HumanDescription:
Carcinoembryonic Antigen Human Recombinant
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
Product # :
PRO-287Price :
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Description
CEA Human Recombinant is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells. CEA is a well-known tumor marker corresponding to the full length human CEA which is approximately 120,000 Dalton.
Source
Baculovirus Insect Cells.
Formulation
The sterile protein solution contains 10mM NaH2PO4, pH 7 and 150mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
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
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
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Physical Appearance
Sterile Filtered colourless solution.
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Stability
CEA should be stored at 2-8°C.Avoid freezing.
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 :
Troponin C-I-T ComplexDescription:
Cardiac Troponin C-I-T Complex Human
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z
Product # :
PRO-2741Price :
Quantity :
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Description
Human Cardiac Troponin C-I-T Complex Protein produced in Human heart tissue having a molecular mass of approximately 75kDa.
Source
Human cardiac tissue.
Formulation
Troponin C-I-T Complex solution (0.2µm filtered) contains 25mM TRIS buffer, 0.15M NaCl, 0.09% sodium azide, pH 7.5.
More Info
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Introduction
Troponin Complex is a heteromeric protein playing an important role in the regulation of skeletal and cardiac muscle contraction. It consists of three subunits, Troponin I , Troponin T and Troponin C. Each subunit is responsible for part of Troponin Complex function. E.g. Troponin I inhibits ATP-ase activity of acto-myosin. Troponin T and Troponin I are presented in cardiac muscles in different forms than in skeletal muscles. Purified subunits of rcTnI, rcTnC and rcTnT are recomplexed in vitro under appropriate conditions.
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z
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Physical Appearance
Sterile Filtered brown 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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Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Syphilis and HIV/HBV/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.
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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 :
Quantity :
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Shipped with Ice Packs
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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.
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.
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Name :
ECSIT HumanDescription:
ECSIT homolog Human Recombinant
ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.
Product # :
PRO-1241Price :
Quantity :
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Shipped with Ice Packs
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Description
ECSIT Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (19-217) and having a molecular mass of 24.6 kDa.ECSIT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ECSIT solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ECSIT homolog (ECSIT) is a ubiquitously expressed protein which has a vital role as an adaptor protein in the cytosolic signal transduction cascade events triggered by Toll receptor activation. ECSIT promotes proteolytic activation of MAP3K1. ECSIT is also involved in the BMP signaling pathway. ECSIT is essential for normal embryonic development. ECSIT was originally classified as a cytoplasmic protein interacting specifically with TNF receptor associated factor (TRAF)-6 in the TLR pathway. ECSIT gene knockdown results in gravely impaired complex I assembly and disrupted mitochondrial function.
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Synonyms
ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.
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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 MGSGTCGAAL TGTSISQVPL PKDSTGAADP PQPHIVGIQS PDQQAALARH NPARPVFVEG PFSLWLRNKC VYYHILRADL LPPEEREVEE TPEEWNLYYP MQLDLEYVRS GWDNYEFDIN EVEEGPVFAM CMAGAHDQAT MAKWIQGLQE TNPTLAQIPV VFRLAGSTRE LQTSSAGLEE PPLPEDHQEE DDNLQRQQQG QS
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 :
CEBPB AntibodyDescription:
CCAAT/enhancer-binding protein beta, Mouse Anti Human
CCAAT/enhancer-binding protein beta, C/EBP beta, Liver activator protein, Nuclear factor NF-IL6, Transcription factor 5, TCF-5, CEBPB, LAP, TCF5, CRP2, IL6DBP, MGC32080.
Product # :
ANT-406Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
CEBPB is an intronless gene and its protein is a bZIP transcription factor which can bind as a homodimer to certain DNA regulatory regions. CEBPB can also form heterodimers with the related proteins CEBP-alpha, CEBP-delta, and CEBP-gamma. CEBPB is important in the regulation of genes involved in immune and inflammatory responses and has been shown to bind to the IL-1 response element in the IL-6 gene, as well as to regulatory regions of several acute-phase and cytokine genes. In addition, CEBPB can bind the promoter and upstream element and stimulate the expression of the collagen type I gene.
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Synonyms
CCAAT/enhancer-binding protein beta, C/EBP beta, Liver activator protein, Nuclear factor NF-IL6, Transcription factor 5, TCF-5, CEBPB, LAP, TCF5, CRP2, IL6DBP, MGC32080.
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Immunogen
Anti-human CEBPB mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CEBPB amino acids 1-271 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P47A1AT.
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Applications
CEBPB antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
CEBPB antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
PIP ProteinDescription:
Prolactin-Induced Protein Human Recombinant
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
Product # :
CYT-793Price :
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Shipped with Ice Packs
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Description
PIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (29-146 a.a.) and having a molecular mass of 15.9kDa.PIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PIP protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Prolactin-inducible protein (PIP) is a main protein component of benign breast gross cysts. PIP is a famous indicator of breast cancer, since it is found in around 50% of all breast cancer specimens. PIP is expressed in exocrine glands, in pathologic conditions, in breast cysts and breast cancers exhibiting apocrine features. PIP and prostate specific antigen are co-expressed in androgen receptor-positive breast tumours.
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Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
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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 MGSQDNTRKI IIKNFDIPKS VRPNDEVTAV LAVQTELKEC MVVKTYLISS IPLQGAFNYK YTACLCDDNP KTFYWDFYTN RTVQIAAVVD VIRELGICPD DAAVIPIKNN RFYTIEILKV E.
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 :
Troponin C-I-T HumanDescription:
Cardiac Troponin C-I-T Complex Human Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-344Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Cardiac Troponin C-I-T complex produced in E.Coli is a single, non-glycosylated, polypeptide chain having the Molar ratio on cTnC to cTnI to cTnT of 1:1:1. Mw is approximately 90kDa.The Cardiac Troponin C-I-T complex is purified by proprietary chromatographic techniques
Source
Escherichia Coli.
Formulation
Human Cardiac Troponin C-I-T complex solution contains 500 mM NaCl, 20mM Tris-HCl, 4mM CaCl2, 4mM MgCl2and 60 mM B-mercaptoethanol, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
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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.
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 :
CST7 HumanDescription:
Cystatin 7 Human Recombinant
Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.
Product # :
PRO-2222Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CST7 Human Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (20-145) and having a molecular mass of 15.3kDa.CST7 is fused to a 7 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CST7 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cystatin 7 (CST7) is a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. Cystatin-7 is comprised of multiple cystatin-like sequences. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions. CST7 protein expression has been observed in numerous human cancer cell lines established from malignant tumors.
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Synonyms
Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.
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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
GPSPDTCSQD LNSRVKPGFP KTIKTNDPGV LQAARYSVEK FNNCTNDMFL FKESRITRAL VQIVKGLKYM LEVEIGRTTC KKNQHLRLDD CDFQTNHTLK QTLSCYSEVW VVPWLQHFEV PVLRCHHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CEBP Gamma HumanDescription:
CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
Product # :
PRO-434Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.
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Synonyms
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.
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 :
EGF Rat ProteinDescription:
Epidermal Growth Factor Rat
Urogastrone, URG, EGF.
Product # :
CYT-556Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.
Source
Adult Male Rat Submandibular Glands.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.
Purity
Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.15kDa.
What is the source or expression system of EGF RAT Protein?
Adult Male Rat Submandibular Glands.
What is the Purity of EGF RAT Protein?
EGF RAT Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF RAT Protein?
The biological functionality of EGF RAT Protein will be determined in the future.
What is the amino acid sequence of EGF RAT Protein?
EGF RAT Protein is composed from 53 amino acids.
What applications can EGF RAT Protein be used in?
EGF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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 :
BMP 4 HumanDescription:
Bone Morphogenetic Protein-4 Human Recombinant
BMP4, ZYME, BMP2B, BMP2B1.
Product # :
CYT-361Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
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Synonyms
BMP4, ZYME, BMP2B, BMP2B1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 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
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
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Background
What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant
As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.
Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.
Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!
How Does Bone Morphogenetic Protein-4 (BMP-4) Work?
Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.
The Role of BMP-4
This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.
However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:
- Embryonic development
- Wound healing
- Bone remodeling
- Immune response modulation
- Tissue repair
- Cardiac development and function
What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?
To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.
As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.
More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:
- Cancer therapy
- Development of engineered tissues and organs
- Bone regeneration for the treatment of osteoporosis and nonunion fractures
- Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
- Promotion of tissue repair and regeneration
Final Thoughts BMP-4
Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.
However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.
What is the molecular weight/Mw of BMP4 Protein?
BMP4 Protein has a total Mw of 13kDa.
What is the source or expression system of BMP4 Protein?
Escherichia Coli.
What is the Purity of BMP4 Protein?
BMP4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP4 Protein?
The biological functionality of BMP4 Protein will be determined in the future.
What is the amino acid sequence of BMP4 Protein?
SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.
What applications can BMP4 Protein be used in?
BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP4 Protein?
The endotoxin level is minimal, BMP4 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 :
ETHE1 HumanDescription:
Ethylmalonic Encephalopathy 1 Human Recombinant
Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.
Product # :
PRO-1027Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ETHE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (13-254) and having a molecular mass of 29.1kDa.ETHE1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ETHE1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ETHE1 is a mitochondrial sulfur dioxygenase involved in catabolism of sulfide that accumulates to toxic levels in ethylmalonic encephalopathy. Mutations of ETHE1 were detected in all the typical ethylmalonic encephalopathy patients analysed, but no ETHE1 mutations were identified in patients presenting with early onset progressive encephalopathy with ethylmalonic aciduria.
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Synonyms
Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLSQRG GSGAPILLRQ MFEPVSCTFT YLLGDRESRE AVLIDPVLET APRDAQLIKE LGLRLLYAVN THCHADHITG SGLLRSLLPG CQSVISRLSG AQADLHIEDG DSIRFGRFAL ETRASPGHTP GCVTFVLNDH SMAFTGDALL IRGCGRTDFQ QGCAKTLYHS VHEKIFTLPG DCLIYPAHDY HGFTVSTVEE ERTLNPRLTL SCEEFVKIMG NLNLPKPQQI DFAVPANMRC GVQTPTA
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HSA ProteinDescription:
HSA Human Protein
HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-354Price :
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Shipping Method :
Shipped with Ice Packs
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Description
HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.
Source
Human Serum.
Formulation
0.2gr/ml solution containing no additives.
Purity
Greater than 97.0% as determined by SDS-PAGE.
More Info
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Introduction
HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications. -
Synonyms
HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Sterile Filtered clear yellowish solution.
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Stability
HSA although stable at room temperature for 2 weeks should be stored at 4°C.
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 :
TCEAL1 HumanDescription:
Transcription Elongation Factor A (SII)-Like 1 Human Recombinant
Transcription elongation factor A protein-like 1, TCEA-like protein 1, Nuclear phosphoprotein p21/SIIR, Transcription elongation factor S-II protein-like 1, TCEAL1, SIIR, p21, pp21.
Product # :
PRO-507Price :
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Shipping Method :
Shipped with Ice Packs
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Description
TCEAL1 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-159 a.a.) and having a molecular mass of 19.7kDa. The TCEAL1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TCEAL1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Transcription elongation factor A protein-like 1 (TCEAL1) is a member of the transcription elongation factor A (SII)-like (TCEAL) family, which may function as nuclear phosphoproteins that modulate transcription in a promoter context-dependent manner. TCEAL1 is involved in transcriptional regulation. TCEAL1 is expressed in all tissues, especially highly expressed in the heart, ovary, prostate and skeletal muscle.
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Synonyms
Transcription elongation factor A protein-like 1, TCEA-like protein 1, Nuclear phosphoprotein p21/SIIR, Transcription elongation factor S-II protein-like 1, TCEAL1, SIIR, p21, pp21.
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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
MDKPRKENEE EPQSAPKTDE ERPPVEHSPE KQSPEEQSSE EQSSEEEFFP EELLPELLPE MLLSEERPPQ EGLSRKDLFE GRPPMEQPPC GVGKHKLEEG SFKERLARSR PQFRGDIHGR NLSNEEMIQA ADELEEMKRV RNKLMIMHWK AKRSRPYPIL EHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EHF HumanDescription:
Ets Homologous Factor Human Recombinant
ESE3, ESE3B, ESEJ, ETS homologous factor, hEHF, ETS domain-containing transcription factor, Epithelium-specific Ets transcription factor 3, EHF.
Product # :
PRO-1436Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EHF Human Recombinant produced in E. coli is a single polypeptide chain containing 323 amino acids (1-300) and having a molecular mass of 37.3kDa. EHF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EHF solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ETS homologous factor (EHF) is a part of the ESE subfamily of Ets transcription factors. Ets factors are an important kind of transcriptional regulators which take part in hema-topoiesis, angiogenesis, organogenesis, oncogenesis and specification of neuronal connectivity. EHF is expressed solely in a subset of epithelial cells, with highest expression noticed in glandular epithelium of the prostate, pancreas, salivary gland and trachea. EHF transactivates the c-Met promoter via 3 high affinity binding sites, which support the notion that EHF contribute to branching morphogenesis.
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Synonyms
ESE3, ESE3B, ESEJ, ETS homologous factor, hEHF, ETS domain-containing transcription factor, Epithelium-specific Ets transcription factor 3, EHF.
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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 MGSMILEGGG VMNLNPGNNL LHQPPAWTDS YSTCNVSSGF FGGQWHEIHP QYWTKYQVWE WLQHLLDTNQ LDANCIPFQE FDINGEHLCS MSLQEFTRAA GTAGQLLYSN LQHLKWNGQC SSDLFQSTHN VIVKTEQTEP SIMNTWKDEN YLYDTNYGST VDLLDSKTFC RAQISMTTTS HLPVAESPDM KKEQDPPAKC HTKKHNPRGT HLWEFIRDIL LNPDKNPGLI KWEDRSEGVF RFLKSEAVAQ LWGKKKNNSS MTYEKLSRAM RYYYKREILE RVDGRRLVYK FGKNARGWRE NEN.
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 :
PF 4 ProteinDescription:
Platelet Factor-4 Human (CXCL4)
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-234Price :
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Shipping Method :
Shipped at Room temp
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Description
Human PF-4 a 7.8 kDa protein consisting of 70 amino acid residues.
Source
Human Platelets.
Formulation
The CXCL4 protein was lyophilized in PBS buffer pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Human PF4 is used for the proof of heparin-induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL4 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
The sequence of the first four N-terminal amino acids was determined and was found to be Glu-Ala-Glu-Glu.
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 :
Protein-A/G/L-CysDescription:
Protein A/G/L-Cys Recombinant
Product # :
PRO-1934Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein- A/G/L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.
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 :
Protein-L, HisDescription:
Protein L Recombinant, His Tag
Product # :
PRO-1930Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 372 amino acids in total and having a molecular mass of 41.5kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHHHHHHKEE TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE DGGYTINIRF AG.
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 :
Cys-Protein-LDescription:
Cys-Protein L Recombinant
Product # :
PRO-1933Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- More Info
Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.
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 :
CUTC HumanDescription:
cutC Copper Transporter Homolog Human Recombinant
Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.
Product # :
PRO-911Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CUTC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-273 a.a) and having a molecular mass of 31.5kDa.CUTC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CUTC protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CUTC belongs to the Cut family and may be involved in efflux trafficking of cuprous ion. The Cut family is linked with the copper homeostasis and involved in several vital metabolisms, such as uptake, storage, delivery, and efflux of copper. Copper which is an essential heavy metal trace element has an imperative role in cell physiology.
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Synonyms
Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKRQGASSER KRARIPSGKA GAANGFLMEV CVDSVESAVN AERGGADRIE LCSGLSEGGT TPSMGVLQVV KQSVQIPVFV MIRPRGGDFL YSDREIEVMK ADIRLAKLYG ADGLVFGALT EDGHIDKELC MSLMAICRPL PVTFHRAFDM VHDPMAALET LLTLGFERVL TSGCDSSALE GLPLIKRLIE QAKGRIVVMP GGGITDRNLQ RILEGSGATE FHCSARSTRD SGMKFRNSSV AMGASLSCSE YSLKVTDVTK VRTLNAIAKN ILV.
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 :
CETN2 HumanDescription:
Centrin-2 Human Recombinant
Centrin-2, Caltractin isoform 1, CETN2, CALT, CEN2.
Product # :
PRO-060Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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- purity
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Description
CETN2 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 192 amino acids (1-172 a.a.) and having a molecular mass of 21.9kDa. The CETN2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CETN2 solution (0.5 mg/ml) 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Caltractin (CETN2) is a member of a family of calcium-binding proteins and is a structural component of the centrosome. CETN2 has a role in nucleotide excision repair via association with xeroderma pigmentosum group C protein, suggesting possible coupling of cell division and nucleotide excision repair.
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Synonyms
Centrin-2, Caltractin isoform 1, CETN2, CALT, CEN2.
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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 MASNFKKANM ASSSQRKRMS PKPELTEEQK QEIREAFDLF DADGTGTIDV KELKVAMRAL GFEPKKEEIK KMISEIDKEG TGKMNFGDFL TVMTQKMSEK DTKEEILKAF KLFDDDETGK ISFKNLKRVA KELGENLTDE ELQEMIDEAD RDGDGEVSEQ EFLRIMKKTS LY.
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 :
PCOLCE Human, Sf9Description:
Procollagen C-Endopeptidase Enhancer Human Recombinant, Sf9
Procollagen C-endopeptidase enhancer 1, Procollagen COOH-terminal proteinase enhancer 1, PCPE-1, Procollagen C-proteinase enhancer 1, Type 1 procollagen C-proteinase enhancer protein, Type I procollagen COOH-terminal proteinase enhancer, PCOLCE, PCPE1, Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase, Enhancer 1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1.
Product # :
ENZ-1075Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PCOLCE produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 433 amino acids (26-449 a.a.) and having a molecular mass of 46.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PCOLCE is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
PCOLCE protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.
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Synonyms
Procollagen C-endopeptidase enhancer 1, Procollagen COOH-terminal proteinase enhancer 1, PCPE-1, Procollagen C-proteinase enhancer 1, Type 1 procollagen C-proteinase enhancer protein, Type I procollagen COOH-terminal proteinase enhancer, PCOLCE, PCPE1, Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase, Enhancer 1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQDHHH 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 :
CEBP Alpha HumanDescription:
CCAAT/enhancer binding protein CEBP Alpha Human Recombinant
CCAAT/enhancer-binding protein alpha, C/EBP alpha, CEBPA, CEBP.
Product # :
PRO-433Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEBP-a Human Recombinant His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 126 (aa 270-358) and having a molecular mass of 14.5 kDa. The Human CEBP-a Human is fused to a 37 amino acids His-Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CCAAT/enhancer binding protein(C/EBP) a is a family of transcription factors that all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and that form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBPs differ significantly in their physiological functions and in their downstream target genes. For example, mice lacking C/EBPa die shortly after birth due to severe hypoglycemia and the absence of glycogen storage in liver, whereas knockout of C/EBPb causes defects in female reproduction.
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Synonyms
CCAAT/enhancer-binding protein alpha, C/EBP alpha, CEBPA, CEBP.
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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 KDRWGSMGAG KAKKSVDKNS NEYRVRRERN NIAVRKSRDK AKQRNVETQQ KVLELTSDND RLRKRVEQLS RELDTLRGIF RQLPESSLVKAMGNCA.
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.