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Search results

1000 results found for “Tropomyosin”

Name

Description

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  • View Data Sheet

    Name :

    CXCL3 Mouse, His

    Description:

    GRO-Gamma Mouse Recombinant (CXCL3), His Tag

    C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    Product # :

    CHM-283

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    Description

    GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

    • Synonyms

      C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    • 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 MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

    • Background

      What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.

      What is the source or expression system of CXCL3 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
      The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

      What applications can CXCL3 MOUSE, HIS Protein be used in?
      CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
      The endotoxin level is minimal, CXCL3 MOUSE, HIS Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gro G Mouse His
  • View Data Sheet

    Name :

    MAP1LC3B Human

    Description:

    Microtubule-Associated Protein 1 Light Chain 3 Beta Human Recombinant

    Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    Product # :

    PRO-076

    Price :

    Quantity :

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    • description
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    Description

    MAP1LC3B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-120a.a.) and having a molecular mass of 16.2kDa.MAP1LC3B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAP1LC3B protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.

    • Synonyms

      Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETFG

    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.

    Map1Lc3B Human
  • View Data Sheet

    Name :

    T.pallidum p15 (Partial), His

    Description:

    Treponema pallidum p15 (Partial) Recombinant, His Tag

    Product # :

    TRP-247

    Price :

    Quantity :

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    • More Info
    • sds-page

    Description

    The E.Coli derived recombinant 6xHis tag fusion protein is a multimer having a molecular mass of 15kDa and contains the Trp. Pallidum p15 immunodominant regions and six histidines fused at the C- terminus.

    Source

    Escherichia Coli.

    Formulation

    70mM Tris-HCl pH 8.0, 50mM NaCl, 50% Glycerol, 1.5 M Urea.

    Purity

    Treponema Pallidum protein is >95% pure as determined by SDS- PAGE.

    sds-page

    T.pallidum p15 (Partial), His sds-page - Product image 1

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Stability

      Treponema Pallidum protein should be stored at 2-8°C. Do NOT freeze.

    • Specificity

      Immunoreactive with sera of Trp. Pallidum infected individuals.

    • Purification Method

      Treponema Pallidum protein was purified by proprietary chromatographic technique.

    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.

    Tpallidum P15 His
  • View Data Sheet

    Name :

    MYBPC3 Human

    Description:

    Myosin Binding Protein C, Cardiac Human Recombinant

    Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.

    Product # :

    PRO-2292

    Price :

    Quantity :

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    • description
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    Description

    MYBPC3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Phe271) containing 281 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 29.6kDa.

    Source

    Escherichia Coli.

    Formulation

    MYBPC3 was filtered (0.4µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin Binding Protein C, Cardiac (MYBPC3) is the cardiac isoform of myosin-binding protein C expressed exclusively in heart muscle. Myosin-binding protein C is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. Regulatory phosphorylation of the cardiac isoform in vivo by cAMP-dependent protein kinase upon adrenergic stimulation may be associated with modulation of cardiac contraction. MYBPC3 gene mutations are one of the causes of familial hypertrophic cardiomyopathy. In vitro MYBPC3 binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. MYBPC3 may modulate muscle contraction or it may have a more structural role.

    • Synonyms

      Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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 0.5mg/ml and let the lyophilized pellet dissolve completely. MYBPC3 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASMPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS ASNKYGLATE GTRHTLTVRE VGPADQGSYA VIAGSSKVKF DLKVIEAEKA EPMLAPAPAP AEATGAPGEA PAPAAELGES APSPKGSSSA ALNGPTPGAP DDPIGLFVMR PQDGEVTVGG SITFSARVAG ASLLKPPVVK WFKGKWVDLS SKVGQHLQLH DSYDRASKVY LFELHITDAQ PAFTGSYRCE VSTKDKFDCS NFNLTVHEAM GTGDLDLLSA F.

    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.

    Mybpc3 Human
  • View Data Sheet

    Name :

    MYLPF Human

    Description:

    Myosin Light chain, Phosphorylatable, Fast Skeletal Muscle Human Recombinant

    Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    Product # :

    PRO-243

    Price :

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    • description
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    • More Info

    Description

    MYLPF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a) and having a molecular mass of 21.2kDa.MYLPF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYLPF protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin regulatory light chains, including MRCL3, MYLPF and MYL9, regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the actin-activated myosin ATPase activity, thus regulating the contractile activity. MYLPF is vital for fast and slow skeletal muscle development.

    • Synonyms

      Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    • 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 MAPKRAKRRT VEGGSSSVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKKFL EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE.

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    Mylpf Human
  • View Data Sheet

    Name :

    Omentin Human, His

    Description:

    Omentin Human Recombinant, His Tag

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-551

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    Description

    Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.

    Purity

    Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Intelectin His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin His Tag in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.

    • Applications

      Elisa
      Western blot.

    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.

    Omentin Human His
  • View Data Sheet

    Name :

    EYA2 Human

    Description:

    Eyes Absent Homolog 2 Human Recombinant

    Eyes absent homolog 2 (Drosophila), EAB1, EC 3.1.3.48.

    Product # :

    PRO-1071

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    Description

    EYA2 Human Recombinant produced in E. coli is a single polypeptide chain containing 295 amino acids (244-514) and having a molecular mass of 33.2kDa.EYA2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EYA2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      EYA2 belongs to tyrosine phosphatase family which specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). EYA2 promotes effective DNA mending by dephosphorylating H2AX, promoting the enlistment of DNA repair complexes having MDC1. EYA2 role as histone phosphatase can explain its part in transcription regulation during organogenesis.

    • Synonyms

      Eyes absent homolog 2 (Drosophila), EAB1, EC 3.1.3.48.

    • 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 MGSMERVFVW DLDETIIIFH SLLTGTFASR YGKDTTTSVR IGLMMEEMIF NLADTHLFFN DLEDCDQIHV DDVSSDDNGQ DLSTYNFSAD GFHSSAPAAN LCLGSGVHGG VDWMRKLAFR YRRVKEMYNT YKNNVGGLIG TPKRETWLQL RAELEALTDL WLTHSLKALN LINSRPNCVN VLVTTTQLIP ALAKVLLYGL GSVFPIENIY SATKTGKESC FERIMQRFGR KAVYVVIGDG VEEEQGAKKH NMPFWRISCH ADLEALRHAL ELEYL.

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    Eya2 Human
  • View Data Sheet

    Name :

    THAP3 Human

    Description:

    THAP Domain Containing, Apoptosis Associated Protein 3 Human Recombinant

    THAP Domain Containing Apoptosis Associated Protein 3, THAP Domain-Containing Protein 3.

    Product # :

    PRO-1630

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    Description

    THAP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (1-239) and having a molecular mass of 29.4kDa.THAP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The THAP3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      THAP3 is an element of a THAP1/THAP3-HCFC1-OGT complex which is essential for the regulation of the transcriptional activity of RRM1. THAP3 is vastly produced in placenta, skeletal muscle and heart.

    • Synonyms

      THAP Domain Containing Apoptosis Associated Protein 3, THAP Domain-Containing Protein 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

      MGSSHHHHHH SSGLVPRGSH MGSMPKSCAA RQCCNRYSSR RKQLTFHRFP FSRPELLKEW VLNIGRGNFK PKQHTVICSE HFRPECFSAF GNRKNLKHNA VPTVFAFQDP TQQVRENTDP ASERGNASSS QKEKVLPEAG AGEDSPGRNM DTALEELQLP PNAEGHVKQV SPRRPQATEA VGRPTGPAGL RRTPNKQPSD HSYALLDLDS LKKKLFLTLK ENEKLRKRLQ AQRLVMRRMS SRLRACKGHQ GLQARLGPEQ QS

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    Thap3 Human
  • View Data Sheet

    Name :

    VAMP4 Human

    Description:

    Vesicle-associated membrane protein 4 Human Recombinant

    Vesicle-associated membrane protein 4, VAMP-4, VAMP4, VAMP24.

    Product # :

    PRO-714

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    Description

    VAMP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids (1-115 a.a.) and having a molecular mass of 14.5kDa.VAMP4 is fused to an 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VAMP4 protein solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      VAMP4 belongs to the synaptobrevin family who are involved in docking and/or fusion of vesicles with cell membrane. VAMP4 is enriched in the trans-Golgi network and may be a factor in the trans-Golgi network-to-endosome transport. VAMP4 is involved in the pathway which functions to eliminate an inhibitor (most likely synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. Synaptobrevins, syntaxins, and SNAP25 are the chief components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane.

    • Synonyms

      Vesicle-associated membrane protein 4, VAMP-4, VAMP4, VAMP24.

    • 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

      MPPKFKRHLN DDDVTGSVKS ERRNLLEDDS DEEEDFFLRG PSGPRFGPRN DKIKHVQNQV DEVIDVMQEN ITKVIERGER LDELQDKSES LSDNATAFSN RSKQLRRQMW WRGCKLEHHH HHH.

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    Vamp4 Human
  • View Data Sheet

    Name :

    BMP3 Human

    Description:

    Bone Morphogenetic protein-3 Human Recombinant

    Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    Product # :

    CYT-937

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    Description

    BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

    Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

    More Info

    • Introduction

      Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.

    • Synonyms

      Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

    • Background

      Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration

      Abstract:

      Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.

      Introduction:

      Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.

      Production of BMP-3 Human Recombinant:

      Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.

      Potential Therapeutic Applications:

      BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.

      Conclusion:

      BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.

      What is the molecular weight/Mw of BMP3 Protein?
      BMP3 Protein has a total Mw of 24.8kDa.

      What is the source or expression system of BMP3 Protein?
      Escherichia Coli.

      What is the Purity of BMP3 Protein?
      BMP3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP3 Protein?
      The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

      What is the amino acid sequence of BMP3 Protein?
      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

      What applications can BMP3 Protein be used in?
      BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP3 Protein?
      The endotoxin level is minimal, BMP3 Protein was purified using conventional chromatography techniques.

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    Bmp3 Human
  • View Data Sheet

    Name :

    CRYM Human

    Description:

    Crystallin, Mu Human Recombinant

    Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    Product # :

    PRO-2291

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    Description

    CRYM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 334 amino acids (1-314) and having a molecular mass of 35.9kDa. CRYM is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CYRM 1mg/ml solution containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crystallin, Mu (CRYM) is a taxon-specific crystallin protein which binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. CRYM doesn’t perform a structural role in lens tissue; instead CRYM binds thyroid hormone for possible regulatory or developmental roles. CRYM gene mutations are linked with autosomal dominant non-syndromic deafness. CRYM specifically catalyzes the reduction of imine bonds in brain substrates which may include cystathionine ketamine and lanthionine ketamine.

    • Synonyms

      Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CRYM although stable at 4°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK

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    Crym Human
  • View Data Sheet

    Name :

    Actin Rabbit

    Description:

    Actin Rabbit

    Product # :

    PRO-517

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    Description

    Ultra pure Actin consists in the alpha-skeletal muscle isoform and is purified from rabbit striated muscle.The purification method used (according to Spudich & Watts) results in a highly purified protein having a Molecular mass of 43,000 dalton.

    Source

    Rabbit Muscle.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM Tris/HCl buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% (w/v) SDS.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Actin is a muscle protein localized in the I band of the myofibrils; acting along with myosin, it is responsible for contraction and relaxation of muscle. Each actin protomer binds one molecule of ATP and has one high affinity site for either calcium or magnesium ions, as well as several low affinity sites. Actin exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP. It occurs in globular (G-actin) and fibrous (F-actin) forms. Actin is found in all eukaryotic cells (except for nematode sperm). Actin is one of the most highly-conserved proteins, differing by no more than 20% in species as diverse as algae and humans. Its other functions include cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the Lyophilized Actin between 2-8°C, do not freeze. Upon reconstitution Actin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Actin in sterile 18MΩ-cm H2O not less than 1mg/ml, which can then be further diluted to other aqueous solutions.

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    Actin
  • View Data Sheet

    Name :

    NPM1 Human

    Description:

    Nucleophosmin Human Recombinant

    Nucleophosmin, NPM, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin, NPM1, NPM, B23.

    Product # :

    PRO-1120

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    Description

    NPM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-294 a.a) and having a molecular mass of 34.7kDa.NPM1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NPM1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nucleophosmin (NPM1) is a phosphoprotein which shuffles between the nucleus and the cytoplasm. NPM1 is assumed to be involved in a number of processes including regulation of the ARF/p53 pathway. Several genes fusion partners have been described, particularly the anaplastic lymphoma kinase gene on chromosome 2. NPM1 gene mutations are linked with acute myeloid leukemia.

    • Synonyms

      Nucleophosmin, NPM, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin, NPM1, NPM, B23.

    • 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 MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA
      DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL.

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    Npm1 Human
  • View Data Sheet

    Name :

    Streptavidin (37-159), His

    Description:

    Streptavidin (37-159 a.a) Recombinant, His Tag

    Product # :

    PRO-1495

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    Description

    Streptavidin Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (37-159) and having a molecular mass of 15.6kDa. Streptavidin is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The Streptavidin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • 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 MGSHMAEAGI TGTWYNQLGS TFIVTAGADG ALTGTYESAV GNAESRYVLT GRYDSAPATD GSGTALGWTV AWKNNYRNAH SATTWSGQYV GGAEARINTQ WLLTSGTTEA NAWKSTLVGH DTFTKVKP.

    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.

    Streptavidin 37 159 His
  • View Data Sheet

    Name :

    TRAPPC3 Human

    Description:

    Trafficking Protein Particle Complex 3 Human Recombinant

    Trafficking protein particle complex subunit 3, BET3, BET3 homolog, 1110058K12Rik.

    Product # :

    PRO-1056

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    Description

    TRAPPC3 Human Recombinant produced in E. coli is a single polypeptide chain containing 200 amino acids (1-180) and having a molecular mass of 22.4kDa.TRAPPC3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TRAPPC3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TRAPPC3 is a part of the TRAPP complex that takes part in connection of transport vesicles to the cis-Golgi membrane. Additionally, TRAPPC3 is involved in vesicular transport from endoplasmic reticulum to Golgi.

    • Synonyms

      Trafficking protein particle complex subunit 3, BET3, BET3 homolog, 1110058K12Rik.

    • 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 MSRQANRGTE SKKMSSELFT LTYGALVTQL CKDYENDEDV NKQLDKMGFN IGVRLIEDFL ARSNVGRCHD FRETADVIAK VAFKMYLGIT PSITNWSPAG DEFSLILENN PLVDFVELPD NHSSLIYSNL LCGVLRGALE MVQMAVEAKF VQDTLKGDGV TEIRMRFIRR IEDNLPAGEE

    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.

    Trappc3 Human
  • View Data Sheet

    Name :

    TRIAP1 Human

    Description:

    TP53 Regulated Inhibitor Of Apoptosis 1 Human Recombinant

    TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.

    Product # :

    PRO-1771

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    Description

    TRIAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 99 amino acids (1-76 a.a) and having a molecular mass of 11.2kDa.TRIAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TRIAP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TRIAP1 has a p53-binding site in its second exon. TRIAP1 expression is reduced by small interfering RNA enhanced apoptosis, while overexpression of TRIAP1 protects cells from apoptosis triggered by DNA damage. TRIAP1 is highly induced when cells have low levels of genotoxic stresses, but not when DNA damage is severe. TRIAP1 is able to control apoptotic pathways by interacting with Hsp70 which inhibits activity of apoptosis protease activating factor-1.

    • Synonyms

      TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMNSVGEA CTDMKREYDQ CFNRWFAEKF LKGDSSGDPC TDLFKRYQQC VQKAIKEKEI PIEGLEFMGH GKEKPENSS

    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.

    Triap1 Human
  • View Data Sheet

    Name :

    TXNDC17 Human

    Description:

    Thioredoxin Domain Containing 17 Human Recombinant

    Thioredoxin domain containing 17, Thioredoxin-like protein 5, Protein 42-9-9, thioredoxin (Trx)-related protein 14 kDa, TRP14, TXNL5, MGC14353.

    Product # :

    PRO-1055

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    Description

    TXNDC17 Human Recombinant produced in E. coli is a single polypeptide chain containing 147 amino acids (1-123) and having a molecular mass of 16.5kDa.TXNDC17 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TXNDC17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM Nacl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TXNDC17 is a disulfide reductase that takes part in several redox reactions using the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. TXNDC17 has peroxidase activity and assists to eliminate cellular hydrogen peroxide.

    • Synonyms

      Thioredoxin domain containing 17, Thioredoxin-like protein 5, Protein 42-9-9, thioredoxin (Trx)-related protein 14 kDa, TRP14, TXNL5, MGC14353.

    • 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 MGSHMARYEE VSVSGFEEFH RAVEQHNGKT IFAYFTGSKD AGGKSWCPDC VQAEPVVREG LKHISEGCVF IYCQVGEKPY WKDPNNDFRK NLKVTAVPTL LKYGTPQKLV ESECLQANLV EMLFSED

    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.

    Txndc17 Human
  • View Data Sheet

    Name :

    GNLY Human

    Description:

    Granulysin Human Recombinant

    LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    Product # :

    PRO-852

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    Description

    GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Granulysin protein was lyophilized from a concentrated (1mg/ml) solution containing no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

    • Synonyms

      LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulysin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulysin 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 Granulysin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
      LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
      TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
      DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
      TGPLGSHHHHHH.

    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.

    Gnly Human
  • View Data Sheet

    Name :

    CXCL2 Mouse

    Description:

    GRO-Beta Mouse Recombinant (CXCL2)

    Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    Product # :

    CHM-338

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    Description

    GRO-Beta Mouse Recombinant also caled mouse MIP-2 produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7849 Dalton. The CXCL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

    Purity

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

    Biological Activity

    The Biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 105-106units/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

    • Synonyms

      Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Mouse in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVVASELRCQ CLKTLPRVDF KNIQSLSVTP PGPHCAQTEV IATLKGGQKV CLDPEAPLVQ KIIQKILNKG KAN.

    • Background

      What is the molecular weight/Mw of CXCL2 MOUSE Protein?
      CXCL2 MOUSE Protein has a total Mw of 7.84kDa.

      What is the source or expression system of CXCL2 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL2 MOUSE Protein?
      CXCL2 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL2 MOUSE Protein?
      The Biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 105-106units/mg.

      What is the amino acid sequence of CXCL2 MOUSE Protein?
      AVVASELRCQ CLKTLPRVDF KNIQSLSVTP PGPHCAQTEV IATLKGGQKV CLDPEAPLVQ KIIQKILNKG KAN.

      What applications can CXCL2 MOUSE Protein be used in?
      CXCL2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL2 MOUSE Protein?
      The endotoxin level is minimal, CXCL2 MOUSE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.015 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 GRO-b 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.

    Gro Beta Mouse
  • View Data Sheet

    Name :

    CXCL1 Mouse, His

    Description:

    GRO/KC (CXCL1) Mouse Recombinant, His Tag

    Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

    Product # :

    CHM-002

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    • SDS-PAGE

    Description

    GRO1/KC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (25-96 a.a.) and having a molecular mass of 10.5kDa.GRO1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GRO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CXCL1 Mouse, His-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.

    • Synonyms

      Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 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 MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.

    • Background

      What is the molecular weight/Mw of CXCL1 MOUSE, HIS Protein?
      CXCL1 MOUSE, HIS Protein has a total Mw of 10.5kDa.

      What is the source or expression system of CXCL1 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL1 MOUSE, HIS Protein?
      CXCL1 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL1 MOUSE, HIS Protein?
      The biological functionality of CXCL1 MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL1 MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.

      What applications can CXCL1 MOUSE, HIS Protein be used in?
      CXCL1 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL1 MOUSE, HIS Protein?
      The endotoxin level is minimal, CXCL1 MOUSE, HIS Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gro A Mouse His
  • View Data Sheet

    Name :

    PTHrP N15 Human

    Description:

    Parathyroid Hormone Related Protein N15 Labeled Human Recombinant

    Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.

    Product # :

    HOR-005

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    Description

    PTHrP N15 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids, having an MW of 10033 Da labeled by the stable isotope N15.The PTHrP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PthRp N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS,
    pH 7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      PTHrP is a powerful and discriminating agonist of PTH2R which takes part in adenyl cyclase activation and intracellular calcium levels elevation. PTHrP encourages protein kinase C beta activation, recruitment of beta-arrestin and PTH2R internalization. Additionally, PTHrP inhibits cell proliferation through its contribution to PTH2R activation, activates nociceptors and nociceptive circuits and acts as a neuropeptide in spermatogenesis.

    • Synonyms

      Parathyroid Hormone 2, PTH2, TIPF39, Tuberoinfundibular 39 Residue Protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PTHrP N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTHrP N15 should be stored at 4C between 2-7 days and for future use below -18C.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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      AVSEHQLLHD KGKSIQDLRR RFFLHHLIAE IHTAEIRATS EVSPNSKPSP NTKNHPVRFG SDDEGRYLTQ ETNKVETYKE QPLKTP.

    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.

    Pthrp N15 Human
  • View Data Sheet

    Name :

    VAMP7 Human

    Description:

    Vesicle-Associated Membrane Protein 7 Human Recombinant

    Vesicle-associated membrane protein 7, Tetanus-insensitive VAMP, tetanus neurotoxin-insensitive VAMP, Synaptobrevin-like protein 1, TI-VAMP, VAMP-7, TIVAMP, SYBL1.

    Product # :

    PRO-1194

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    Description

    VAMP7 Human Recombinant produced in E. coli is a single polypeptide chain containing 211 amino acids (1-188) and having a molecular mass of 23.0 kDa.VAMP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The VAMP7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Vesicle-Associated Membrane Protein 7 (VAMP7) is a member of the synaptobrevin family. VAMP7 is a transmembrane protein, which is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family. VAMP7 is involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. VAMP7 localizes to late endosomes and lysosomes and is involved in the fusion of transport vesicles to their target membranes. VAMP7 is essential for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. It is also necessary for calcium regulated lysosomal exocytosis. In addition, VAMP7 is involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Furthermore, VAMP7 is needed for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells.

    • Synonyms

      Vesicle-associated membrane protein 7, Tetanus-insensitive VAMP, tetanus neurotoxin-insensitive VAMP, Synaptobrevin-like protein 1, TI-VAMP, VAMP-7, TIVAMP, SYBL1.

    • 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 MGSMAILFAV VARGTTILAK HAWCGGNFLE VTEQILAKIP SENNKLTYSH GNYLFHYICQ DRIVYLCITD DDFERSRAFN FLNEIKKRFQ TTYGSRAQTA LPYAMNSEFS SVLAAQLKHH SENKGLDKVM ETQAQVDELK GIMVRNIDLV AQRGERLELL IDKTENLVDS SVTFKTTSRN LARAMCMKNL K

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    Vamp7 Human
  • View Data Sheet

    Name :

    TROVE2 Bovine, Biotin

    Description:

    TROVE Domain Family Member 2 Human Recombinant, Biotinlyated

    60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    Product # :

    PRO-2561

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    Description

    TROVE2 is a biotinlyated natural protein having a molecular mass of 58kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.

    Source

    Bovine tissues.

    Formulation

    TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl and 20% glycerol.

    Purity

    Greater than 83.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

    • Synonyms

      60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    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.

    Ro60 Bovine
  • View Data Sheet

    Name :

    T.pallidum p17 (Partial)

    Description:

    Treponema pallidum p17 (Partial) Recombinant

    Product # :

    TRP-248

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    • More Info

    Description

    The E.Coli derived recombinant protein is fused at N-terminus with 6xHis tag and contains the Trp. Pallidum p17 immunodominant regions.

    Source

    Escherichia Coli.

    Formulation

    70mM Tris-HCl pH8.0, 50mM NaCl, 50% Glycerol, 1.5M Urea.

    Purity

    Treponema Pallidum protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

    • Stability

      Treponema Pallidum protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of Trp. Pallidum with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of Trp. Pallidum infected individuals.

    • Purification Method

      Treponema Pallidum protein was purified by proprietary chromatographic technique.

    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.

    Tpallidum P17 Partial
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