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1000 results found for “Maltose Binding Protein”
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Name :
MAGEA8 HumanDescription:
Melanoma Antigen Family A, 8 Human Recombinant
Melanoma Antigen Family A8, MAGE-8 Antigen, MAGE8, Cancer/Testis Antigen 1.8, CT1.8, Cancer/Testis Antigen Family 1, Member 8, Cancer/Testis Antigen Family 1, Melanoma-Associated Antigen 8, Melanoma Antigen Family A, 8, Member 8, MAGEA8.
Product # :
PRO-2206Price :
Quantity :
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Shipped with Ice Packs
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Description
MAGEA8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 37.6kDa.MAGEA8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAGEA8 protein solution (0.25mg/ml) containing Phosphate Buffered Saline, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Melanoma Antigen Family A 8, also known as MAGEA8 belongs to the MAGE gene family, which includes twelve known genes, of which six are expressed in tumors. Furthermore, the MAGE genes were at first isolated from different kinds of tumors, and according to their virtually exclusive tumor-specific expression in adult tissues, they have been used as targets for cancer immunotherapy.
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Synonyms
Melanoma Antigen Family A8, MAGE-8 Antigen, MAGE8, Cancer/Testis Antigen 1.8, CT1.8, Cancer/Testis Antigen Family 1, Member 8, Cancer/Testis Antigen Family 1, Melanoma-Associated Antigen 8, Melanoma Antigen Family A, 8, Member 8, MAGEA8.
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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 MGSMLLGQKS QRYKAEEGLQ AQGEAPGLMD VQIPTAEEQK AASSSSTLIM GTLEEVTDSG SPSPPQSPEG ASSSLTVTDS TLWSQSDEGS SSNEEEGPST SPDPAHLESL FREALDEKVA ELVRFLLRKY QIKEPVTKAE MLESVIKNYK NHFPDIFSKA SECMQVIFGI DVKEVDPAGH SYILVTCLGL SYDGLLGDDQ STPKTGLLII VLGMILMEGS RAPEEAIWEA LSVMGLYDGR EHSVYWKLRK LLTQEWVQEN YLEYRQAPGS DPVRYEFLWG PRALAETSYV KVLEHVVRVN ARVRISYPSL HEEALGEEKG V.
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 :
POP4 HumanDescription:
Processing Of Precursor 4 Human Recombinant
RPP29, Ribonuclease P protein subunit p29, hPOP4.
Product # :
PRO-1407Price :
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Description
POP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a.) and having a molecular mass of 27.8kDa.POP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
POP4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Processing of Precursor 4 (POP4) is a member of the eukaryotic/archaeal RNase P protein component 1 family. POP4 is one of the protein subunits of the small nucleolar ribonucleoprotein complexes: the endoribonuclease for mitochondrial RNA processing complex and the ribonuclease P complex. POP4 is confined to the nucleus and associates promptly with the RNA component of this complexes.POP4 is participating in processing of precursor RNAs.
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Synonyms
RPP29, Ribonuclease P protein subunit p29, hPOP4.
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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 MGSMKSVIYH ALSQKEANDS DVQPSGAQRA EAFVRAFLKR STPRMSPQAR EDQLQRKAVV LEYFTRHKRK EKKKKAKGLS ARQRRELRLF DIKPEQQRYS LFLPLHELWK QYIRDLCSGL KPDTQPQMIQ AKLLKADLHG AIISVTKSKC PSYVGITGIL LQETKHIFKI ITKEDRLKVI PKLNCVFTVE TDGFISYIYG SKFQLRSSER SAKKFKAKGT IDL.
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 :
FLRT3 Human, HEKDescription:
Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant, HEK
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
Product # :
PRO-2805Price :
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Description
FLRT3 Human Recombinant is a single, glycosylated, polypeptide chain (29-528 a.a) containing a total of 506 amino acids and having a molecular mass of 57.3 kDa. FLRT3 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
FLRT3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
>40%. Measured by the ability of the immobilized protein to support the adhesion of Neuro-2a neuroblast cells. When cells are added to human FLRT3 coated plates 5 ug/ml.
More Info
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Synonyms
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
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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
KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS
YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN
PTTTLNREQE KEPYKNPNLP HHHHHH. -
Background
Fibronectin leucine-rich transmembrane protein 3, commonly known as FLRT3, stands as a molecular architect in the intricate landscape of neural development. Its roles, initially discovered in the embryonic nervous system, have expanded to encompass various physiological and pathological processes in both the brain and beyond. This research endeavors to unravel the enigma of FLRT3 protein, exploring its structural intricacies, physiological functions, and its far-reaching implications in neurobiology, embryogenesis, and disease. By delving into FLRT3's multifaceted roles, scientists aim to decipher the underlying mechanisms that govern its diverse functions and explore potential therapeutic avenues in the realms of neuroscience and beyond.
Structural Complexities of FLRT3:
FLRT3 belongs to the FLRT family, characterized by extracellular leucine-rich repeats (LRRs) and a transmembrane domain. These structural motifs enable FLRT3 to participate in a myriad of interactions, including binding with cell adhesion molecules and guidance cues. Understanding the three-dimensional architecture of FLRT3 is fundamental for unraveling its molecular partnerships, biological activities, and its contributions to cell adhesion and signaling.
Physiological Functions in Neural Development:
In the developing nervous system, FLRT3 acts as a guidance molecule, steering growing axons and dendrites to their precise destinations. Through interactions with other cell surface receptors and ligands, FLRT3 modulates axon pathfinding, synapse formation, and neuronal migration. Its presence in growth cones and developing neural circuits underscores its significance in sculpting the intricate neural networks essential for proper brain function.
Beyond Neural Development:
Beyond its canonical roles in neurodevelopment, FLRT3 has emerged as a versatile player in various physiological processes. It participates in tissue morphogenesis, modulates cell adhesion, and influences immune responses. Recent studies have also implicated FLRT3 in cancer progression, highlighting its involvement in pathological conditions and making it a potential target for therapeutic interventions in cancer therapy.
FLRT3 as a Therapeutic Target:
The diverse roles of FLRT3 in neural development and diseases position it as an attractive target for therapeutic interventions. Modulating FLRT3 interactions offers novel avenues for neurological disorder treatments, including neurodevelopmental disorders and neurodegenerative diseases. Moreover, understanding FLRT3's involvement in cancer biology opens doors for innovative cancer therapies, making it a promising target for precision medicine approaches.
FLRT3, with its intricate structural features and diverse functional roles, stands as a linchpin in the realms of neuroscience, embryogenesis, and disease. Its multifaceted contributions to neural development, tissue morphogenesis, and disease pathogenesis underscore its significance in both health and pathology. As researchers continue to unravel FLRT3’s complexities, they not only deepen our understanding of fundamental biological processes but also pave the way for groundbreaking discoveries in neuroscience and therapeutic interventions, ultimately shaping the future landscape of medicine and scientific inquiry.
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 :
SERPING1 HumanDescription:
Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant
C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.
Product # :
PRO-1401Price :
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Description
SERPING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 499 amino acids (23-500a.a) and having a molecular mass of 55.1kDa. SERPING1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SERPING1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.
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Synonyms
C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.
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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 MNPNATSSSS QDPESLQDRG EGKVATTVIS KMLFVEPILE VSSLPTTNST TNSATKITAN TTDEPTTQPT TEPTTQPTIQ PTQPTTQLPT DSPTQPTTGS FCPGPVTLCS DLESHSTEAV LGDALVDFSL KLYHAFSAMK KVETNMAFSP FSIASLLTQV LLGAGENTKT NLESILSYPK DFTCVHQALK GFTTKGVTSV SQIFHSPDLA IRDTFVNASR TLYSSSPRVL SNNSDANLEL INTWVAKNTN NKISRLLDSL PSDTRLVLLN AIYLSAKWKT TFDPKKTRME PFHFKNSVIK VPMMNSKKYP VAHFIDQTLK AKVGQLQLSH NLSLVILVPQ NLKHRLEDME QALSPSVFKA IMEKLEMSKF QPTLLTLPRI KVTTSQDMLS IMEKLEFFDF SYDLNLCGLT EDPDLQVSAM QHQTVLELTE TGVEAAAASA ISVARTLLVF EVQQPFLFVL WDQQHKFPVF MGRVYDPRA.
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 :
GM-CSF Human, PichiaDescription:
Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Pichia
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
Product # :
CYT-324Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in Yeast is a single, glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 26-32 kDa. rhGMCSF differs from the natural human GM-CSF by a substitution of leucine at position 23 (R to L), and the carbohydrate moiety may be different from the native protein. GM-CSF is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM phosphate buffer pH 7.0, 40 mg mannitol and 10 mg sucrose.
Purity
Greater than 97.0% as determined by1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating 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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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
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Background
What is the molecular weight/Mw of GM-CSF HUMAN, PICHIA Protein?
GM-CSF HUMAN, PICHIA Protein has a total Mw of 29kDa.
What is the source or expression system of GM-CSF HUMAN, PICHIA Protein?
Pichia Pastoris.
What is the Purity of GM-CSF HUMAN, PICHIA Protein?
GM-CSF HUMAN, PICHIA Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF HUMAN, PICHIA Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.183 ng/ml, corresponding to a Specific Activity of 5,500,000IU/mg.
What is the amino acid sequence of GM-CSF HUMAN, PICHIA Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
What applications can GM-CSF HUMAN, PICHIA Protein be used in?
GM-CSF HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF HUMAN, PICHIA Protein?
The endotoxin level is minimal, GM-CSF HUMAN, PICHIA 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 :
SIGLEC10 HumanDescription:
Sialic Acid Binding Ig Like Lectin 10 Human Recombinant
SIGLEC10, PRO940, SLG2, SIGLEC-10, Sialic acid-binding Ig-like lectin 10 isoform 3, Siglec-like protein 2.
Product # :
PRO-2610Price :
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Shipped with Ice Packs
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Description
SIGLEC10 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 678 amino acids (17-455 a.a.) and having a molecular mass of 75.6kDa. SIGLEC10 is expressed with a 239 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The SIGLEC10 solution (0.25mg/ml) contains 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
Sialic Acid Binding Ig Like Lectin 10(SIGLEC10) is a part of the immunoglobulin superfamily that is expressed on eosinophils, B cells, monocytes and neutrophils. SIGLEC10 is an adhesion molecule that mediates sialic-acid dependent binding to cells.SIGLEC10 is a ligand for CD52, the target of the therapeutic monoclonal antibody Alemtuzumab. Also, it binds to Vascular adhesion protein 1 (VAP-1) and to the co-stimulatory molecule CD24.This binding is modulated by cis interactions of SIGLEC10 with sialated molecules on the same cell.
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Synonyms
SIGLEC10, PRO940, SLG2, SIGLEC-10, Sialic acid-binding Ig-like lectin 10 isoform 3, Siglec-like protein 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDGRFWIRVQ ESVMVPEGLC ISVPCSFSYP RQDWTGSTPA YGYWFKAVTE TTKGAPVATN
HQSREVEMST RGRFQLTGDP AKGNCSLVIR DAQMQDESQY FFRVERGSYV RYNFMNDGFF
LKVTALTQKP DVYIPETLEP GQPVTVICVF NWAFEECPPP SFSWTGAALS SQGTKPTTSH
FSVLSFTPRP QDHNTDLTCH VDFSRKGVSA QRTVRLRVAY APRDLVISIS RDNTPALEPQ
PQGNVPYLEA QKGQFLRLLC AADSQPPATL SWVLQNRVLS SSHPWGPRPL GLELPGVKAG
DSGRYTCRAE NRLGSQQRAL DLSVQYPPEN LRVMVSQANR TVLENLGNGT SLPVLEGQSL
CLVCVTHSSP PARLSWTQRG QVLSPSQPSD PGVLELPRVQ VEHEGEFTCH ARHPLGSQHV
SLSLSVHYKK GLISTAFSNL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR
TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN
GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS
DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.
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 :
HRSP12 HumanDescription:
Heat-Responsive Protein 12 Human Recombinant
Ribonuclease UK114, 14.5 kDa translational inhibitor protein, p14.5, Heat-responsive protein 12, UK114 antigen homolog, HRSP12, PSP.
Product # :
PRO-052Price :
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Description
HRSP12 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 157 amino acids (1-137 a.a.) and having a molecular mass of 16.6kDa. The HRSP12 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HRSP12 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HRSP12 (UK114) is an endoribonuclease found mainly in the human adult kidney and liver, and which is responsible for inhibiting translation by cleaving mRNA. HRSP12 cleaves phosphodiester bonds only in single-stranded RNA. HRSP12 may be an important biomarker for heptatic carcinoma.
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Synonyms
Ribonuclease UK114, 14.5 kDa translational inhibitor protein, p14.5, Heat-responsive protein 12, UK114 antigen homolog, HRSP12, PSP.
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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 MSSLIRRVIS TAKAPGAIGP YSQAVLVDRT IYISGQIGMD PSSGQLVSGG VAEEAKQALK NMGEILKAAG CDFTNVVKTT VLLADINDFN TVNEIYKQYF KSNFPARAAY QVAALPKGSR IEIEAVAIQG PLTTASL.
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 :
RPL26 HumanDescription:
Ribosomal Protein L26 Human Recombinant
L26, Ribosomal Protein L26, 60S Ribosomal Protein L26.
Product # :
PRO-1538Price :
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Description
RPL26 Human Recombinant produced in E. coli is a single polypeptide chain containing 168 amino acids (1-145) and having a molecular mass of 19.6kDa. RPL26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPL26 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Ribosomal Protein L26 (RPL26) is a ribosomal protein which is a component of the 60S subunit (the large subunit of the ribosome). RPL26 is a part of the L24P family of ribosomal proteins which is located in the cytoplasm. There are numerous processed pseudogenes of RPL26 dispersed through the genome as usual for genes encoding ribosomal proteins.
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Synonyms
L26, Ribosomal Protein L26, 60S Ribosomal Protein L26.
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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 MGSMKFNPFV TSDRSKNRKR HFNAPSHIRR KIMSSPLSKE LRQKYNVRSM PIRKDDEVQV VRGHYKGQQI GKVVQVYRKK YVIYIERVQR EKANGTTVHV GIHPSKVVIT RLKLDKDRKK ILERKAKSRQ VGKEKGKYKE ETIEKMQE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
B.Microti p32Description:
Babesia Microti p32 Recombinant
Product # :
PRO-2269Price :
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Shipped with Ice Packs
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Description
Recombinant Babesia Microti p32 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 35,808 Dalton. B.Microti p32 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
B.Microti p32 is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Babesiosis is a disease caused by apicomplexan parasites of the Babesia genus. The Babesia microti life cycle involves 2 hosts, which include a rodent, mainly the white-footed mouse (Peromyscus leucopus) and a tick in the Ixodes genus. During a blood meal, a Babesia-infected tick introduces sporozoites into the mouse host. Sporozoites pass into the erythrocytes and undergo asexual reproduction (budding). In the blood, some parasites differentiate into male and female gametes, though these cannot be distinguished by light microscopy. The definitive host is the tick. Once ingested by an proper tick, gametes unite and undergo a sporogonic cycle resulting in sporozoites. Transovarial transmission (aka vertical or hereditary transmission) has been detected for "large" Babesia species but not for the "small" Babesia, such as B. microti. Humans enter the cycle when bitten by the infected ticks. Thus during a blood meal, a Babesia-infected tick introduces sporozoites into the human host. Sporozoites then enter erythrocytes and undergo asexual replication (budding). Multiplication of the blood-stage parasites is responsible for the clinical manifestations of the disease. Humans typically are dead-end hosts. However, human-to-human transmission is well acknowledged to occur via contaminated blood transfusions.
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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 :
CENPB HumanDescription:
Centromere Protein B Human Recombinant
Major centromere autoantigen B, Centromere protein B, CENP-B, CENPB.
Product # :
PRO-390Price :
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Shipped with Ice Packs
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Description
CENPB Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 80kDa. CENPB is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
CENPB is supplied at a concentration of in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Centromere proteins are a group of proteins which form and/or mediate the function of centromeres, the central structures of chromosomes to which spindle fibers/microtubuli attach and pull the chromosomes apart in cell division. Currently, 9 centromere proteins are known and designated CENPA to CENP-I. Most of the centromere proteins are targets of autoantibodies, the anti-centromere antibodies.
CENPB is the most important of the centromeric autoantigens: it has a molecular weight of approx. 66 kDa and plays an important role in the formation of the centromeric chromatin. CENPB antibodies are present in the sera of up to 80% of patients with CREST syndrome. -
Synonyms
Major centromere autoantigen B, Centromere protein B, CENP-B, CENPB.
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Physical Appearance
Sterile Filtered liquid formulation.
-
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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coating concentration
0.15-0.375 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.
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 :
SERPINA3 HumanDescription:
Alpha-1 AntiChymotrypsin Human
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Product # :
PRO-378Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Alpha-1 AntiChymotrypsin produced from normal human serum having a molecular mass of 68kDa.
Source
Human Serum.
Formulation
Lyophilized from 0.02M Tris-buffer,pH-7.5 and 0.15M Nacl.
Purity
Greater than 90.0%.
More Info
-
Introduction
Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1- ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT. -
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Human SERPINA3 although stable at room temperature for 3 weeks, should be stored between 2-8°C. Do not freeze.
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Solubility
It is recommended to reconstitute the lyophilized human A1ACT in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.
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 :
GSTP1 AntibodyDescription:
Glutathione S-Transferase pi 1, Mouse Anti Human
Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.
Product # :
ANT-729Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells. -
Synonyms
Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human GSTP1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GSTP1 amino acids 1-210 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
PAT12C10AT
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Applications
GSTP1 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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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
GSTP1 antibody was purified from mouse ascitic fluids by protein-A 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.
- View Data Sheet
Name :
CMC1 HumanDescription:
COX Assembly Mitochondrial Protein 1 Human Recombinant
C3orf68, Cmc1p, COX assembly mitochondrial protein homolog.
Product # :
PRO-1651Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CMC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106 a.a.) and having a molecular mass of 14.9kDa.CMC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CMC1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
COX Assembly Mitochondrial Protein 1(CMC1) is a member of the CMC family. CMC1 is required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. CMC1 attaches copper and might be involved in copper trafficking and distribution to COX and SOD1.
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Synonyms
C3orf68, Cmc1p, COX assembly mitochondrial protein homolog.
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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 MGSMALDPAD QHLRHVEKDV LIPKIMREKA KERCSEQVQD FTKCCKNSGV LMVVKCRKEN SALKECLTAY YNDPAFYEEC KMEYLKEREE FRKTGIPTKK RLQKLPTSM.
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 :
MIF Human His CDescription:
Macrophage Migration Inhibitory Factor Human Recombinant, His Tag C-Terminus
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-521Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MIF human Recombinant, fused to His-tag at C-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques.Macrophage Inducing Factor Human Recombinant is a single, non-glycosylated, polypeptide chaincontaining 123 amino acidsand having a molecular mass of 13.5 kDa.
Source
Escherichia Coli.
Formulation
Human MIF was lyophilized from a 1mg/ml solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind rhCD74 in a functional ELISA.More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF 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
MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPC
ALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTF
ALEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CANX HumanDescription:
Calnexin Human Recombinant
Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.
Product # :
PRO-725Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CANX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 462 amino acids (21-481 a.a.) and having a molecular mass of 52.5kDa.The CANX is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CANX protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.
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Synonyms
Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.
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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
MHDGHDDDVI DIEDDLDDVI EEVEDSKPDT TAPPSSPKVT YKAPVPTGEV YFADSFDRGT LSGWILSKAK KDDTDDEIAK YDGKWEVEEM KESKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTPELNLDQF HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGIYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIPDPEAV KPDDWDEDAP AKIPDEEATK PEGWLDDEPE YVPDPDAEKP EDWDEDMDGE WEAPQIANPR CESAPGCGVW QRPVIDNPNY KGKWKPPMID NPSYQGIWKP RKIPNPDFFE DLEPFRMTPF SAIGLELWSM TSDIFFDNFI ICADRRIVDD WANDGWGLKK AADGAAEPGV VGQMIEAAEE RP.
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 :
RHOD HumanDescription:
Ras Homolog Gene Family Member D Human Recombinant
Rho-related GTP-binding protein RhoD, Rho-related protein HP1, RhoHP1, RHOD, ARHD, Rho, RHOM.
Product # :
PRO-190Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RHOD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (18-207 a.a.) and having a molecular mass of 23.8kDa.RHOD is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RHOD solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 200mM NaCl, 2mM EDTA and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Rho-related GTP-binding protein (RhoD) is a member of the small GTPase superfamily. The small GTPase Rho D promotes the rearrangement of the actin cytoskeleton and cell surface and also regulates endosome motility and distribution.
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Synonyms
Rho-related GTP-binding protein RhoD, Rho-related protein HP1, RhoHP1, RHOD, ARHD, Rho, RHOM.
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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 MVKVVLVGDG GCGKTSLLMV FADGAFPESY TPTVFERYMV NLQVKGKPVH LHIWDTAGQD DYDRLRPLFY PDASVLLLCF DVTSPNSFDN IFNRWYPEVN HFCKKVPIIV VGCKTDLRKD KSLVNKLRRN GLEPVTYHRG QEMARSVGAV AYLECSARLH
DNVHAVFQEA AEVALSSRGR NFWRRITQGF 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.
- View Data Sheet
Name :
SRGN HumanDescription:
Serglycin Human Recombinant
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
Product # :
PRO-965Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.
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Synonyms
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
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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 MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.
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 :
MOBKL3 HumanDescription:
MOB1, Mps One Binder kinase Activator-Like 3 Human Recombinant
Mps one binder kinase activator-like 3, 2C4D, Class II mMOB1, Mob1 homolog 3, Mob3, Preimplantation protein 3, MOBKL3, MOB3, PREI3, MOB1, PREI3, CGI-95, MGC12264.
Product # :
PRO-049Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MOBKL3 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 245 amino acids (1-225 a.a.) and having a molecular mass of 28.1kDa. The MOBKL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MOBKL3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) containing 0.2M Nacl, 5mM DTT, 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Mps one binder kinase activator-like 3 (MOBKL3) is a member of the MOB1/Phocein family and is phosphorylated on serine residues. MOBKL3 is usually linked with membranes but can be present in the cytosol, where it behaves as a protein complex. MOBKL3 is the major partner of the striatin family members, which are scaffolding proteins involved in signaling and trafficking.
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Synonyms
Mps one binder kinase activator-like 3, 2C4D, Class II mMOB1, Mob1 homolog 3, Mob3, Preimplantation protein 3, MOBKL3, MOB3, PREI3, MOB1, PREI3, CGI-95, MGC12264.
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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 MVMAEGTAVL RRNRPGTKAQ DFYNWPDESF DEMDSTLAVQ QYIQQNIRAD CSNIDKILEP PEGQDEGVWK YEHLRQFCLE LNGLAVKLQS ECHPDTCTQM TATEQWIFLC AAHKTPKECP AIDYTRHTLD GAACLLNSNK YFPSRVSIKE SSVAKLGSVC RRIYRIFSHA YFHHRQIFDE YENETFLCHR FTKFVMKYNL MSKDNLIVPI LEEEVQNSVS GESEA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Description:
Adiponectin Globular Recombinant, His Tag
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-277Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Acrp30 Human has a total of 171 amino acids. N-terminal underlined amino acids are His-tag and the protease cleavage site (31AA-Underlined). The AA sequence of Acrp30 Human is homologous to the 105-244 amino acid sequence of the Human full-length Adiponectin (Swiss-prot entry Q15848).
Source
Escherichia Coli.
Formulation
Acrp30 Human is a filtered powder, lyophilized from 0.6mg/ml in PBS buffer.
Purity
Purity of Acrp30 Human is greater than 95% as determined by SDS PAGE.
More Info
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Introduction
Adiponectin is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Stability
For long term, store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized Acrp30 Human remains stable for 24 months when stored at -20°C.
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Solubility
Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.
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Amino Acid Sequence
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
TYW5 HumanDescription:
tRNA-yW Synthesizing Protein 5 Human Recombinant
tRNA wybutosine-synthesizing protein 5, hTYW5, TYW5, C2orf60.
Product # :
PRO-1315Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
TYW5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (1-315 a.a.) and having a molecular mass of 38.9kDa.TYW5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TYW5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
tRNA wybutosine-synthesizing protein 5 (TYW5) functions as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position closest to the anticodon of eukaryotic phenylalanine tRNA. TYW5 catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW). OHyW is a derivative of wybutosine observed in higher eukaryotes.
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Synonyms
tRNA wybutosine-synthesizing protein 5, hTYW5, TYW5, C2orf60.
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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 MGSMAGQHLP VPRLEGVSRE QFMQHLYPQR KPLVLEGIDL GPCTSKWTVD YLSQVGGKKE VKIHVAAVAQ MDFISKNFVY RTLPFDQLVQ RAAEEKHKEF FVSEDEKYYL RSLGEDPRKD VADIRKQFPL LKGDIKFPEF FKEEQFFSSV FRISSPGLQL WTHYDVMDNL LIQVTGKKRV VLFSPRDAQY LYLKGTKSEV LNIDNPDLAK YPLFSKARRY ECSLEAGDVL FIPALWFHNV ISEEFGVGVN IFWKHLPSEC YDKTDTYGNK DPTAASRAAQ ILDRALKTLA ELPEEYRDFY ARRMVLHIQD KAYSKNSE.
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 :
Leptin Receptor ChickenDescription:
Leptin Receptor Chicken Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
Product # :
CYT-509Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.
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Physical Appearance
Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.
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Stability
Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of Leptin Binding Domain as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IMPAD1 Human, ActiveDescription:
Inositol Monophosphatase Domain Containing 1 Human Recombinant, BioActive
Inositol monophosphatase 3, IMP 3, IMPase 3, EC 3.1.3.25, EC 3.1.3.7, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3, IMPAD1, IMPA3, GPAPP, IMP-3
Product # :
PRO-2638Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IMPAD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (34-359 a.a.) and having a molecular mass of 37.6kDa.IMPAD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IMPAD1 solution (0.25mg/ml) contains Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3300pmol/min/ug, and is defined as its ability to dephosphorylate adenosine 3'5'-diphosphate sodium slat at pH7.5, 25˚C.
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Introduction
Inositol Monophosphatase Domain Containing 1 or IMPAD1 is a protein, part of the inositol monophosphatase group of proteins. The protein is found in Golgi apparatus and enhances phosphoadenosine phosphate hydrolysis to adenosine monophosphate. When Mutation in the IMPAD1 gene occurs leads to GRAPP type chondrodysplasia and therefore joint dislocations. On long arm chromosome 1 a pseudogene can be found.
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Synonyms
Inositol monophosphatase 3, IMP 3, IMPase 3, EC 3.1.3.25, EC 3.1.3.7, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3, IMPAD1, IMPA3, GPAPP, IMP-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 MGSGRFSLFG LGGEPGGGAA GPAAAADGGT VDLREMLAVS VLAAVRGGDE VRRVRESNVL HEKSKGKTRE GAEDKMTSGD VLSNRKMFYL LKTAFPSVQI NTEEHVDAAD QEVILWDHKI PEDILKEVTT PKEVPAESVT VWIDPLDATQ EYTEDLRKYV TTMVCVAVNG KPMLGVIHKP FSEYTAWAMV DGGSNVKARS SYNEKTPRIV VSRSHSGMVK QVALQTFGNQ TTIIPAGGAG YKVLALLDVP DKSQEKADLY IHVTYIKKWD ICAGNAILKA LGGHMTTLSG EEISYTGSDG IEGGLLASIR MNHQALVRKL PDLEKTGHK
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 2 Human, HEKDescription:
Bone Morphogenetic protein-2 Human Recombinant, HEK
BMP-2, BMP2A.
Product # :
CYT-080Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BMP-2 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 28kDa due to glycosylation. The BMP2 is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The BMP2 was lyophilized from 0.67mg/ml in 2xPBS + 6% ethanol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.
More Info
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Introduction
BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.
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Synonyms
BMP-2, BMP2A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-2 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 BMP-2 in sterile 4mM HCl containing 0.1% endotoxin-free recombinant HSA.
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Amino Acid Sequence
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.
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Background
What is the molecular weight/Mw of BMP2 Protein?
BMP2 Protein has a total Mw of 28kDa.
What is the source or expression system of BMP2 Protein?
Hek.
What is the Purity of BMP2 Protein?
BMP2 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP2 Protein?
The specific activity as determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) was found to be 6.53ng/ml.
What is the amino acid sequence of BMP2 Protein?
QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNST NHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR.
What applications can BMP2 Protein be used in?
BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP2 Protein?
The endotoxin level is minimal, BMP2 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 :
UBL3 HumanDescription:
Ubiquitin-Like 3 Human Recombinant
Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.
Product # :
PRO-230Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UBL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-114a.a) and having a molecular mass of 15.0kDa.UBL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBL3 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
UBL3 - a member of the ubiquitin-like family is found in the membrane. UBL3 holds two N-glycosylation sites, a C-terminal prenylation site and a protein kinase C phosphorylation site. Even though Ubiquitin-like proteins are not directly involved in protein degradation, it seems they have several mechanistic similarities to the ubiquitin pathway.
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Synonyms
Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
UBL3 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSNVPADMI NLRLILVSGK TKEFLFSPND SASDIAKHVY DNWPMDWEEE QVSSPNILRL IYQGRFLHGN VTLGALKLPF GKTTVMHLVA RETLPEPNSQ GQRNREKTGE SNCC
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.