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Search results

1000 results found for “Osteopontin”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    TSPAN7 Human

    Description:

    Tetraspanin 7 Human Recombinant

    Tspan-7, Cell surface glycoprotein A15, Membrane component chromosome X surface marker 1, T-cell acute lymphoblastic leukemia-associated antigen 1, TALLA-1, Transmembrane 4 superfamily member 2, CD231, A15, DXS1692E, MXS1, TM4SF2.

    Product # :

    PRO-2414

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    Description

    TSPAN7 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 110 amino acids (113-213a.a.) and having a molecular mass of 12.6kDa. (Molecular size on SDS-PAGE under reducing conditions 13.5-18kDa). TSPAN7 is expressed with a 6amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    TSPAN7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tetraspanin 7, also known as TSPAN7, is part of the transmembrane 4 superfamily, which is also familiar as the tetraspanin family. Most of these proteins mediate signal transduction events which play a role in the regulation of cell development, activation, growth as well as motility. Furthermore, TSPAN7 is associated with X-linked mental retardation in addition to neuropsychiatric diseases such as Huntington's chorea, fragile X syndrome and myotonic dystrophy. Lately, TSPAN7 has been acknowledged as a key immune system target in type 1 diabetes.

    • Synonyms

      Tspan-7, Cell surface glycoprotein A15, Membrane component chromosome X surface marker 1, T-cell acute lymphoblastic leukemia-associated antigen 1, TALLA-1, Transmembrane 4 superfamily member 2, CD231, A15, DXS1692E, MXS1, TM4SF2.

    • 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

      ADPRHEIKDT FLRTYTDAMQ TYNGNDERSR AVDHVQRSLS CCGVQNYTNW STSPYFLEHG IPPSCCMNET DCNPQDLHNL TVAATKVNQK GCYDLVTSFM ETNMHHHHHH.

    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.

    Tspan7 Human
  • View Data Sheet

    Name :

    Procalcitonin Rat

    Description:

    Procalcitonin Rat Recombinant

    Calcitonin, Calca, Calc.

    Product # :

    HOR-019

    Price :

    Quantity :

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    Description

    Procalcitonin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val26-Asn136) containing 121 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 13.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Procalcitonin was filtered (0.4µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 8.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin, Calca, Calc.

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

    • Amino Acid Sequence

      MKHHHHHHASVPLRSTLESS PGMATLSEEE ARLLAALVQN YMQMKVRELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVGA PGKKRDMAKD LETNHHPYFG N.

    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.

    Procalcitonin Rat
  • View Data Sheet

    Name :

    CFL2 Human

    Description:

    Cofilin-2 Human Recombinant

    Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    Product # :

    PRO-912

    Price :

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    Description

    CFL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-166 a.a.) and having a molecular mass of 20.9kDa.CFL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CFL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CFL2 protein is a member of the actin-binding proteins ADF family which contains 1 ADF-H domain. Cofilin is a broadly distributed intracellular actin-modulating protein which binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Defects in the CFL2 gene are the cause of nemaline myopathy type 7 (NEM7).

    • Synonyms

      Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    • 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 MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL.

    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.

    Cfl2 Human
  • View Data Sheet

    Name :

    RAB32 Human

    Description:

    RAB32, Member RAS Oncogene Family Human Recombinant

    RAB32 member RAS oncogene family, ras-related protein Rab-32.

    Product # :

    PRO-950

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    Description

    RAB32 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (1-225) and having a molecular mass of 27.6 kDa.RAB32 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RAB32 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl, 0.2M EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAB32 is a member of the small GTPase superfamily. RAB32 controls ER calcium management and disturbs the specific enhancement of calnexin on the MAM (mitochondria-associated membrane), however avoids affecting the ER distribution of protein-disulfide isomerase and mitofusin-2. Furthermore, RAB32 regulates the targeting of PKA (cAMP-dependent protein kinase) to mitochondrial and ER membranes and by inactivation or overexpression enhances the phosphorylation of Drp1 and Bad. Using a combination of its functions as a regulator of MAM properties and a PKA-anchoring protein, the activity and expression level of RAB32 define the speed of apoptosis onset.

    • Synonyms

      RAB32 member RAS oncogene family, ras-related protein Rab-32.

    • 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 MGSHMAGGGA GDPGLGAAAA PAPETREHLF KVLVIGELGV GKTSIIKRYV HQLFSQHYRA TIGVDFALKV LNWDSRTLVR LQLWDIAGQE RFGNMTRVYY KEAVGAFVVF DISRSSTFEA VLKWKSDLDS KVHLPNGSPI PAVLLANKCD QNKDSSQSPS QVDQFCKEHG FAGWFETSAK DNINIEEAAR FLVEKILVNH QSFPNEENDV DKIKLDQETL RAENKSQCC

    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.

    Rab32 Human
  • View Data Sheet

    Name :

    RALY Human

    Description:

    RALY Human Recombinant

    RALY Heterogeneous Nuclear Ribonucleoprotein, RNA-Binding Protein (Autoantigenic, HnRNP-Associated With Lethal Yellow), HnRNP Associated With Lethal Yellow Protein Homolog, Heterogeneous Nuclear Ribonucleoprotein C-Like 2, HnRNP Core Protein C-Like 2, Autoantigen P542, HNRPCL2, P542, RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog (Mouse)), RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog), RNA-Binding Protein (Autoantigenic), RNA-Binding Protein Raly, RNA-binding protein Raly.

    Product # :

    PRO-2095

    Price :

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    Description

    RALY Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-306 a.a) and having a molecular mass of 34.9kDa. RALY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RALY belongs to the heterogeneous nuclear ribonucleoprotein (hnRNP) gene family. RALY takes part in pre-mRNA splicing and also in embryonic development. Moreover, alternate splicing results in multiple transcript variants have been found for RALY.

    • Synonyms

      RALY Heterogeneous Nuclear Ribonucleoprotein, RNA-Binding Protein (Autoantigenic, HnRNP-Associated With Lethal Yellow), HnRNP Associated With Lethal Yellow Protein Homolog, Heterogeneous Nuclear Ribonucleoprotein C-Like 2, HnRNP Core Protein C-Like 2, Autoantigen P542, HNRPCL2, P542, RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog (Mouse)), RNA Binding Protein, Autoantigenic (HnRNP-Associated With Lethal Yellow Homolog), RNA-Binding Protein (Autoantigenic), RNA-Binding Protein Raly, RNA-binding protein Raly.

    • 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 MGSMSLKLQA SNVTNKNDPK SINSRVFIGN LNTALVKKSD VETIFSKYGR VAGCSVHKGY AFVQYSNERH ARAAVLGENG RVLAGQTLDI NMAGEPKPDR PKGLKRAASA IYSGYIFDYD YYRDDFYDRL FDYRGRLSPV PVPRAVPVKR PRVTVPLVRR VKTNVPVKLF ARSTAVTTSS AKIKLKSSEL QAIKTELTQI KSNIDALLSR LEQIAAEQKA NPDGKKKGDG GGAGGGGGGG GSGGGGSGGG GGGGSSRPPA PQENTTSEAG LPQGEARTRD DGDEEGLLTH SEEELEHSQD TDADDGALQ.

    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.

    Raly Human
  • View Data Sheet

    Name :

    RANBP1 Human

    Description:

    RAN Binding Protein 1 Human Recombinant

    RAN binding protein 1, HTF9A, ran-specific GTPase-activating protein, RanBP1.

    Product # :

    PRO-1064

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    Description

    RANBP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 225 amino acids (1-201) and having a molecular mass of 25.8kDa (molecular size on SDS-PAGE will appear higher).RANBP1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RANBP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      RANBP1 is a member of a family of proteins which bind Ran GTPase. Ran GTPase is vital for cell cycle control, mRNA processing, nuclear transport, mitotic spindle assembly, and postmitotic nuclear re-assembly and nuclear architecture maintenance. RANBP1 does not stimulate GTPase activity of RAN however RANBP1 does distinctly raise GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). Additionally, RANBP1 operates as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN.

    • Synonyms

      RAN binding protein 1, HTF9A, ran-specific GTPase-activating protein, RanBP1.

    • 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 MGSHMAAAKD THEDHDTSTE NTDESNHDPQ FEPIVSLPEQ EIKTLEEDEE ELFKMRAKLF RFASENDLPE WKERGTGDVK LLKHKEKGAI RLLMRRDKTL KICANHYITP MMELKPNAGS DRAWVWNTHA DFADECPKPE LLAIRFLNAE NAQKFKTKFE ECRKEIEERE KKAGSGKNDH AEKVAEKLEA LSVKEETKED AEEKQ.

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    Ranbp1 Human
  • View Data Sheet

    Name :

    RAP2B Human

    Description:

    RAP2B, Member RAS Oncogene Family Human Recombinant

    RAP2B, member of RAS oncogene family, Ras-related protein Rap-2b, Ras Family Small GTP Binding Protein RAP2B2, Small GTP Binding Protein.

    Product # :

    PRO-1364

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    Description

    RAP2B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-183 a.a) and having a molecular mass of 22.9kDa. RAP2B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RAP2B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ras-related protein Rap-2b (RAP2B) is a part of RAS-related genes family. RAP2B has a threonine residue at aa 61Unlike normal ras proteins which have a nontransforming glutamine residue at that position. The threonine residue makes the intrinsic GTPase activity for Rap2B lower, by this means allows RAP2B to exist in the activated state for a longer period of time than normal ras proteins. RAP2B is a platelet protein which is activated by thrombin and involved in platelet activation. RAP2B may be a candidate oncogene which takes part in carcinogenesis through activation of NF-kappaB pathway.

    • Synonyms

      RAP2B, member of RAS oncogene family, Ras-related protein Rap-2b, Ras Family Small GTP Binding Protein RAP2B2, Small GTP Binding Protein.

    • 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 MGSMREYKVV VLGSGGVGKS ALTVQFVTGS FIEKYDPTIE DFYRKEIEVD SSPSVLEILD TAGTEQFASM RDLYIKNGQG FILVYSLVNQ QSFQDIKPMR DQIIRVKRYE RVPMILVGNK VDLEGEREVS YGEGKALAEE WSCPFMETSA KNKASVDELF AEIVRQMNYA AQPNGDEGCC SACVIL.

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    Rap2B Human
  • View Data Sheet

    Name :

    RBM3 Human

    Description:

    RNA Binding Motif Protein 3 Human Recombinant

    IS1-RNPL, RNPL, RNA-binding motif protein 3, Putative RNA-Binding Protein 3, RNA Binding Motif (RNP1, RRM) Protein 3.

    Product # :

    PRO-1462

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    Description

    RBM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-157 a.a) and having a molecular mass of 19kDa. RBM3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RBM3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 5mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RBM3 belongs to the glycine-rich RNA-binding protein family and encodes a protein with one RNArecognition motif (RRM) domain. By cold shock and low oxygen tension the expression of this gene is induced. On chromosome 1 a pseudogene exists. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.Diseases associated with RBM3 include vaccinia, andcryptorchidism. GO annotations linked to this gene include RNA binding and ribosomal large subunit binding. An important paralog of this gene is RBMY1J.

    • Synonyms

      IS1-RNPL, RNPL, RNA-binding motif protein 3, Putative RNA-Binding Protein 3, RNA Binding Motif (RNP1, RRM) Protein 3.

    • 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 MGSMSSEEGK LFVGGLNFNT DEQALEDHFS SFGPISEVVV VKDRETQRSR GFGFITFTNP EHASVAMRAM NGESLDGRQI RVDHAGKSAR GTRGGGFGAH GRGRSYSRGG GDQGYGSGRY YDSRPGGYGY GYGRSRDYNG RNQGGYDRYS GGNYRDNYDN

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    Rbm3 Human
  • View Data Sheet

    Name :

    RCN2 Human

    Description:

    Reticulocalbin 2 Human Recombinant

    Reticulocalbin-2, Calcium-binding protein ERC-55, E6-binding protein, 6BP, RCN2, ERC55, E6BP, ERC-55, TCBP49.

    Product # :

    PRO-189

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    Description

    RCN2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (26-317 a.a.) and having a molecular mass of 36.8kDa (Molecular weight on SDS-PAGE will appear higher).RCN2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RCN2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Reticulocalbin-2 (RCN2) is a member of the CREC protein family. RCN2 is a calcium-binding protein found in the lumen of the ER. RCN2 contains 6 conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.

    • Synonyms

      Reticulocalbin-2, Calcium-binding protein ERC-55, E6-binding protein, 6BP, RCN2, ERC55, E6BP, ERC-55, TCBP49.

    • 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 MEELHYPLGE RRSDYDREAL LGVQEDVDEY VKLGHEEQQK RLQAIIKKID LDSDGFLTES ELSSWIQMSF KHYAMQEAKQ QFVEYDKNSD DTVTWDEYNI QMYDRVIDFD ENTALDDAEE ESFRKLHLKD KKRFEKANQD SGPGLSLEEF IAFEHPEEVD
      YMTEFVIQEA LEEHDKNGDG FVSLEEFLGD YRWDPTANED PEWILVEKDR FVNDYDKDND GRLDPQELLP WVVPNNQGIA QEEALHLIDE MDLNGDKKLS EEEILENPDL FLTSEATDYG RQLHDDYFYH DEL.

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    Rcn2 Human
  • View Data Sheet

    Name :

    REG4 Human

    Description:

    Regenerating Islet-Derived 4 Human Recombinant

    Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.

    Product # :

    PRO-424

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    Description

    The Recombinant Human REG-4 is manufactured with N-terminal fusion of His Tag. The Recombinant Human REG-IV His-Tagged Fusion Protein is 17.4 kDa protein containing 136 amino acid residues of the Human REG 4 and 12 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
      Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system.

    • Synonyms

      Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.

    • 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

      Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS HMDIIMRPSC APGWFYHKSN CYGYFRKLRN WSDAELECQS YGNGAHLASI LSLKEASTIA EYISGYQRSQ PIWIGLHDPQ KRQQWQWIDG AMYLYRSWSG KSMGGNKHCA EMSSNNNFLT WSSNECNKRQ HFLCKYRP.

    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.

    Reg4 Human
  • View Data Sheet

    Name :

    ZFAND1 Human

    Description:

    Zinc Finger, AN1-Type Domain 1 Human Recombinant

    AN1-type zinc finger protein 1, ZFAND1, Zinc finger AN1-type domain 1.

    Product # :

    PRO-1564

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    Description

    ZFAND1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 291 amino acids (1-268 a.a) and having a molecular mass of 33.2kDa.ZFAND1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ZFAND1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AN1-type zinc finger protein 1 isoform a (ZFAND1) is a member of the Zinc-finger proteins. Proteins from this family contain DNA-binding domains and have an extensive variety of functions, most of which encompass some form of transcriptional activation or repression. ZFAND1 is a 268 amino acid protein, which contains two AN1-type zinc fingers that are repeatedly found in proteins which contain an ubiquitin-like domain and for that reason have a role in the ubiquitination pathway ZFAND1 is comprised of 6 conserved cysteines and 2 histidines and have a dimetal (zinc)-bound alpha/beta fold. As a result of alternative splicing events two isoforms of ZFAND1 are produced.

    • Synonyms

      AN1-type zinc finger protein 1, ZFAND1, Zinc finger AN1-type domain 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 MGSMAELDIG QHCQVEHCRQ RDFLPFVCDD CSGIFCLEHR SRESHGCPEV TVINERLKTD QHTSYPCSFK DCAERELVAV ICPYCEKNFC LRHRHQSDHE CEKLEIPKPR MAATQKLVKD IIDSKTGETA SKRWKGAKNS ETAAKVALMK LKMHADGDKS LPQTERIYFQ VFLPKGSKEK SKPMFFCHRW SIGKAIDFAA SLARLKNDNN KFTAKKLRLC HITSGEALPL DHTLETWIAK EDCPLYNGGN IILEYLNDEE QFCKNVESYL E.

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    Zfand1 Human
  • View Data Sheet

    Name :

    RPAIN Human

    Description:

    RPA Interacting Protein Human Recombinant

    HRIP, RIP, RPA-interacting protein, hRIP, RPAIN.

    Product # :

    PRO-1661

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    Description

    RPAIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106 a.a.) and having a molecular mass of 14.7kDa.RPAIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RPAIN protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RPA-interacting protein isoform d (RPAIN) is a single-stranded-DNA binding protein which participates in various eukaryotic DNA processes such as replication, repair and recombination. RPAIN interacting protein has been indicated as an adapter protein that is involved in RPA nuclear import instead of the prototypical importin proteins that normally mediate nuclear import. RPAIN is mainly expressed in pancreas, kidney, muscle, liver, lung, placenta, brain, heart, leukocytes, colon, intestine, ovary, testis, prostate, thymus and spleen.

    • Synonyms

      HRIP, RIP, RPA-interacting protein, hRIP, RPAIN.

    • 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 MGSMAESLRS PRRSLYKLVG SPPWKEAFRQ RCLERMRNSR DRLLNRYRQA GSSGPGNSQN SFLVQEVMEE EWNALQSVEN CPEDLAQLEE LIDMAVLEEI QQELINQGL.

    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.

    Rpain Human
  • View Data Sheet

    Name :

    SERPING1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant

    C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    Product # :

    PRO-1401

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    Description

    SERPING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 499 amino acids (23-500a.a) and having a molecular mass of 55.1kDa. SERPING1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SERPING1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    • 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 MNPNATSSSS QDPESLQDRG EGKVATTVIS KMLFVEPILE VSSLPTTNST TNSATKITAN TTDEPTTQPT TEPTTQPTIQ PTQPTTQLPT DSPTQPTTGS FCPGPVTLCS DLESHSTEAV LGDALVDFSL KLYHAFSAMK KVETNMAFSP FSIASLLTQV LLGAGENTKT NLESILSYPK DFTCVHQALK GFTTKGVTSV SQIFHSPDLA IRDTFVNASR TLYSSSPRVL SNNSDANLEL INTWVAKNTN NKISRLLDSL PSDTRLVLLN AIYLSAKWKT TFDPKKTRME PFHFKNSVIK VPMMNSKKYP VAHFIDQTLK AKVGQLQLSH NLSLVILVPQ NLKHRLEDME QALSPSVFKA IMEKLEMSKF QPTLLTLPRI KVTTSQDMLS IMEKLEFFDF SYDLNLCGLT EDPDLQVSAM QHQTVLELTE TGVEAAAASA ISVARTLLVF EVQQPFLFVL WDQQHKFPVF MGRVYDPRA.

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    Serping1 Human
  • View Data Sheet

    Name :

    SCF Mouse

    Description:

    Stem Cell Factor Mouse Recombinant

    Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.

    Product # :

    CYT-275

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    Description

    Stem Cell Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18309 Dalton. The SCF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of Human TF-1 cell line is < 10 ng/ml, corresponding to a Specific Activity of 1x105 IU/mg.

    More Info

    • Introduction

      Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
      SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).

    • Synonyms

      Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MKEICGNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV IQLSLSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVLC MEENAPKNIK ESPKRPETRS FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.52 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 Stem Cell Factor as a Reference Standard.

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    Scf Mouse
  • View Data Sheet

    Name :

    Myostatin Human, HEK

    Description:

    Myostatin Human Recombinant, HEK

    GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    Product # :

    CYT-833

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    Description

    Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Ser375) containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.

    Source

    HEK 293.

    Formulation

    Myostatin solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.

    • Synonyms

      GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

    • Physical Appearance

      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

      HHHHHHASNE NSEQKENVEK EGLCNACTWR QNTKSSRIEA IKIQILSKLR LETAPNISKD VIRQLLPKAP PLRELIDQYD VQRDDSSDGS LEDDDYHATT ETIITMPTES DFLMQVDGKP KCCFFKFSSK IQYNKVVKAQ LWIYLRPVET PTTVFVQILR LIKPMKDGTR YTGIRSLKLD MNPGTGIWQS IDVKTVLQNW LKQPESNLGI EIKALDENGH DLAVTFPGPG EDGLNPFLEV KVTDTPKRSR RDFGLDCDEH STESRCCRYP LTVDFEAFGW DWIIAPKRYK ANYCSGECEF VFLQKYPHTH LVHQANPRGS AGPCCTPTKM SPINMLYFNG KEQIIYGKIP AMVVDRCGCS.

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    Myostatin Human Hek
  • View Data Sheet

    Name :

    GDNF Human

    Description:

    Glial-Derived Neurotrophic Factor Human Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-305

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    • sds-page

    Description

    Glial derived Neurotrophic Factor Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 x 135 amino acids and having a total molecular mass of approximately 30kDa. GDNF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.

    sds-page

    GDNF sds-page - Product image 1

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of minergic neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of minergic neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.

    • Background

      What is the molecular weight/Mw of GDNF HUMAN Protein?
      GDNF HUMAN Protein has a total Mw of 30kDa.

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

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

      What is the Biological Activity of GDNF HUMAN Protein?
      The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.

      What is the amino acid sequence of GDNF HUMAN Protein?
      SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
      What applications can GDNF HUMAN Protein be used in?
      GDNF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDNF HUMAN Protein?
      The endotoxin level is minimal, GDNF HUMAN 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.

    Gdnf Human
  • View Data Sheet

    Name :

    Troponin-C Protein

    Description:

    Cardiac Troponin-C Human

    Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.

    Product # :

    PRO-2571

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    Description

    Troponin-C Human produced from Human Cardiac Tissue, having a molecular mass of 18kDa. The Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.

    Source

    Human cardiac tissue

    Formulation

    The protein solution contains 150 mM NaCl, 10 mM sodium phosphate and 0.05% NaN3, (pH 7.0).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.

    • Synonyms

      Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

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    Cardiac Troponin C
  • View Data Sheet

    Name :

    Leptin qA Mouse, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Mouse Recombinant

    Product # :

    CYT-1244

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    Description

    Leptin Antagonist Quadruple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin Quadruple anatagonist Pegylated runs as a 55 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Mouse Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.  Pegylated recombinant mouse leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super mouse leptin antagonist but in vivo it has profound weight gain effect, resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin produced mainly by adipocytes. Leptin mostly regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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    Leptin Mouse Ta Peg
  • View Data Sheet

    Name :

    Thymosin beta 4

    Description:

    Thymosin β4

    Thymosin beta-4. TB500, TB-500

    Product # :

    HOR-275

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    Description

    Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.

    • Synonyms

      Thymosin beta-4. TB500, TB-500

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.

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    Thymosin Beta 4
  • View Data Sheet

    Name :

    ESM1 Human, SF9

    Description:

    Endothelial Cell-Specific Molecule 1 Human Recombinant, Sf9

    Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.

    Product # :

    PRO-2588

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    Description

    ESM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 174 amino acids (20-184a.a.) and having a molecular mass of 19.2kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). ESM1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ESM1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ESM1, also knows as, Endothelial cell-specific molecule 1 is a protein encoded by a gene called ESM1 in humans. ESM1 is a secreted protein that is highly expressed in human kidney and lung tissues (in the endothelial cells). There are suggestions regarding the protein’s involvement in endothelium-dependent pathological diseases, due to his regulation that is performed by cytokines.

    • Synonyms

      Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.

    • 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

      ADLWSNNYAV DCPQHCDSSE CKSSPRCKRT VLDDCGCCRV CAAGRGETCY RTVSGMDGMK CGPGLRCQPS NGEDPFGEEF GICKDCPYGT FGMDCRETCN CQSGICDRGT GKCLKFPFFQ YSVTKSSNRF VSLTEHDMAS GDGNIVREEV VKENAAGSPV MRKWLNPRHH HHHH.

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    Esm1 Antigen
  • View Data Sheet

    Name :

    iL22RA (Y51A) Mouse, PEG

    Description:

    Interleukin-22 Receptor Antagonist (Y51A), PEG Mouse Recombinant

    Product # :

    CYT-1248

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    Description

    Interleukin 22 Y51A mutan Mouse Recombinant is a single non-glycosilated polypeptide chain containing 147 amino acids and additional Ala at N-terminus. The iL22RA is bound to 20 kDa PEG molecule at N-terminus, resulting in 36.0 kDa. The Mouse iL22RA (Y51A) Pegylated runs as a 50 kDa due to enlarged hydrodymanic volume. iL22RA Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse iL22RA (Y51A) was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Mouse iL22RA inhibits mouse IL-22 induced STAT3 phosphorylation in HepG cells. Its inhibitory acrtivity in vitro is ~ 10-20% compared to the non-pegylated mIL22 (Y51A) mutant.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized iL22RA (Y51A) Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization iL22RA mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized iL22RA (Y51A) Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      IL-22 is a part of the IL-10 family of regulatory cytokines and produced by several populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 takes effect on non-hematopoietic cells. IL-22 takes part in wound healing and in protection against microbs. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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    Il22Ra Mouse Peg
  • View Data Sheet

    Name :

    TNIP1 Human

    Description:

    TNFAIP3 Interacting Protein 1 Human Recombinant

    TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.

    Product # :

    PRO-005

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    Description

    TNIP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 458 amino acids (94-530 a.a.) and having a molecular mass of 51.8kDa. The TNIP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TNIP1 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol, 5mM DTT and 200mM NaCl.

    Purity

    Greater than 75.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFAIP3-interacting protein 1 (TNIP1) interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with a RIP- or TRAF2-mediated transactivation signal. Furthermore, TNIP1 interacts with HIV-1 matrix protein and is packaged into virions and its overexpression can inhibit viral replication. TNIP1 can regulate matrix nuclear localization, both nuclear import of Preintegration complex (PIC) and export of GAG polyprotein and viral genomic RNA during virion production.

    • Synonyms

      TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-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 MSNVTASPTA PACPSDKPAP VQKPPSSGTS SEFEVVTPEE QNSPESSSHA NAMALGPLPR EDGNLMLHLQ RLETTLSVCA EEPDHGQLFT HLGRMALEFN RLASKVHKNE QRTSILQTLC EQLRKENEAL KAKLDKGLEQ RDQAAERLRE ENLELKKLLM SNGNKEGASG RPGSPKMEGT GKKAVAGQQQ ASVTAGKVPE VVALGAAEKK VKMLEQQRSE LLEVNKQWDQ HFRSMKQQYE QKITELRQKL ADLQKQVTDL EAEREQKQRD FDRKLLLAKS KIEMEETDKE QLTAEAKELR QKVKYLQDQL SPLTRQREYQ EKEIQRLNKA LEEALSIQTP PSSPPTAFGS PEGAGALLRK QELVTQNELL KQQVKIFEED FQRERSDRER MNEEKEELKK QVEKLQAQVT LSNAQLKAFK DEEKAREALR QQKRKAKA.

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    Tnip1 Human
  • View Data Sheet

    Name :

    USE1 Human

    Description:

    Unconventional SNARE In The ER 1 Human Recombinant

    Vesicle transport protein USE1, Putative MAPK-activating protein PM26, USE1-like protein, p31, USE1L, MDS032, Q-SNARE, SLT1, SNARE-Like Tail-Anchored Protein 1 Homolog, Protein P31.

    Product # :

    PRO-1464

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    Description

    USE1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 254 amino acids (1-231 a.a) and having a molecular mass of 28.3kDa.USE1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    USE1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      USE1 Belongs to the USE1 family, this protein is a vesicle transport protein. USE1 is a component of a SNAREcomplex consisting of STX18, USE1L, BNIP1/SEC20L and SEC22B. In addition USE1 interacts directly with STX18. SNARE maybe involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. Diseases associated with USE1 comprise dysentery and hemolytic-uremic syndrome. Among its related super-pathways are Nicotine Pathway (Dopaminergic Neuron) and Pharmacodynamics. GO annotations related to this gene include protein binding.

    • Synonyms

      Vesicle transport protein USE1, Putative MAPK-activating protein PM26, USE1-like protein, p31, USE1L, MDS032, Q-SNARE, SLT1, SNARE-Like Tail-Anchored Protein 1 Homolog, Protein P31.

    • 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 MGSMAASRLE LNLVRLLSRC EAMAAEKRDP DEWRLEKYVG ALEDMLQALK VHASKPASEV INEYSWKVDF LKGMLQAEKL TSSSEKALAN QFLAPGRVPT TARERVPATK TVHLQSRARY TSEMRSELLG TDSAEPEMDV RKRTGVAGSQ PVSEKQSAAE LDLVLQRHQN LQEKLAEEML GLARSLKTNT LAAQSVIKKD NQTLSHSLKM ADQNLEKLKT ESERLEQHTQ KSVN

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    Use1 Human
  • View Data Sheet

    Name :

    MAPK11 Human

    Description:

    Mitogen-Activated Protein Kinase 11 Human Recombinant

    Mitogen-activated protein kinase 11, PRKM11, SAPK2, p38-2, p38Beta, Mitogen-activated protein kinase p38 beta, Stress-activated protein kinase 2b, SAPK2B, MAP kinase 11, MAP kinase p38 beta, MAPK 11, P38BETA2, mitogen-activated protein kinase p38-2, EC 2.7.11, EC 2.7.11.24.

    Product # :

    PKA-013

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    Description

    MAPK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-364 a.a.) and having a molecular mass of 43.8kDa.MAPK11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAPK11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 2mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE analysis.

    More Info

    • Introduction

      MAPK11 belongs to the MAP kinase family and is most associated with p38 MAP kinases (MAPKs). MAPKs are activated mainly as a reaction to cellular stress and inflammatory cytokines, and inhibitors that target the MAPK14 and MAPK11 have demonstrated ability to cure inflammatory disease. MAPK11 cooperates with HDAC3 and Promyelocytic leukemia protein and takes part in a signal transduction pathway which is activated by alterations in the osmolarity of the extracellular environment, by environmental stress, or by cytokines.

    • Synonyms

      Mitogen-activated protein kinase 11, PRKM11, SAPK2, p38-2, p38Beta, Mitogen-activated protein kinase p38 beta, Stress-activated protein kinase 2b, SAPK2B, MAP kinase 11, MAP kinase p38 beta, MAPK 11, P38BETA2, mitogen-activated protein kinase p38-2, EC 2.7.11, EC 2.7.11.24.

    • 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 MGSMSGPRAG FYRQELNKTV WEVPQRLQGL RPVGSGAYGS VCSAYDARLR QKVAVKKLSR PFQSLIHARR TYRELRLLKH LKHENVIGLL DVFTPATSIE DFSEVYLVTT LMGADLNNIV KCQALSDEHV QFLVYQLLRG LKYIHSAGII HRDLKPSNVA VNEDCELRIL DFGLARQADE EMTGYVATRW YRAPEIMLNW MHYNQTVDIW SVGCIMAELL QGKALFPGSD YIDQLKRIME VVGTPSPEVL AKISSEHART YIQSLPPMPQ KDLSSIFRGA NPLAIDLLGR MLVLDSDQRV SAAEALAHAY FSQYHDPEDE PEAEPYDESV EAKERTLEEW KELTYQEVLS FKPPEPPKPP GSLEIEQ.

    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.

    Mapk11 Human
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