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Search results

1000 results found for “TTC”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    CST3 Rat, sf9

    Description:

    Cystatin C Rat Recombinant, sf9

    Cystatin-C, Cystatin-3.

    Product # :

    PRO-2311

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CST3 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 128 amino acids (21-140a.a.) and having a molecular mass of 14.3kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). CST3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques

    Source

    Sf9, Baculovirus cells.

    Formulation

    CST3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      GTSRPPPRLL GAPQEADASE EGVQRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGI NYYLDVEMGR TTCTKSQTNL TNCPFHDQPH LMRKALCSFQ IYSVPWKGTH TLTKSSCKNA LEHHHHHH.

    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.

    Cst3 Rat Sf9
  • View Data Sheet

    Name :

    SMNDC1 Human

    Description:

    Survival Motor Neuron Domain Containing 1 Human Recombinant

    SMNR, SMN-related protein, SPF30, Survival Motor Neuron Domain Containing 1, 30kDa Splicing Factor SMNrp, Splicing Factor 30, Survival of Motor Neuron-related.

    Product # :

    PRO-035

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    SMNDC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 258 amino acids (1-238a.a.) and having a molecular mass of 28.9kDa.SMNDC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SMNDC1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SMNDC1 is a vital splicing factor obligatory for spliceosome assembly which is a part of the SMN family. SMNDC1 has one Tudor domain with significant similarity to Survival Motor Neuron (SMN) and is expressed in heart, pancreas and skeletal muscle, localizing to Cajal bodies and nuclear speckles. Mutations in SMNDC1 are cause of autosomal recessive proximal spinal muscular atrophy.

    • Synonyms

      SMNR, SMN-related protein, SPF30, Survival Motor Neuron Domain Containing 1, 30kDa Splicing Factor SMNrp, Splicing Factor 30, Survival of Motor Neuron-related.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSEDLAKQLA SYKAQLQQVE AALSGNGENE DLLKLKKDLQ EVIELTKDLL STQPSETLAS SDSFASTQPT HSWKVGDKCM AVWSEDGQCY EAEIEEIDEE NGTAAITFAG YGNAEVTPLL NLKPVEEGRK AKEDSGNKPM SKKEMIAQQR EYKKKKALKK AQRIKELEQE REDQKVKWQQ FNNRAYSKNK KGQVKRSIFA SPESVTGKVG VGTCGIADKP MTQYQDTSKY NVRHLMPQ

    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.

    Smndc1 Human
  • View Data Sheet

    Name :

    ATF4 Human

    Description:

    Activating Transcription Factor-4 Human Recombinant

    Cyclic AMP-dependent transcription factor ATF-4, cAMP-dependent transcription factor, ATF-4, Activating transcription factor 4, Cyclic AMP-responsive element-binding protein 2, CREB-2, cAMP-responsive element-binding protein 2, DNA-binding protein, TAXREB67, Tax-responsive enhancer element-binding protein 67, TaxREB67, ATF4, CREB2, TXREB.

    Product # :

    PKA-006

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • purity
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    Description

    ATF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 510 amino acids (1-351 a.a.) and having a molecular mass of 56.6kDa.ATF4 is fused to a 159 amino acid His-Calmodulin-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ATF4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Activating transcription factor 4 (ATF4) is a member of a family of DNA-binding proteins which includes the AP-1 family of transcription factors, cAMP-response element binding proteins and CREB-like proteins. The ATF4 gene encodes a transcription factor which was initially identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1.

    • Synonyms

      Cyclic AMP-dependent transcription factor ATF-4, cAMP-dependent transcription factor, ATF-4, Activating transcription factor 4, Cyclic AMP-responsive element-binding protein 2, CREB-2, cAMP-responsive element-binding protein 2, DNA-binding protein, TAXREB67, Tax-responsive enhancer element-binding protein 67, TaxREB67, ATF4, CREB2, TXREB.

    • Physical Appearance

      ATF4 is supplied as a 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.

    • Amino Acid Sequence

      MHHHHHHMAD QLTEEQIAEF KEAFSLFDKD GDGTITTKEL GTVMRSLGQN PTEAELQDMI NEVDADGNGT IDFPEFLTMM ARKMKDTDSE EEIREAFRVF DKDGNGYISA AELRHVMTNL GEKLTDEEVD EMIREADIDG DGQVNYEEFV QMMTAKGSHM TEMSFLSSEV LVGDLMSPFD
      QSGLGAEESL GLLDDYLEVA KHFKPHGFSS DKAKAGSSEW LAVDGLVSPS NNSKEDAFSG TDWMLEKMDL KEFDLDALLG IDDLETMPDD LLTTLDDTCD LFAPLVQETN KQPPQTVNPI GHLPESLTKP DQVAPFTFLQ PLPLSPGVLS STPDHSFSLE LGSEVDITEG DRKPDYTAYV
      AMIPQCIKEE DTPSDNDSGI CMSPESYLGS PQHSPSTRGS PNRSLPSPGV LCGSARPKPY DPPGEKMVAA KVKGEKLDKK LKKMEQNKTA ATRYRQKKRA EQEALTGECK ELEKKNEALK ERADSLAKEI QYLKDLIEEV RKARGKKRVP.

    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.

    Atf4 Human
  • View Data Sheet

    Name :

    OCM Human

    Description:

    Oncomodulin-1 Human Recombinant

    Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

    Product # :

    PRO-143

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • More Info

    Description

    The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    Oncomodulin-1 was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    More Info

    • Introduction

      Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.

    • Synonyms

      Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.

    • Applications

      Western blotting.

    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.

    Ocm Human
  • View Data Sheet

    Name :

    TACSTD2 Human, sf9

    Description:

    Tumor-Associated Calcium Signal Transducer 2 Human Recombinant, Sf9

    Tumor-Associated Calcium Signal Transducer 2,Membrane Component Chromosome 1 Surface Marker 1, Pancreatic Carcinoma Marker Protein GA733-1,Cell Surface Glycoprotein Trop-2, GA733-1,TROP2, M1S1, 40kD Glycoprotein, Identified By Monoclonal Antibody GA733,Membrane Component, Chromosome 1, Surface Marker 1, Gastrointestinal Tumor-Associated Antigen GA7331,Pancreatic Carcinoma Marker Protein GA7331,Cell Surface Glycoprotein TROP2,Epithelial Glycoprotein-1Truncated TACSTD2,GA7331,EGP-1,EGP1,GP50, TACSTD2.

    Product # :

    PRO-2364

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    TACSTD2 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 253 amino acids (31-274a.a) and having a molecular mass of 28.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).TACSTD2 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TACSTD2 protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor-associated calcium signal transducer 2 (TACSTD2), is a member of to the EPCAM family. TACSTD2 is an intronless gene which encodes a carcinoma-associated antigen. TACSTD2 may act as a growth factor receptor and as a cell surface receptor that transduces calcium signals. Mutations of TACSTD2 have been associated with gelatinous drop-like corneal dystrophy.

    • Synonyms

      Tumor-Associated Calcium Signal Transducer 2,Membrane Component Chromosome 1 Surface Marker 1, Pancreatic Carcinoma Marker Protein GA733-1,Cell Surface Glycoprotein Trop-2, GA733-1,TROP2, M1S1, 40kD Glycoprotein, Identified By Monoclonal Antibody GA733,Membrane Component, Chromosome 1, Surface Marker 1, Gastrointestinal Tumor-Associated Antigen GA7331,Pancreatic Carcinoma Marker Protein GA7331,Cell Surface Glycoprotein TROP2,Epithelial Glycoprotein-1Truncated TACSTD2,GA7331,EGP-1,EGP1,GP50, TACSTD2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPQDNCTCP TNKMTVCSPD GPGGRCQCRA LGSGMAVDCS TLTSKCLLLK ARMSAPKNAR TLVRPSEHAL VDNDGLYDPD CDPEGRFKAR QCNQTSVCWC VNSVGVRRTD KGDLSLRCDE LVRTHHILID LRHRPTAGAF NHSDLDAELR RLFRERYRLH PKFVAAVHYE QPTIQIELRQNTSQKAAGDV DIGDAAYYFE RDIKGESLFQ GRGGLDLRVR GEPLQVERTL IYYLDEIPPK FSMKRLTHHH HHH.

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    Tacstd2 Human Sf9
  • View Data Sheet

    Name :

    CANT1 Human

    Description:

    Calcium Activated Nucleotidase 1 Human Recombinant

    Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.

    Product # :

    PRO-1010

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    Description

    CANT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (63-401 a.a.) and having a molecular mass of 40.5kDa. CANT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CANT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.

    • Synonyms

      Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMRPAPG RPPTHNAHNW RLGQAPANWY NDTYPLSPPQ RTPAGIRYRI AVIADLDTES RAQEENTWFS YLKKGYLTLS DSGDKVAVEW DKDHGVLESH LAEKGRGMEL SDLIVFNGKL YSVDDRTGVV YQIEGSKAVP WVILSDGDGT VEKGFKAEWL AVKDERLYVG GLGKEWTTTT GDVVNENPEW VKVVGYKGSV DHENWVSNYN ALRAAAGIQP PGYLIHESAC WSDTLQRWFF LPRRASQERY SEKDDERKGA NLLLSASPDF GDIAVSHVGA VVPTHGFSSF KFIPNTDDQI IVALKSEEDS GRVASYIMAF TLDGRFLLPE TKIGSVKYEG IEFI.

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    Cant1 Human
  • View Data Sheet

    Name :

    GCA Human

    Description:

    Grancalcin Human Recombinant

    Grancalcin EF-hand calcium binding protein, GCL, Grancalcin penta-EF-hand protein.

    Product # :

    PRO-080

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    Description

    GCA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217.a.) and having a molecular mass of 26.1kDa. GCA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GCA protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Grancalcin is calcium-binding protein which is particularly abundant in human neutrophils. GCA is a member of the penta EF-hand (PEF) subfamily of EF-hand proteins, who also comprises calpain, sorcin, peflin, and ALG-2. GCA undergoes essential conformational changes upon binding of calcium, which subsequently exposes hydrophobic amino acid residues, that direct the protein to hydrophobic surfaces. GCA cooperates with L-plastin, a protein known to have actin bundling activity, which suggests that GCA has a part in the regulation of neutrophils adhesion.

    • Synonyms

      Grancalcin EF-hand calcium binding protein, GCL, Grancalcin penta-EF-hand protein.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAYPGYGGGF GNFSIQVPGM QMGQPVPETG PAILLDGYSG PAYSDTYSSA GDSVYTYFSA VAGQDGEVDA EELQRCLTQS GINGTYSPFS LETCRIMIAM LDRDHTGKMG FNAFKELWAA LNAWKENFMT VDQDGSGTVE HHELRQAIGL MGYRLSPQTL TTIVKRYSKN GRIFFDDYVA CCVKLRALTD FFRKRDHLQQ GSANFIYDDF LQGTMAI

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    Gca Human
  • View Data Sheet

    Name :

    MAPT Human

    Description:

    Microtubule-Associated Protein Tau Human Recombinant

    TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.

    Product # :

    PRO-295

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    Description

    MAPT Recombinant Human (Isoform-4) produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352 a.a.) and having a molecular mass of 38.9 kDa (Real molecular weight on SDS-PAGE will be shift up). The MAPT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAPT solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPT is a neuronal microtubule associated protein localized mostly on axons.
      MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain.

    • Synonyms

      TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL.

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    Mapt Human
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    • Activity

    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    bdnf activity - Product image 1

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

      What is the source or expression system of BDNF Protein?
      Escherichia Coli.

      What is the Purity of BDNF Protein?
      BDNF Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

      What applications can BDNF Protein be used in?
      BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BDNF Protein?
      The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 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 standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.

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    Bdnf Human
  • View Data Sheet

    Name :

    RTN4IP1 Human

    Description:

    Reticulon 4 Interacting Protein 1 Human Recombinant

    Reticulon-4-interacting protein 1 mitochondrial, NOGO-interacting mitochondrial protein, RTN4IP1, NIMP.

    Product # :

    PRO-1014

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    Description

    RTN4IP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 379 amino acids (41-396 a.a.) and having a molecular mass of 41.4kDa. RTN4IP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RTN4IP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      RTN4IP1 is a unique mitochondrial protein that interacts with reticulon 4, which is an effective inhibitor of regeneration ensuing spinal cord injury. The reticulon 4 interaction with mitochondrial proteins may offer insight into the mechanisms for reticulon-induced inhibition of neurite growth.

    • Synonyms

      Reticulon-4-interacting protein 1 mitochondrial, NOGO-interacting mitochondrial protein, RTN4IP1, NIMP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSTVMPAWV IDKYGKNEVL RFTQNMMMPI IHYPNEVIVK VHAASVNPID VNMRSGYGAT ALNMKRDPLH VKIKGEEFPL TLGRDVSGVV MECGLDVKYF KPGDEVWAAV PPWKQGTLSE FVVVSGNEVS HKPKSLTHTQ AASLPYVALT AWSAINKVGG LNDKNCTGKR VLILGASGGV GTFAIQVMKA WDAHVTAVCS QDASELVRKL GADDVIDYKS GSVEEQLKSL KPFDFILDNV GGSTETWAPD FLKKWSGATY VTLVTPFLLN MDRLGIADGM LQTGVTVGSK ALKHFWKGVH YRWAFFMASG PCLDDIAELV DAGKIRPVIE QTFPFSKVPE AFLKVERGHA RGKTVINVV.

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    Rtn4Ip1 Human
  • View Data Sheet

    Name :

    SAR1A Human

    Description:

    GTP-Binding Protein SAR1A Human Recombinant

    GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.

    Product # :

    PRO-709

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    Description

    SAR1A Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 218 amino acids (1- 198 a.a.) and having a molecular mass of 24.5kDa.The SAR1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAR1A solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SAR1A is a member of the small GTPase superfamily. SAR1A is a vital component of COPII vesicle coats involved in export of cargo from the ER (Endoplasmic Reticulum). The GTPase activity of SAR1A serves as a molecular switch to control protein-protein and protein-lipid interactions which dictate vesicle budding from the ER. SAR1A, while GDP-bound interacts with the membrane-bound exchange factor Sec12 and trades its bound GDP for GTP. SAR1A is also involved in the transport from the ER to the Golgi apparatus. SAR1A is required to maintain SEC16A localization at distinct locations on the ER membrane possibly by preventing its dissociation. SAR1A-GTP-dependent compilation of SEC16A on the ER membrane creates a structured scaffold defining endoplasmic reticulum exit sites.

    • Synonyms

      GTP-binding protein SAR1a, COPII-associated small GTPase, SAR1A, SAR1, SARA, SARA1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSFIFEWIYN GFSSVLQFLG LYKKSGKLVF LGLDNAGKTT LLHMLKDDRL GQHVPTLHPT SEELTIAGMT FTTFDLGGHE QARRVWKNYL PAINGIVFLV DCADHSRLVE SKVELNALMT DETISNVPIL ILGNKIDRTD AISEEKLREI FGLYGQTTGK GNVTLKELNA RPMEVFMCSV LKRQGYGEGF RWLSQYID.

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    Sar1A Human
  • View Data Sheet

    Name :

    SAR1B Human

    Description:

    GTP-Binding Protein SAR1B Human Recombinant

    GTP-binding protein SAR1b, GTP-binding protein B, GTBPB, SAR1B, SARA2, SARB, ANDD, CMRD.

    Product # :

    PRO-310

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    Description

    SAR1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-198 a.a) and having a molecular mass of 24.8kDa.SAR1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SAR1B protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SAR1B is a small GTPase that functions as a homodimer. GTP-Binding Protein SAR1B (SAR1b) is involved in transport from the endoplasmic reticulum to the Golgi apparatus and also in the selection of the protein cargo and the assembly of the COPII coat complex. The SAR1B protein is activated by the guanine nucleotide exchange factor PREB. SAR1B gene defects are a cause of chylomicron retention disease (CMRD), also known as Anderson disease (ANDD).

    • Synonyms

      GTP-binding protein SAR1b, GTP-binding protein B, GTBPB, SAR1B, SARA2, SARB, ANDD, CMRD.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSFIFDW IYSGFSSVLQ FLGLYKKTGK LVFLGLDNAG KTTLLHMLKD DRLGQHVPTL HPTSEELTIA GMTFTTFDLG GHVQARRVWK NYLPAINGIV FLVDCADHER LLESKEELDS LMTDETIANV PILILGNKID RPEAISEERL REMFGLYGQT TGKGSISLKE LNARPLEVFM CSVLKRQGYG EGFRWMAQYI D.

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    Sar1B Human
  • View Data Sheet

    Name :

    NNMT Human

    Description:

    Nicotinamide N-Methyltransferase Human Recombinant

    Nicotineamide N-methyltransferase, NNMT.

    Product # :

    ENZ-418

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    Description

    NNMT Human Recombinant fused with a 20 amino acid His-Tag tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 284 amino acids (1-264 a.a.) and having a molecular mass of 31.7 kDa.The NNMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NNMT solution contains 20mM Tris pH 8.0 & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.

    • Synonyms

      Nicotineamide N-methyltransferase, NNMT.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI DIGSGPTIYQLLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ SYSSTMANNEGLFSLVARKL SRPL.

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    Nnmt Human
  • View Data Sheet

    Name :

    NT5C3B Human

    Description:

    5'-Nucleotidase, Cytosolic IIIB Human Recombinant

    NT5C3L, 7-methylguanosine phosphate-specific 5'-nucleotidase, Cytosolic 5'-nucleotidase 3B, Cytosolic 5'-nucleotidase III-like protein, cN-III-like protein, N(7)-methylguanylate 5'-phosphatase.

    Product # :

    ENZ-836

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    Description

    NT5C3B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300 a.a) and having a molecular mass of 36.8kDa.NT5C3B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT5C3B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      7-methylguanosine phosphate-specific 5'-nucleotidase (NT5C3B) includes transferase activity and nucleotide binding. Among NT5C3B’s related super-pathways are adenosine nucleotides degradation II and Pyrimidine metabolism. NT5C3B hydrolyzes 7-methylguanosine monophosphate (m(7)GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m(7)GMP guards cells against undesired retrieval of m(7)GMP and its incorporation into nucleic acids. In addition, NT5C3B has weak activity for CMP.

    • Synonyms

      NT5C3L, 7-methylguanosine phosphate-specific 5'-nucleotidase, Cytosolic 5'-nucleotidase 3B, Cytosolic 5'-nucleotidase III-like protein, cN-III-like protein, N(7)-methylguanylate 5'-phosphatase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAEEVST LMKATVLMRQ PGRVQEIVGA LRKGGGDRLQ VISDFDMTLS RFAYNGKRCP SSYNILDNSK IISEECRKEL TALLHHYYPI EIDPHRTVKE KLPHMVEWWT KAHNLLCQQK IQKFQIAQVV RESNAMLREG YKTFFNTLYH NNIPLFIFSA GIGDILEEII RQMKVFHPNI HIVSNYMDFN EDGFLQGFKG QLIHTYNKNS SACENSGYFQ QLEGKTNVIL LGDSIGDLTM ADGVPGVQNI LKIGFLNDKV EERRERYMDS YDIVLEKDET LDVVNGLLQH ILCQGVQLEM QGP.

    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.

    Nt5C3B Human
  • View Data Sheet

    Name :

    TACSTD2 Human

    Description:

    Tumor-Associated Calcium Signal Transducer 2 Human Recombinant

    EGP-1, EGP1, GA733-1, GA7331, GP50, M1S1, TROP2, Cell surface glycoprotein Trop-2, Membrane component chromosome 1 surface marker 1, Pancreatic carcinoma marker protein GA733-1.

    Product # :

    PRO-157

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    Description

    TACSTD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (31-274a.a.) and having a molecular mass of 29.9kDa. TACSTD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TACSTD2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor-associated calcium signal transducer 2 (TACSTD2), is a member of to the EPCAM family. TACSTD2 is an intronless gene which encodes a carcinoma-associated antigen. TACSTD2 may act as a growth factor receptor and as a cell surface receptor that transduces calcium signals. Mutations of TACSTD2 have been associated with gelatinous drop-like corneal dystrophy.

    • Synonyms

      EGP-1, EGP1, GA733-1, GA7331, GP50, M1S1, TROP2, Cell surface glycoprotein Trop-2, Membrane component chromosome 1 surface marker 1, Pancreatic carcinoma marker protein GA733-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQDNCTCP TNKMTVCSPD GPGGRCQCRA LGSGMAVDCS TLTSKCLLLK ARMSAPKNAR TLVRPSEHAL VDNDGLYDPD CDPEGRFKAR QCNQTSVCWC VNSVGVRRTD KGDLSLRCDE LVRTHHILID LRHRPTAGAF NHSDLDAELR RLFRERYRLH PKFVAAVHYE QPTIQIELRQ NTSQKAAGDV DIGDAAYYFE RDIKGESLFQ GRGGLDLRVR GEPLQVERTL IYYLDEIPPK FSMKRLT.

    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.

    Tacstd2 Human
  • View Data Sheet

    Name :

    Globular Adiponectin Human, His

    Description:

    Adiponectin Globular Recombinant, His Tag

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-277

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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

    • 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.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • 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.

    • Solubility

      Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.

    • Amino Acid Sequence

      MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

    • 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.

    Gacrp30 Human His
  • View Data Sheet

    Name :

    LZTFL1 Human

    Description:

    Leucine Zipper Transcription Factor-Like 1 Human Recombinant

    Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.

    Product # :

    PRO-2157

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    Description

    LZTFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a) and having a molecular mass of 37.0kDa. LZTFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LZTFL1 protein solution (1mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine Zipper Transcription Factor-Like 1, also known as LZTFL1 is a ubiquitously expressed protein which localizes to the cytoplasm. LZTFL1 interacts with Bardet-Biedl Syndrome proteins (BBS) and during its interaction with BBS protein complexes, regulates protein trafficking to the ciliary membrane. Nonsense mutations in LZTFL1 cause a form of Bardet-Biedl Syndrome; a ciliopathy characterized partly by polydactyly, obesity, cognitive impairment, hypogonadism, and kidney failure. LZTFL1 also acts as a tumor suppressor; possibly by interacting with E-cadherin as well as the actin cytoskeleton and in this manner regulating the transition of epithelial cells to mesenchymal cells.

    • Synonyms

      Leucine Zipper Transcription Factor-Like 1, BBS17, Leucine Zipper Transcription Factor-Like Protein 1, Leucine zipper transcription factor-like protein 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAELGLN EHHQNEVINY MRFARSKRGL RLKTVDSCFQ DLKESRLVED TFTIDEVSEV LNGLQAVVHS EVESELINTA YTNVLLLRQL FAQAEKWYLK LQTDISELEN RELLEQVAEF EKAEITSSNK KPILDVTKPK LAPLNEGGTA ELLNKEILRL QEENEKLKSR LKTIEIQATN ALDEKSKLEK ALQDLQLDQG NQKDFIKAQD LSNLENTVAA LKSEFQKTLN DKTENQKSLE ENLATAKHDL LRVQEQLHMA EKELEKKFQQ TAAYRNMKEI LTKKNDQIKD LRKRLAQYEP ED.

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    Lztfl1 Human
  • View Data Sheet

    Name :

    CLTA Human

    Description:

    Clathrin, Light Chain A Human Recombinant

    Clathrin light chain A, Lca, CLTA.

    Product # :

    PRO-1144

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    Description

    CLTA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-218 a.a) and having a molecular mass of 26.2kDa (Molecular weight on SDS-PAGE will appear higher).CLTA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLTA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Clathrin, light chain A (CLTA) is a member of the clathrin family. Clathrin, which is a large, soluble protein, is comprised of heavy and light chains. CLTA is one of 2 clathrin light chain proteins which are supposed to function as regulatory elements. CLTA is a key cytosolic coat protein in pits and vesicles originating from the plasma membrane and the trans-Golgi network. In receptor-mediated endocytosis, receptor proteins are encapsulated by Clathrin-coated vesicles.

    • Synonyms

      Clathrin light chain A, Lca, CLTA.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAELDP FGAPAGAPGG PALGNGVAGA GEEDPAAAFL AQQESEIAGI ENDEAFAILD GGAPGPQPHG EPPGGPDAVD GVMNGEYYQE SNGPTDSYAA ISQVDRLQSE PESIRKWREE QMERLEALDA NSRKQEAEWK EKAIKELEEW YARQDEQLQK
      TKANNRAAEE AFVNDIDESS PGTEWERVAR LCDFNPKSSK QAKDVSRMRS VLISLKQAPL VH.

    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.

    Clta Human
  • View Data Sheet

    Name :

    TNFA Bovine

    Description:

    Tumor Necrosis Factor-alpha Bovine Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-1104

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    Description

    TNFA Bovine produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (78-234 a.a.) and having a molecular mass of 17.5kDa. TNFA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TNFA (1mg/ml) contains Phosphate buffer saline(pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 Is < 15 ng/ml and is measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.

    More Info

    • Introduction

      Tumor necrosis factor is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is involved in systemic inflammationand secreted mainly by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MLRSSSQASS NKPVAHVVAD INSPGQLRWW DSYANALMAN GVKLEDNQLV VPADGLYLIY SQVLFRGQGC PSTPLFLTHT ISRIAVSYQT KVNILSAIKS PCHRETPEWA EAKPWYEPIY QGGVFQLEKG DRLSAEINLP DYLDYAESGQ VYFGIIAL.

    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.

    Tnfa Bovine
  • View Data Sheet

    Name :

    CD3 FITC Antibody

    Description:

    CD3, Mouse Anti-Human FITC

    Product # :

    ANT-137

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    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

    More Info

    • Introduction

      CD3 has four peptide chains (gamma, delta, epsilon and zeta) that form CD3. Defects in CD3 are associated with T cell immunodeficiency CD3 complex mediates signal transduction.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified human PBL T cells.

    • Ig Subclass

      Mouse IgG2a.

    • Clone

      hCD3.

    • Applications

      Blocking, staining and activating antibody. For staining, use 10 µl/1,000,000 cells. Titer for blocking and activating T cells should be determined by the investigator.

    • Available Conjugates

      This antibody is also available conjugated to biotin.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4oC. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • Purification Method

      Ion exchange column.

    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.

    Cd3 Fitc Antibody
  • View Data Sheet

    Name :

    PTH (1-84) N15 Human

    Description:

    Parathyroid Hormone (1-84) N15 Labeled Human Recombinant

    Parathyrin, PTH, Parathormone.

    Product # :

    HOR-002

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    Description

    PTH (1-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 84 amino acids and having a molecular mass of 9550 Dalton labeled by the stable isotope N15.The PTH (1-84) N15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTH (1-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 9,000 Units/mg.

    More Info

    • Introduction

      Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
      In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
      In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
      Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures.

    • Synonyms

      Parathyrin, PTH, Parathormone.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Parathyrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Parathormone in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ.

    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.

    Pth 1 84 N15 Human
  • View Data Sheet

    Name :

    LHRH Human

    Description:

    Luteinizing Hormone Releasing Hormone Human

    Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.

    Product # :

    HOR-261

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    Description

    Lutenizing Hormone Releasing Hormone Human Synthetic is a single, non-glycosylated, polypeptide chain containing 10 amino acids and having a molecular mass of 1182.2 Dalton. The molecular formula is C55H75N17O13.C2H4O2. The CAS Number is 71447-49-9.

    Formulation

    The LHRH was lyophilized from a concentrated (1 mg/ml) solution with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Gonadotropin-releasing hormone 1 (GNRH1), also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
      At the pituitary, GNRH1 stimulates the synthesis and secretion of the gonadotropins follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
      There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
      GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male.

    • Synonyms

      Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LHRH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LNRH should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized LHRH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. The LHRH is also soluble in a 1% glacial acetic acid.

    • Amino Acid Sequence

      Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.

    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.

    Lhrh Human
  • View Data Sheet

    Name :

    CSDC2 Human

    Description:

    Cold Shock Domain Containing C2 Human Recombinant

    Cold shock domain-containing protein C2, RNA-binding protein PIPPin, PIPPIN, DJ347H13.2.

    Product # :

    PRO-1439

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    Description

    CSDC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 19.2kDa. CSDC2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The CSDC2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cold shock domain-containing protein C2 (CSDC2) is RNA-binding factor that binds specifically to the very 3'-UTR ends of both histone H1 and H3. 3 mRNAs encompass the polyadenylation signal. The CSDPs (cold shock domain containing proteins) are one group of the evolutionarily conserved nucleic acid-binding proteins extensively distributed in bacteria, plants, animals, and involved in a variety of cellular processes, including adaptation to low temperature, cellular growth, nutrient stress and stationary phase. CSDC2 has a central role in the negative regulation of histone variant synthesis in the developing brain.

    • Synonyms

      Cold shock domain-containing protein C2, RNA-binding protein PIPPin, PIPPIN, DJ347H13.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMTSESTS PPVVPPLHSP KSPVWPTFPF HREGSRVWER GGVPPRDLPS PLPTKRTRTY SATARASAGP VFKGVCKQFS RSQGHGFITP ENGSEDIFVH VSDIEGEYVP VEGDEVTYKM CPIPPKNQKF QAVEVVLTQL APHTPHETWS GQVVGS.

    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.

    Csdc2 Human
  • View Data Sheet

    Name :

    AKR1C4 Human, His

    Description:

    Aldo-Keto Reductase Family 1 Member C4 Human Recombinant, His Tag

    Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.

    Product # :

    ENZ-145

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    Description

    AKR1C4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323) and having a molecular mass of 39.2 kDa.The AKR1C4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AKR1C4 protein 1mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 700 pmol/min/ug, and is defined as the amount of enzyme that catalyze the oxidation of 1.0 pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25°C.

    More Info

    • Introduction

      AKR1C4 is a member of the aldo/keto reductase superfamily that has over 40 known enzymes and proteins. AKR1C4 enables the conversion of aldehydes and ketones to their corresponding alcohols by using NADH and/or NADPH as cofactors. AKR1C4 takes part in the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in liver.

    • Synonyms

      Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.

    • Physical Appearance

      AKR1C4 is supplied as a 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID SAYLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE SSLKKLQLDY VDLYLLHFPM ALKPGETPLP KDENGKVIFD TVDLSATWEV MEKCKDAGLA
      KSIGVSNFNC RQLEMILNKP GLKYKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN RNYRYVVMDF LMDHPDYPFS DEY.

    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.

    Akr1C4 Human
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