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1000 results found for “secretoglobin”
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Name :
NOV HumanDescription:
Nephroblastoma Overexpressed Human Recombinant
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
Product # :
CYT-805Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.
Purity
Greater than 95.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Biological Activity
Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.More Info
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Introduction
Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.
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Synonyms
Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NOV although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NOV 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 NOV 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
MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M.
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 :
C.Albicans EnolaseDescription:
Candida Albicans Enolase Recombinant
Product # :
PRO-2297Price :
Quantity :
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Description
Recombinant Candida Albicans Enolase produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. C.Albicans Enolase is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
C.Albicans Enolase is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Candida albicans is a diploid fungus, which grows both as yeast and filamentous cells and a contributory agent of opportunistic oral and genital infections in humans, and candidal onychomycosis (an infection of the nail plate). Systemic fungal infections (fungemias) including those by C. albicans are regarded as key causes of morbidity and mortality in immunocompromised patients (e.g., AIDS, cancer chemotherapy, organ or bone marrow transplantation). C. albicans biofilms may develop on the surface of implantable medical devices. C. albicans is commensal and a constituent of the normal gut flora containing microorganisms which live in the human mouth and gastrointestinal tract. Overgrowth of the fungus leads to in candidiasis (candidosis). Candidiasis is frequently detected in immunocompromised persons, including HIV-infected patients. To infect host tissue, the habitual unicellular yeast-like form of C. albicans reacts to environmental signals and changes into an invasive, multicellular filamentous form, a phenomenon which is known as dimorphism.
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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. 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 :
Treponema TP0453Description:
Outer Membrane Protein Treponema pallidum Recombinant
Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453
Product # :
TRP-255Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Treponema pallidum Outer Membrane Protein TP0453 has a Mw of 26kDa, and was purified from E. coli.The Recombinant Treponema pallidum Outer Membrane Protein TP0453 is fused to 6 amino acid His tag at its C terminal and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Treponema TP0453 solution contains 25mM K2CO3 with PBS.
Purity
Protein is >95% pure as determined by SDS-PAGE (coomassie staining).
More Info
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Introduction
Tp0453 is a carrier of lipids and glycolipids during outer membrane. Tp045 is hypothesized to be a new type of bacterial outer membrane protein, which reduces T.pallidum outer membrane permeability to nutrients while remaining inaccessible to antibodies. Tp0453 exhibited 100% specificity and sensitivity in reaction with syphilis patients’ sera, giving negative result with Lyme disease, relapsing-fever or leptospirosis patients’ sera.
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Synonyms
Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453
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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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Applications
Rapid test, Immunoassay.
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 :
KLK3 ProteinDescription:
Kallikrein-3 Recombinant Human
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
Product # :
ENZ-1102Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Kallikrein-3 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 237 amino acids and having a molecular mass of 26.1kDa.KLK3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 3% trehalose.
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
Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KLK3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kallikrein-3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Kallikrein-3 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
IVGGWECEKH SQPWQVLVAS RGRAVCGGVL VHPQWVLTAA HCIRNKSVIL LGRHSLFHPE DTGQVFQVSH SFPHPLYDMS LLKNRFLRPG DDSSHDLMLL RLSEPAELTDA VKVMDLPTQE PALGTTCYAS GWGSIEPEEF LTPKKLQCVD LHVISNDVCA QVHPQKVTKF MLCAGRWTGG KSTCSGDSGG PLVCNGVLQG ITSWGSEPCA LPERPSLYTK VVHYRKWIKD TIVANP.
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 :
SERPINB4 HumanDescription:
Serpin Peptidase Inhibitor, Clade B Member 4 Human Recombinant
SERPINB4, Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member, Squamous Cell Carcinoma, Antigen, SCCA2, Serine (Or Cysteine) Proteinase Inhibitor, Clade B (Ovalbumin), Member, Peptidase Inhibitor, LEUPIN, SCCA, PI11, Protease Inhibitor (Leucine-Serpin) Squamous Cell Carcinoma Antigen, SCCA2/SCCA1 Fusion Protein, Serpin B4, SCCA1 PI-11.
Product # :
PRO-2208Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SERPINB4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-390 a.a) and having a molecular mass of 47.2kDa.SERPINB4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SERPINB4 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Serpin Peptidase Inhibitor, Clade B Member 4, also known as SERPINB4 is a member of the serpin family. SERPINB4 acts as a protease inhibitor to modulate the host immune response against tumor cells. Among the diseases associated with SERPINB4 are: inverted papilloma as well as burns.
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Synonyms
SERPINB4, Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member, Squamous Cell Carcinoma, Antigen, SCCA2, Serine (Or Cysteine) Proteinase Inhibitor, Clade B (Ovalbumin), Member, Peptidase Inhibitor, LEUPIN, SCCA, PI11, Protease Inhibitor (Leucine-Serpin) Squamous Cell Carcinoma Antigen, SCCA2/SCCA1 Fusion Protein, Serpin B4, SCCA1 PI-11.
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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 MGSMEDLCVA NTLFALNLFK HLAKASPTQN LFLSPWSISS TMAMVYMGSR GSTEDQMAKV LQFNEVGANA VTPMTPENFT SCGFMQQIQK GSYPDAILQA QAADKIHSSF RSLSSAINAS TGNYLLESVN KLFGEKSASF REEYIRLCQK YYSSEPQAVD FLECAEEARK KINSWVKTQT KGKIPNLLPE GSVDGDTRMV LVNAVYFKGK WKTPFEKKLN GLYPFRVNSA QRTPVQMMYL REKLNIGYIE DLKAQILELP YAGDVSMFLL LPDEIADVST GLELLESEIT YDKLNKWTSK DKMAEDEVEV YIPQFKLEEH YELRSILRSM GMEDAFNKGR ANFSGMSERN DLFLSEVFHQ AMVDVNEEGT EAAAGTGGVM TGRTGHGGPQ FVADHPFLFL IMHKITNCIL FFGRFSSP.
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 :
Cardiac Actin BovineDescription:
Cardiac Actin Bovine
Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.
Product # :
PRO-519Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ultra pure Cardiac Actin having a Molecular mass of 43,000 dalton.
Source
Bovine Heart.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 10mM Tris-acetate buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% SDS.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Alpha-cardiac actin belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in the cardiac actin have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).
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Synonyms
Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiac-Actin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cardiac Actin 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 Cardiac Actin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Protein standard in 1D and 2D SDS gelelectrophoresis
Immunoassays
Immunization.
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 :
KPNB1 HumanDescription:
Karyopherin Beta 1 Human Recombinant
Importin subunit beta-1, Importin-90, Karyopherin subunit beta-1, Nuclear factor p97, Pore targeting complex 97kDa subunit, PTAC97, KPNB1, NTF97.
Product # :
PRO-1001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KPNB1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 899 amino acids (1-876 a.a.) and having a molecular mass of 99.6kDa. KPNB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
KPNB1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
KPNB1 is a member of the importin beta family. The KPNB1 protein is engaged in nuclear protein import, either by coupling itself with an adapter protein (e.g., importin-alpha subunit which binds to nuclear localization signals (NLS) in cargo substrates), or by functioning autonomously as a nuclear transport receptor (acts as NLS receptor, docking of the importin/substrate complex to the nuclear pore complex).
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Synonyms
Importin subunit beta-1, Importin-90, Karyopherin subunit beta-1, Nuclear factor p97, Pore targeting complex 97kDa subunit, PTAC97, KPNB1, NTF97.
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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 MGSMELITIL EKTVSPDRLE LEAAQKFLER AAVENLPTFL VELSRVLANP GNSQVARVAA GLQIKNSLTS KDPDIKAQYQ QRWLAIDANA RREVKNYVLQ TLGTETYRPS SASQCVAGIA CAEIPVNQWP ELIPQLVANV TNPNSTEHMK ESTLEAIGYI CQDIDPEQLQ DKSNEILTAI IQGMRKEEPS NNVKLAATNA LLNSLEFTKA NFDKESERHF IMQVVCEATQ CPDTRVRVAA LQNLVKIMSL YYQYMETYMG PALFAITIEA MKSDIDEVAL QGIEFWSNVC DEEMDLAIEA SEAAEQGRPP EHTSKFYAKG ALQYLVPILT QTLTKQDEND DDDDWNPCKA AGVCLMLLAT CCEDDIVPHV LPFIKEHIKN PDWRYRDAAV MAFGCILEGP EPSQLKPLVI QAMPTLIELM KDPSVVVRDT AAWTVGRICE LLPEAAINDV YLAPLLQCLI EGLSAEPRVA SNVCWAFSSL AEAAYEAADV ADDQEEPATY CLSSSFELIV QKLLETTDRP DGHQNNLRSS AYESLMEIVK NSAKDCYPAV QKTTLVIMER LQQVLQMESH IQSTSDRIQF NDLQSLLCAT LQNVLRKVQH QDALQISDVV MASLLRMFQS TAGSGGVQED ALMAVSTLVE VLGGEFLKYM EAFKPFLGIG LKNYAEYQVC LAAVGLVGDL CRALQSNIIP FCDEVMQLLL ENLGNENVHR SVKPQILSVF GDIALAIGGE FKKYLEVVLN TLQQASQAQV DKSDYDMVDY LNELRESCLE AYTGIVQGLK GDQENVHPDV MLVQPRVEFI LSFIDHIAGD EDHTDGVVAC AAGLIGDLCT AFGKDVLKLV EARPMIHELL TEGRRSKTNK AKTLATWATK ELRKLKNQA.
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 :
COMMD9 HumanDescription:
COMM Domain Containing 9 Human Recombinant
COMM Domain Containing Protein 9, FLJ31106, HSPC166, COMM9.
Product # :
PRO-1244Price :
Quantity :
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Shipped with Ice Packs
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Description
COMMD9 Human Recombinant produced in E. coli is a single polypeptide chain containing 221 amino acids (1-198) and having a molecular mass of 24.2 kDa. COMMD9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The COMMD9 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
COMM domain-containing protein 9 (COMMD9), is a part of the COMMD family. The COMMD family is a group of evolutionary conserved proteins that share a common COMM domain at their extreme C-terminus, which provides an interface for protein-protein interactions. COMMD9 is a 198 amino acid ubiquitously expressed protein which contains one COMM domain and involved in signaling events all over the cell.
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Synonyms
COMM Domain Containing Protein 9, FLJ31106, HSPC166, COMM9.
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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 MGSMAALTAE HFAALQSLLK ASSKDVVRQL CQESFSSSAL GLKKLLDVTC SSLSVTQEEA EELLQALHRL TRLVAFRDLS SAEAILALFP ENFHQNLKNL LTKIILEHVS TWRTEAQANQ ISLPRLVDLD WRVDIKTSSD SISRMAVPTC LLQMKIQEDP SLCGDKPSIS AVTVELSKET LDTMLDGLGR IRDQLSAVAS K.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCL13 Human, HisDescription:
Monocyte Chemotactic Protein-4 Human Recombinant (CCL13), His-Tag
CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.
Product # :
CHM-275Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MCP4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 96 amino acids (24-98) and having a molecular mass of 10.8 kDa. The MCP-4 is fused to 21 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The His Tag 0.25mg/ml MCP4 protein solution contains PBS pH-7.4, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CCL13 chemokine is part of the CC chemokine family (TARC). CCL13 protein induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. CCL13 is induced by the inflammatory cytokines IL1 & TNFA.
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Synonyms
CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.
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Physical Appearance
Sterile Filtered colorless clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
.AHTLKT -
Background
What is the molecular weight/Mw of CCL13 HUMAN, HIS Protein?
CCL13 HUMAN, HIS Protein has a total Mw of 10.8kDa.
What is the source or expression system of CCL13 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL13 HUMAN, HIS Protein?
CCL13 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL13 HUMAN, HIS Protein?
The biological functionality of CCL13 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL13 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
.AHTLKT
What applications can CCL13 HUMAN, HIS Protein be used in?
CCL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL13 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL13 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Noggin HumanDescription:
Noggin Human Recombinant
SYM1, SYNS1, NOG.
Product # :
CYT-475Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.
More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC. -
Background
Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.
Abstract:
Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.
Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.
This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.
Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
- Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.
Molecular Characteristics of Noggin :
- This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.
Inhibition of BMP Signaling by Noggin:
- Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.
Physiological Functions of Noggin:
- Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.
Therapeutic Implications of Noggin:
- The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.
Clinical Studies and Translational Research:
- This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.
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 :
HSFY1 HumanDescription:
Heat Shock Transcription Factor, Y-Linked 1 Human Recombinant
Heat shock transcription factor, Y-linked, Heat shock transcription factor 2-like protein, HSF2-like, HSFY1, HSF2L, HSFY, HSFY2, Y-linked isoform 1, Y-Linked 1.
Product # :
HSP-059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HSFY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 424 amino acids (1-401) and having a molecular mass of 47.5kDa.HSFY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSFY1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Heat Shock Transcription Factor, Y-Linked 1 (HSFY1) is a member of the heat shock factor (HSF) family of transcriptional activators for heat shock proteins. HSFY1 is localizes to an area of chromosome Y which is from time to time deleted in infertile males and therefore is considered a gene for azoospermia. The genome has 2 identical duplicates of HSFY1 within a palindromic area.
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Synonyms
Heat shock transcription factor, Y-linked, Heat shock transcription factor 2-like protein, HSF2-like, HSFY1, HSF2L, HSFY, HSFY2, Y-linked isoform 1, Y-Linked 1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAHVSSE TQDVSPKDEL TASEASTRSP LCEHTFPGDS DLRSMIEEHA FQVLSQGSLL ESPSYTVCVS EPDKDDDFLS LNFPRKLWKI VESDQFKSIS WDENGTCIVI NEELFKKEIL ETKAPYRIFQ TDAIKSFVRQ LNLYGFSKIQ QNFQRSAFLA TFLSEEKESS VLSKLKFYYN PNFKRGYPQL LVRVKRRIGV KNASPISTLF NEDFNKKHFR AGANMENHNS ALAAEASEES LFSASKNLNM PLTRESSVRQ IIANSSVPIR SGFPPPSPST SVGPSEQIAT DQHAILNQLT TIHMHSHSTY MQARGHIVNF ITTTTSQYHI ISPLQNGYFG LTVEPSAVPT RYPLVSVNEA PYRNMLPAGN PWLQMPTIAD RSAAPHSRLA LQPSPLDKYH PNYN.
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 :
MIA Human, HisDescription:
Melanoma Inhibitory Activity Protein Human Recombinant, His Tag
Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.
Product # :
CYT-810Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (25-131) and having a molecular mass of 14.4 kDa.MIA is fused to a 21 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The MIA solution (0.25mg/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
The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain. MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.
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Synonyms
Melanoma-derived growth regulatory protein precursor, Cartilage-derived retinoic acid-sensitive protein, CD-RAP, MIA.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGPMPKLADR KLCADQECSH PISMAVALQD YMAPDCRFLT IHRGQVVYVF SKLKGRGRLF WGGSVQGDYY GDLAARLGYF PSSIVREDQT LKPGKVDVKT DKWDFYCQ
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 :
HB-EGF HumanDescription:
HB-EGF Human Recombinant
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
Product # :
CYT-119Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.
More Info
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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
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Synonyms
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-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 Human HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
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Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.9kDa.
What is the source or expression system of HB-EGF Protein?
Escherichia Coli.
What is the Purity of HB-EGF Protein?
HB-EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.
What is the amino acid sequence of HB-EGF Protein?
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
What applications can HB-EGF Protein be used in?
HB-EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-EGF 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 :
ADAM10 Human, Sf9Description:
A Disintegrin and Metalloproteinase Domain 10 Human Recombinant, Sf9
Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.
Product # :
PRO-2359Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ADAM10 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 467 amino acids (214-672 aa) and having a molecular mass of 51.6kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).ADAM10 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ADAM10 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
ADAM10 is part of the ADAM family which are cell surface proteins with a distinctive structure possessing both potential adhesion and protease domains. ADAM10 cleaves many proteins including TNF-alpha and E-cadherin. ADAM10 cleaves the membrane-bound precursor of tnf-alpha at 76- ala-|-val-77 to its mature soluble form. ADAM10 is in charge for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-a2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein ADAM10 is involved in the normal cleavage of the cellular prion protein. ADAM10 is involved in the cleavage of the adhesion molecule l1 at the cell surface and in the release of membrane vesicles, suggesting a vesicle-based protease activity. ADAM10 controls the proteolytic processing of notch and mediates lateral inhibition during neurogenesis.
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Synonyms
Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
TTSAEKNTCQ LYIQTDHLFF KYYGTREAVI AQISSHVKAI DTIYQTTDFS GIRNISFMVK RIRINTTADE KDPTNPFRFP NIGVEKFLEL NSEQNHDDYC LAYVFTDRDF DDGVLGLAWV GAPSGSSGGI CEKSKLYSDG KKKSLNTGII TVQNYGSHVP PKVSHITFAH EVGHNFGSPH DSGTECTPGE SKNLGQKENG NYIMYARATS GDKLNNNKFS LCSIRNISQV LEKKRNNCFV ESGQPICGNG MVEQGEECDC GYSDQCKDEC CFDANQPEGR KCKLKPGKQC SPSQGPCCTA QCAFKSKSEK CRDDSDCARE GICNGFTALC PASDPKPNFT DCNRHTQVCI NGQCAGSICE KYGLEECTCA SSDGKDDKEL CHVCCMKKMD PSTCASTGSV QWSRHFSGRT ITLQPGSPCN DFRGYCDVFM RCRLVDADGP LARLKKAIFS PELYENIAEL EHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
UXT HumanDescription:
Ubiquitously-Expressed, Prefoldin-Like Chaperone Human Recombinant
Protein UXT, Androgen receptor trapped clone 27 protein, ART-27, Ubiquitously expressed transcript protein, UXT, HSPC024, STAP1.
Product # :
PRO-1312Price :
Quantity :
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Shipped with Ice Packs
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Description
UXT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (1-157 a.a.) and having a molecular mass of 20.4kDa.UXT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UXT protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitously-expressed transcript (UXT) is a member of the UXT family. UXT serves as a cofactor which modulates androgen receptor-dependent transcription, and also has a crucial role in tumor necrosis factor-induced apoptosis. UXT gene expression has a role in tumorigenesis. UXT is ubiquitous expressed: it is expressed in prostate epithelial cells, overexpressed in a number of tumor tissues. The highest levels are found in the heart, skeletal muscle, pancreas, kidney, liver, adrenal gland, peripheral blood leukocytes, lymph node, prostate, and thyroid and the lowest levels in bladder and uterus.
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Synonyms
Protein UXT, Androgen receptor trapped clone 27 protein, ART-27, Ubiquitously expressed transcript protein, UXT, HSPC024, STAP1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATPPKRRAV EATGEKVLRY ETFISDVLQR DLRKVLDHRD KVYEQLAKYL QLRNVIERLQ EAKHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE LTLAEALKFI DRKSSLLTEL SNSLTKDSMN IKAHIHMLLE GLRELQGLQN FPEKPHH.
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 :
CALM HumanDescription:
Calmodulin Human
Calmodulin, CaM, CALM.
Product # :
PRO-2799Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Source
Human brain tissue.
Formulation
CALM was lyophilized with 2mM EDTA.
Purity
Greater than 95.0%.
More Info
-
Synonyms
Calmodulin, CaM, CALM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin 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 CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Blood samples from tissue donors were tested and found to be negative for syphilis, HBsAg, HIV-1 and HIV-2 antibodies and HCV.
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Background
Calmodulin, a small, ubiquitous calcium-binding protein, stands as a linchpin in cellular signalling cascades. Its ability to modulate diverse cellular processes by transducing calcium signals has made it a focal point of scientific inquiry. With its role extending from muscle contraction to neurotransmitter release and gene expression, calmodulin orchestrates intricate physiological responses. This research delves into the multifaceted world of calmodulin, exploring its structural characteristics, calcium-binding properties, and its pivotal involvement in various biological pathways.
Structural Marvel of Calmodulin:
Calmodulin boasts a unique dumbbell-shaped structure, composed of four EF-hand motifs that enable it to bind calcium ions. When calcium binds to calmodulin, it undergoes a conformational change, allowing it to interact with a myriad of target proteins. This structural adaptability is fundamental to its ability to regulate a wide array of cellular activities.
Calcium Signalling and Transduction:
Intracellular calcium serves as a ubiquitous second messenger, and calmodulin is the key mediator of calcium signalling. When calcium levels rise, calmodulin binds calcium ions, triggering its activation. This activated form of calmodulin modulates the activity of various proteins, including enzymes, ion channels, and transcription factors. By doing so, calmodulin influences processes such as muscle contraction, neurotransmitter release, and cell proliferation.
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 :
HSP90 Alpha HumanDescription:
Heat Shock Protein-90 Alpha Human Recombinant
HSPN, LAP2, HSP86, HSPC1, HSPCA, Hsp89, Hsp90, HSP90A, HSP90N, HSPCAL1, HSPCAL4, FLJ31884, Heat shock protein HSP 90-alpha, Renal carcinoma antigen NY-REN-38, HSP 86, HSP90AA1.
Product # :
HSP-090Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human HSP-90 produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 1-732) containing 752 amino acids and having a molecular mass of 86.8kDa. HSP90 is expressed with a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSP90 protein solution contains PBS, pH-7.4 and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HSP90 has been identified in the cytosol, nucleus and endoplasmic reticulum, and is reported to exist in many tissue types. In several tissues, including smooth muscle, HSP90 comprises up to 2% of total cellular protein. HSP90 functions as a dimer, assembled as part of heterocomplex. It possesses ATP-binding site and low ATPase activity. HSP90 is able to associate with actin filaments in certain conditions. Another important property of HSP90 is the binding of unoccupied steroid hormone receptors. HSP90 has been characterized as a molecular chaperone able to keep the target protein in a folding-competent state. It has an enhanced chaperone activity in oligomeric form at high temperatures. HSP90 function is sensitive to bivalent cations concentration.
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Synonyms
HSPN, LAP2, HSP86, HSPC1, HSPCA, Hsp89, Hsp90, HSP90A, HSP90N, HSPCAL1, HSPCAL4, FLJ31884, Heat shock protein HSP 90-alpha, Renal carcinoma antigen NY-REN-38, HSP 86, HSP90AA1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED KEEEKEKEEK ESEDKPEIED VGSDEEEEKK DGDKKKKKKI KEKYIDQEEL NKTKPIWTRN PDDITNEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFVPRRAPFD LFENRKKKNN IKLYVRRVFI MDNCEELIPE YLNFIRGVVD SEDLPLNISR EMLQQSKILK VIRKNLVKKC LELFTELAED KENYKKFYEQ FSKNIKLGIH EDSQNRKKLS ELLRYYTSAS GDEMVSLKDY CTRMKENQKH IYYITGETKD QVANSAFVER LRKHGLEVIY MIEPIDEYCV QQLKEFEGKT LVSVTKEGLE LPEDEEEKKK QEEKKTKFEN LCKIMKDILE KKVEKVVVSN RLVTSPCCIV TSTYGWTANM ERIMKAQALR DNSTMGYMAA KKHLEINPDH SIIETLRQKA EADKNDKSVK DLVILLYETA LLSSGFSLEDPQTHANRIYR MIKLGLGIDE DDPTADDTSA AVTEEMPPLE GDDDTSRMEE VD.
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 :
Shipping Method :
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
-
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.
-
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 :
CCL21 MouseDescription:
Exodus-2 Mouse Recombinant (CCL21)
Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.
Product # :
CHM-371Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
Exodus-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 110 amino acids and having a molecular mass of 12kDa. The CCL21 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer and 0.15M NaCl pH-7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE & RP-HPLC.
Biological Activity
Determined by its ability to chemoattract total murine T cell population using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 21 (CCL21) is a small cytokine belonging to the CC chemokine family. This chemokine is also known as 6Ckine (because it has six conserved cysteine residues instead of the four cysteines typical to chemokines), exodus-2, and secondary lymphoid-tissue chemokine (SLC). CCL21 is expressed predominantly in the lymph nodes and, in contrast to other CC chemokines, is chemotactic for lymphocytes. The gene for CCL21 is located on human chromosome 9. CCL21 elicits its effects by binding to a cell surface chemokine receptor known as CCR7.
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Synonyms
Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Exodus-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL21 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 Exodus2 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
SDGGGQDCCL KYSQKKIPYS IVRGYRKQEP SLGCPIPAIL FLPRKHSKPE LCANPEEGWV QNLMRRLDQP PAPGKQSPGC RKNRGTSKSG KKGKGSKGCK RTEQTQPSRG.
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Background
What is the molecular weight/Mw of CCL21 MOUSE Protein?
CCL21 MOUSE Protein has a total Mw of 12kDa.
What is the source or expression system of CCL21 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL21 MOUSE Protein?
CCL21 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL21 MOUSE Protein?
Determined by its ability to chemoattract total murine T cell population using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL21 MOUSE Protein?
SDGGGQDCCL KYSQKKIPYS IVRGYRKQEP SLGCPIPAIL FLPRKHSKPE LCANPEEGWV QNLMRRLDQP PAPGKQSPGC RKNRGTSKSG KKGKGSKGCK RTEQTQPSRG.
What applications can CCL21 MOUSE Protein be used in?
CCL21 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL21 MOUSE Protein?
The endotoxin level is minimal, CCL21 MOUSE 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 :
Cor a 1.0401Description:
Major Pollen Allergen Cor a 1 .0401 Recombinant
Major allergen Cor a 1.0401, CORA1.0401.
Product # :
ALR-012Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
Recombinant Cor a 1.0401 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 18,952 Dalton. Cor a 1.0401 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Cor a 1.0401 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Cor a 1.0401 is a part of the Bet v1 homologues family and is related to the major hazel pollen allergen Cor a 1.0103. Cor a 1.0401 is a hazelnut allergen from Corylus avellana.
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Synonyms
Major allergen Cor a 1.0401, CORA1.0401.
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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. Avoid multiple freeze-thaw cycles.
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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 :
LCN2 MouseDescription:
Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Mouse Recombinant
Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.
Product # :
ENZ-875Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
LCN2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-200 a.a) and having a molecular mass of 23.3kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCN2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke. -
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.
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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 MGSQDSTQNL IPAPSLLTVP LQPDFRSDQF RGRWYVVGLA GNAVQKKTEG SFTMYSTIYE LQENNSYNVT SILVRDQDQG CRYWIRTFVP SSRAGQFTLG NMHRYPQVQS YNVQVATTDY NQFAMVFFRK TSENKQYFKI TLYGRTKELS PELKERFTRF AKSLGLKDDN IIFSVPTDQC IDN.
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 :
C5a MouseDescription:
Complement Component C5a Mouse Recombinant
Complement C5, Hemolytic complement, C5, Hc, He, C5a.
Product # :
PRO-085Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
C5a Mouse Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9kDa.The Mouse C5a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Mouse C5a was lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.5 and 350mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 of Recombinant Mouse C5a as determined by its ability to induce N-acetyl-b-D-glucosaminidase release from differentiated U937 human histiocytic lymphoma cells was 5-20ng/ml.More Info
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Introduction
Mouse Complement 5a (C5a) is a glycoprotein which is a member of a family of structurally and functionally related proteins known as anaphylatoxins. C5a is a 77 a.a. peptide created by the C5a convertase proteolytic cleavage of C5 ? chain in the classical and alternative complement pathway (C4b2a3b, C3bBb3b). The mouse C5a has four ? helices and three intrachain disulfide bonds which form a triple loop structure. C5a functions through G-protein coupled receptor (GPCR) (C5aR/CD88). C5a is a effective chemoattractant and anaphylatoxin which functions on all classes of leukocytes and on many other cell types including endothelial, smooth muscle, kidney, liver, and neural cells. Mouse C5a also mediates IL-8 release from bronchial epithelial cells. Furthermore, it triggers an oxidative surge in macrophages and neutrophils, causing the release of histamine in basophils and mast cells. The C5a anaphylatoxin activity on hepatocytes results indirectly from interaction with nonparenchymal cell via prostanoid secretion.
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Synonyms
Complement C5, Hemolytic complement, C5, Hc, He, C5a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse C5a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse C5a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Mouse C5a 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 five N-terminal amino acids was determined and was found to be Asn-Leu-His-Leu-Leu.
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 :
CXCL9 MouseDescription:
MIG Mouse Recombinant (CXCL9)
Small inducible cytokine B9, CXCL9, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, M119.
Product # :
CHM-337Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
MIG (CXCK9) Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 12208 Dalton. The MIG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH7.4 and 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability to chemoattract Human lymphocytes using a concentration of 0.1-1 ng/ml.More Info
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Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by MIG. CXCL9 is a T-cell chemoattractant. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
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Synonyms
Small inducible cytokine B9, CXCL9, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, M119.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL9 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 MIG 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
TLVIRNARCS CISTSRGTIH YKSLKDLKQF APSPNCNKTE IIATLKNGDQ TCLDPDSANV KKLMKEWEKK INQKKKQKRG KKHQKNMKNR KPKTPQSRRR SRKTT.
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Background
What is the molecular weight/Mw of CXCL9 MOUSE Protein?
CXCL9 MOUSE Protein has a total Mw of 12.2kDa.
What is the source or expression system of CXCL9 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL9 MOUSE Protein?
CXCL9 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL9 MOUSE Protein?
The Activity is calculated by the ability to chemoattract Human lymphocytes using a concentration of 0.1-1 ng/ml.
What is the amino acid sequence of CXCL9 MOUSE Protein?
TLVIRNARCS CISTSRGTIH YKSLKDLKQF APSPNCNKTE IIATLKNGDQ TCLDPDSANV KKLMKEWEKK INQKKKQKRG KKHQKNMKNR KPKTPQSRRR SRKTT.
What applications can CXCL9 MOUSE Protein be used in?
CXCL9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL9 MOUSE Protein?
The endotoxin level is minimal, CXCL9 MOUSE 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.