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Search results

1000 results found for “Myostatin”

Name

Description

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  • View Data Sheet

    Name :

    MEK1 Human

    Description:

    Mitogen Activated Kinase Kinase 1 Human Recombinant

    Product # :

    PKA-256

    Price :

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    • More Info

    Description

    MAP2K1 active Human Recombinant produced in Sf9 cells is a glycosylated, polypeptide chain containing amino acids 2-393 having a molecular mass of 47 kDa. MAP2K1 is fused to a polyhistidine tag and is purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    MEK1 is supplied at a concentration of in 40mM Tris, pH-8, 0.15M NaCl, 0.27M sucrose, 1mM DTT, 0.2mM PMSF, 1mM benzamidine, 0.1mM sodium vanadate and 0.03% Brij-35.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    ~125-175 units/mg. One unit of MEK1 activity transfers 1 nmol of phosphate to ERK1/2 peptide per minute at 30°C in a reaction containing 100µM ATP.
    Recombinant active MEK1 also phosphorylates ERK1, ERK2, and GSK-3?. Kinase activity may vary depending on the substrate and reaction conditions.
    The optimal concentration should be determined for each specific application.

    More Info

    • Introduction

      MAP2K1 is a member of the dual specificity protein kinase family, which plays a role as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, are recognized as extracellular signal-regulated kinases (ERKs), that act as an integration position for multiple biochemical signals. MEK1 is located upstream of MAP kinases and stimulates the enzymatic activity of MAP kinases upon wide variety of extra- and intracellular signals. As a key player of MAP kinase signal transduction pathway, MEK1 is involved in many cellular processes such as proliferation, differentiation, transcription regulation and development. MAP2K1 catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a thr-glu-tyr sequence located in map kinases. MEK1 activates erk1 and erk2 map kinases.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 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.

    Mek1 Human
  • View Data Sheet

    Name :

    PHPT1 Human

    Description:

    Phosphohistidine Phosphatase 1 Human Recombinant

    PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    Product # :

    ENZ-012

    Price :

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    Description

    PHPT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-125a.a.) and having a molecular mass of 15.9kDa.PHPT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHPT1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0) 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.

    • Synonyms

      PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    • 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 MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW ANDGY

    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.

    Phpt1 Human
  • View Data Sheet

    Name :

    AMBP

    Description:

    Alpha-1 Microglobulin Human Recombinant

    Alpha-1-microglobulin/bikunin precursor, HCP, ITIL, ITI, EDC1, HI30, IATIL, ITILC, UTI, A1M, bikunin, complex-forming glycoprotein heterogeneous in charge, growth-inhibiting protein 19, inter-alpha-trypsin inhibitor light chain, protein AMBP, protein HC, trypstatin, uristatin, uronic-acid-rich protein.

    Product # :

    PRO-957

    Price :

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    Description

    AMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (20-203) and having a molecular mass of 23.1 kDa.AMBP is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The AMBP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species.
      A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore.
      Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin.
      Alpha-1-microglobulin was first discovered in pathological human urine.
      It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.

    • Synonyms

      Alpha-1-microglobulin/bikunin precursor, HCP, ITIL, ITI, EDC1, HI30, IATIL, ITILC, UTI, A1M, bikunin, complex-forming glycoprotein heterogeneous in charge, growth-inhibiting protein 19, inter-alpha-trypsin inhibitor light chain, protein AMBP, protein HC, trypstatin, uristatin,
      uronic-acid-rich 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 MGPVPTPPDN IQVQENFNIS RIYGKWYNLA IGSTCPWLKK IMDRMTVSTL VLGEGATEAE ISMTSTRWRK GVCEETSGAY EKTDTDGKFL YHKSKWNITM ESYVVHTNYD EYAIFLTKKF SRHHGPTITA KLYGRAPQLR ETLLQDFRVV AQGVGIPEDS IFTMADRGEC VPGEQEPEPI LIPRV.

    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.

    Ambp Human
  • View Data Sheet

    Name :

    GDF15 Mouse

    Description:

    Growth and Differentiation factor 15 Mouse Recombinant

    Growth/differentiation factor 15, GDF-15.

    Product # :

    CYT-857

    Price :

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    • sds-page

    Description

    GDF15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (189-303 a.a) and having a molecular mass of 14.9kDa. GDF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF15 protein solution (1.0mg/ml) containing 20mM Phosphate buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    GDF15 Mouse - Product image 1

    More Info

    • Introduction

      GDF15 is part of the TGF-Beta superfamily which is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

    • Synonyms

      Growth/differentiation factor 15, GDF-15.

    • 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 MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.

    • Background

      What is the molecular weight/Mw of GDF15 MOUSE Protein?
      GDF15 MOUSE Protein has a total Mw of 14.9kDa.

      What is the source or expression system of GDF15 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GDF15 MOUSE Protein?
      GDF15 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 MOUSE Protein?
      The biological functionality of GDF15 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of GDF15 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.

      What applications can GDF15 MOUSE Protein be used in?
      GDF15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF15 MOUSE Protein?
      The endotoxin level is minimal, GDF15 MOUSE Protein was purified using conventional chromatography techniques.

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

    Gdf15 Mouse
  • View Data Sheet

    Name :

    TPM4 Human

    Description:

    Tropomyosin-4 Human Recombinant

    Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4.

    Product # :

    PRO-187

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    Description

    TPM4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 268 amino acids (1-248 a.a.) and having a molecular mass of 30.7kDa.TPM4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPM4 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TPM4 is a member of the tropomyosin family. Tropomyosins exist in practically all eukaryotic cells (both muscle and nonmuscle), where they bind actin filaments and function to modulate actin-myosin interaction and stabilize actin filament structure. TPM4 binds to actin filaments in muscle and nonmuscle cells and plays a central role, in connection with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction.

    • Synonyms

      Tropomyosin alpha-4 chain, TM30p1, Tropomyosin-4, TPM4.

    • 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 MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI.

    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.

    Tpm4 Human
  • View Data Sheet

    Name :

    Leptin qA Human, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Human Recombinant

    Product # :

    CYT-1251

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    Description

    Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/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

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

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist 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 Human Leptin Pegylated Quadruple Antagonist 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

      Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 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).

    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.

    Leptin Human Qa Peg
  • View Data Sheet

    Name :

    CRYAB Mouse

    Description:

    Crystallin Alpha B Mouse Recombinant

    CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    Product # :

    HSP-018

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    Description

    Recombinant CRYAB Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20 kDa. Mouse CRYAB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse CRYAB protein solution contains 20mM Tris-HCl buffer pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.

    • Synonyms

      CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    • 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

      MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVA AAPKK.

    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.

    Cryab Mouse
  • View Data Sheet

    Name :

    TOMM20 Human

    Description:

    Translocase Of Outer Mitochondrial Membrane 20 Human Recombinant

    Mmitochondrial import receptor subunit TOM20 homolog, TOMM20, MAS20, MOM19, KIAA0016, Outer mitochondrial membrane receptor Tom20, Mitochondrial 20 kDa outer membrane protein.

    Product # :

    PRO-1471

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    Description

    TOMM20 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (25-145) and having a molecular mass of 16.2 kDa. TOMM20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TOMM20 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mmitochondrial import receptor subunit TOMM20 homolog (TOMM20) is a member of the Tom20 family. The Tom machinery consists of import receptors for the initial binding of cytosolically synthesized preproteins and a general import pore (GIP) for the membrane translocation of various preproteins into the mitochondria. TOMM20 acts as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.

    • Synonyms

      Mmitochondrial import receptor subunit TOM20 homolog, TOMM20, MAS20, MOM19, KIAA0016, Outer mitochondrial membrane receptor Tom20, Mitochondrial 20 kDa outer membrane 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 MGSDRKRRSD PNFKNRLRER RKKQKLAKER AGLSKLPDLK DAEAVQKFFL EEIQLGEELL AQGEYEKGVD HLTNAIAVCG QPQQLLQVLQ QTLPPPVFQM LLTKLPTISQ RIVSAQSLAE DDVE.

    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.

    Tomm20 Human
  • View Data Sheet

    Name :

    TOMM34 Human

    Description:

    Translocase Of Outer Mitochondrial Membrane 34 Human Recombinant

    HTOM34P, TOM34, URCC3, Mitochondrial import, TOMM34 receptor subunit TOM34, hTom34, Translocase of outer membrane 34 kDa subunit.

    Product # :

    PRO-1501

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    Description

    TOMM34 Human Recombinant produced in E. coli is a single polypeptide chain containing 332 amino acids (1-309) and having a molecular mass of 36.9kDa. TOMM34 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TOMM34 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Translocase of Outer Mitochondrial Membrane 34 (TOMM34) which is found in the cytoplasm and sometimes associated with the outer mitochondrial membrane is involved in the import of precursor proteins into mitochondria. TOMM34 has a chaperone-like activity, binding the mature portion of unfolded proteins and aiding their import into mitochondria. TOMM34 has a weak ATPase activity and contains 6 TPR repeats.

    • Synonyms

      HTOM34P, TOM34, URCC3, Mitochondrial import, TOMM34 receptor subunit TOM34, hTom34, Translocase of outer membrane 34 kDa subunit.

    • 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 MGSMAPKFPD SVEELRAAGN ESFRNGQYAE ASALYGRALR VLQAQGSSDP EEESVLYSNR AACHLKDGNC RDCIKDCTSA LALVPFSIKP LLRRASAYEA LEKYPMAYVD YKTVLQIDDN VTSAVEGINR MTRALMDSLG PEWRLKLPSI PLVPVSAQKR WNSLPSENHK EMAKSKSKET TATKNRVPSA GDVEKARVLK EEGNELVKKG NHKKAIEKYS ESLLCSNLES ATYSNRALCY LVLKQYTEAV KDCTEALKLD GKNVKAFYRR AQAHKALKDY KSSFADISNL LQIEPRNGPA QKLRQEVKQN LH.

    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.

    Tomm34 Human
  • View Data Sheet

    Name :

    MCTS1 Human

    Description:

    Malignant T-Cell-Amplified Sequence 1 Human Recombinant

    MCT-1, MCT1, Malignant T-cell-amplified sequence 1, Multiple copies T-cell malignancies.

    Product # :

    PRO-1387

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    Description

    MCTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 204 amino acids (1-181 a.a.) and having a molecular mass of 22.9kDa. MCTF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    MCTF1 protein solution (0.5mg/ml) contains 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

      Malignant T cell amplified sequence 1 (MCTS1) is an Anti-oncogene which takes part in cell cycle regulation by means of decreasing cell doubling time and encouraging-dependent growth and also by shorting the duration of G1 transit time and G1/S transition. MCTS1 also plays a role as translation enhancer. MCTS1 recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, thereupon altering the mRNA translation profile; Up-regulates protein levels of BCL2L2, TFDP1, MRE11A, CCND1 and E2F1, while mRNA levels remains constant.

    • Synonyms

      MCT-1, MCT1, Malignant T-cell-amplified sequence 1, Multiple copies T-cell malignancies.

    • 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 MGSMFKKFDE KENVSNCIQL KTSVIKGIKN QLIEQFPGIE PWLNQIMPKK DPVKIVRCHE HIEILTVNGE LLFFRQREGP FYPTLRLLHK YPFILPHQQV DKGAIKFVLS GANIMCPGLT SPGAKLYPAA VDTIVAIMAE GKQHALCVGV MKMSAEDIEK VNKGIGIENI HYLNDGLWHM KTYK.

    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.

    Mcts1 Human
  • View Data Sheet

    Name :

    CST4 Human

    Description:

    Cystatin 4 Human Recombinant

    Cystatin-SA-III, Cystatin-4, cystatin S, Salivary acidic protein 1.

    Product # :

    PRO-1097

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    Description

    CST4 Human Recombinant produced in E. coli is a single polypeptide chain containing 145 amino acids (21-141) and having a molecular mass of 16.8kDa.CST4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CST4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CST4 is a member of the cystatin superfamily which contains proteins that hold multiple cystatin-like sequences. Several family members are active cysteine protease inhibitors, whereas others have lost or possibly never attained this inhibitory activity. CST4 strongly inhibits papain (non-competitively) and ficin, partially inhibits stem bromelain and bovine cathepsin C, however does not inhibit porcine cathepsin B or clostripain.

    • Synonyms

      Cystatin-SA-III, Cystatin-4, cystatin S, Salivary acidic protein 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSSSKEE NRIIPGGIYD ADLNDEWVQR ALHFAISEYN KATEDEYYRR PLQVLRAREQ TFGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WEDRMSLVNS RCQEA

    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.

    Cst4 Human
  • View Data Sheet

    Name :

    BD 1 Mouse

    Description:

    BD 1 Mouse

    Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

    Product # :

    CYT-044

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    Description

    BD 1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 37 amino acids and having a molecular mass of 4.1 KDa.The BD 1 Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

    Purity

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

    Biological Activity

    Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml, corresponding to a specific activity of 1,000-10,000units/mg.

    More Info

    • Introduction

      The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
      Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
      Beta Defensin is highly expressed by epithelial cells.
      Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.

    • Synonyms

      Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse BD 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD 1 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 Mouse BD-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DQYKCLQHGG FCLRSSCPSN TKLQGTCKPD KPNCCKS.

    • Background

      What is the molecular weight/Mw of BD1 Protein?
      BD1 Protein has a total Mw of 4.1kDa.

      What is the source or expression system of BD1 Protein?
      Escherichia Coli.

      What is the Purity of BD1 Protein?
      BD1 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD1 Protein?
      Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml, corresponding to a specific activity of 1,000-10,000units/mg.

      What is the amino acid sequence of BD1 Protein?
      DQYKCLQHGG FCLRSSCPSN TKLQGTCKPD KPNCCKS.

      What applications can BD1 Protein be used in?
      BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD1 Protein?
      The endotoxin level is minimal, BD1 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.

    Bd 1 Mouse
  • View Data Sheet

    Name :

    CKMT3 Human

    Description:

    Creatine Kinase Muscle Type-3 Human Recombinant

    Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.

    Product # :

    CKI-272

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    • More Info

    Description

    CKMT3 Human Recombinant produced in Pichia Pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to MM Isoenzyme in ELISA.The CKMT3 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Each mg of protein contains 20mM Tris pH-8, 1mM EDTA and 1mM DTT.

    Purity

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

    Biological Activity

    The biological activity measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 500 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 2,000ng/ml.

    More Info

    • Introduction

      The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

    • Synonyms

      Creatine kinase M-type, EC 2.7.3.2, Creatine kinase M chain, M-CK, CKM, CKMM, CKMMITIII.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. Please prevent 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.

    Ckmmitiii Human
  • View Data Sheet

    Name :

    TNNI1 Paired Antibody

    Description:

    Mouse Anti Human Troponin I Type 1 Paired

    DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.

    Product # :

    ANT-724

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    Description

    TNNI1 conjugation antibody and TNNI1 coating antibody are used to develop rapid test for TNNI1 rapid test.

    Please note that when ordering for example: 100µg antibody we ship 50µg from each of the antibodies (100µg in total).

    Formulation

    * TNNI1 conjugation in 50mM Na-citrate, pH 6.0, 0.9% NaCl and 0.095 % NaN3.

    * TNNI1 coating antibody in 50mM Na-citrate, pH 6.0 0.9% NaCl and 0.095 % NaN3.

    Purity

    Greater than 95%.

    More Info

    • Introduction

      Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.

    • Synonyms

      DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.

    • Physical Appearance

      2 vials of sterile Filtered clear colorless solution.

    • Applications

      Lateral flow immunoassay.

    • Type

      Mouse Anti Human Monoclonal.

    • Purification Method

      Purified monoclonal IgG by protein A chromatography.

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

    Tnni1 Paired Antibody
  • View Data Sheet

    Name :

    Collagen-I Goat

    Description:

    Goat Collagen-I

    Product # :

    PRO-2682

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    Description

    Goat Collagen-I is a natural protein purified from Goat tissues. Collagen-I is purified by proprietary chromatographic techniques.

    Source

    Goat tissues.

    Formulation

    Collagen-I was lyophilized without additives.

    Purity

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

    More Info

    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Collagen-I although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-I 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 Add 0.5 M acetic acid, pH 2.5 to prepare a working stock solution not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Collagen I Goat
  • View Data Sheet

    Name :

    Atosiban

    Description:

    Atosiban

    Product # :

    HOR-239

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    • HPLC, MS

    Description

    Atosiban also called ADH (Anti-Diuretic Hormone) has a molecular formula of C43H67N11O12S2, 3-Mercaptopropionyl-D-Tyr(ET)-Ile-Thr-Asn-Cys-Pro-Orn-Gly-NH2 having a Mw of 994.2 Dalton.

    Formulation

    The Atosiban peptide was lyophilized with no additives.

    Purity

    Greater than 98.0% as determined by analysis by RP-HPLC.

    HPLC, MS

    atosiban hplc - Product image 1
    atosiban hplc - Product image 2

    More Info

    • Introduction

      Atosiban is the first oxytocin antagonist to be specifically developed for the treatment of preterm labor. Atosiban has a specific mode of action, inhibiting oxytocin-induced uterine contractions by blocking oxytocin receptors in the uterus. Extensive clinical investigations have shown Atosiban to be at least as effective as current tocolytic agents. In addition, due to its novel and specific mode of action, Atosiban has a markedly improved maternal side effects profile compared with conventional therapies.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    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.

    Atosiban
  • View Data Sheet

    Name :

    Leptin Receptor Chicken

    Description:

    Leptin Receptor Chicken Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    Product # :

    CYT-509

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    Description

    Leptin Binding Domain Chicken Recombinant also called Leptin Receptor produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 208 amino acids and having a molecular mass of 24.5 kDa. Chicken Leptin Receptor consists of the cytokine binding domain of leptin receptor amino acids 420-626 of chicken leptin receptor.The Leptin Binding Domain is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was filter sterilized and stored at 4°C (0.2 to 0.5 mg/ml) solution of Tris-HCl buffer, pH 9.0 with 150mM NaCl.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Leptin Receptor is a part of the gp130 family of cytokine receptors that stimulate gene transcription by activating cytosolic STAT proteins. Leptin Receptor plays a role in the regulation of fat metabolism and in novel hematopoietic pathway that is obligatory for normal lymphopoiesis. Leptin Receptorparticipates in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus.Leptin Receptoraffectsspecifically on T lymphocyte responses.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor, Leptin Receptor.

    • Physical Appearance

      Sterile Filtered colorless solution at a concentration of 0.4 mg/ml.

    • Stability

      Sterile solutions at 0.5mg/ml or less are stable at 4°C for several months.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Ile-Asp-Val-Asn-Ile Biological ActivityBiological Activity is evidenced by high affinity binding of mammalian leptins at 1:1 molar ratio.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 2.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of Leptin Binding Domain as a Reference Standard.

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

    Leptin Receptor Chicken
  • 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.

    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.

    Actin
  • View Data Sheet

    Name :

    OSTF1 Human

    Description:

    Osteoclast Stimulating Factor-1 Human Recombinant

    SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

    Product # :

    CYT-630

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    Description

    OSTF1 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 225 amino acids (1-217) and having a molecular mass of 25.1kDa. The OSTF1 is fused to an 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSTF1 protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH 8, 0.5mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.

    • Synonyms

      SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MSKPPPKPVK PGEGGQVKVF RALYTFEPRT PDELYFEEGD IIYITDMSDT NWWKGTSKGR TGLIPSNYVA EQAESIDNPL HEAAKRGNLS WLRECLDNRV GVNGLDKAGS TALYWACHGG HKDIVEMLFT QPNIELNQQN KLGDTALHAA AWKGYADIVQ LFLAKGARTD LRNIEKKLAF DMATNAACAS LLKKKQGTDA VRTLSNAEDY LDDEDSDLEH HHHHH.

    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.

    Ostf1 Human
  • View Data Sheet

    Name :

    Activin-A Human Active

    Description:

    Activin-A Human Recombinant, Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-145

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    Description

    Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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

      Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential

      Introduction:

      Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.

      Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.

      Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.

      Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.

      The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.

      In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

    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.

    Inhba Human
  • View Data Sheet

    Name :

    MRM1 Human

    Description:

    Mitochondrial RRNA Methyltransferase 1 Human Recombinant

    Mitochondrial rRNA methyltransferase 1 homolog, rRNA methyltransferase 1, mitochondrial, Mitochondrial large ribosomal RNA ribose methylase, MRM1.

    Product # :

    PRO-1416

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    • More Info

    Description

    MRM1 Human Recombinant produced in E. coli is a single polypeptide chain containing 356 amino acids (21-353) and having a molecular mass of 38.8kDa. MRM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MRM1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial rRNA methyltransferase 1 homolog (MRM1) is a part of the RNA methyltransferase TrmH family. MRM1 methylates the ribose of guanosine G-2270 in the peptidyl transferase center of the mitochondrial large ribosomal RNA (21S).

    • Synonyms

      Mitochondrial rRNA methyltransferase 1 homolog, rRNA methyltransferase 1, mitochondrial, Mitochondrial large ribosomal RNA ribose methylase, MRM1.

    • 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 MGSSHAARHG ERPGGEELSR LLLDDLVPTS RLELLFGMTP CLLALQAARR SVARLLLQAG KAGLQGKRAE LLRMAEARDI PVLRPRRQKL DTMCRYQVHQ GVCMEVSPLR PRPWREAGEA SPGDDPQQLW LVLDGIQDPR NFGAVLRSAH FLGVDKVITS RRNSCPLTPV VSKSSAGAME VMDVFSTDDL TGFLQTKAQQ GWLVAGTVGC PSTEDPQSSE IPIMSCLEFL WERPTLLVLG NEGSGLSQEV QASCQLLLTI LPRRQLPPGL ESLNVSVAAG ILLHSICSQR KGFPTEGERR QLLQDPQEPS ARSEGLSMAQ HPGLSSGPEK ERQNEG.

    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.

    Mrm1 Human
  • View Data Sheet

    Name :

    Streptavidin, His

    Description:

    Streptavidin Recombinant, His Tag

    Product # :

    PRO-621

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    • More Info

    Description

    Recombinant Streptomyces Avidinii Streptavidin produced in E.Coli is a single, non-glycosylated polypeptide chain (25-183) containing a total of 167 amino acids and having a molecular mass of 17kDa. The Streptavidin protein is fused to an 8 aa N-terminal His-Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Streptavidin protein solution (1mg/ml) contains 20mM Tris-HCl pH7.5.

    Purity

    Greater than 95.0% as determined by analysis 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

      MVHHHHHHDP SKDSKAQVSA AEAGITGTWY NQLGSTFIVT AGADGALTGT YESAVGNAES RYVLTGRYDS APATDGSGTA LGWTVAWKNN YRNAHSATTW SGQYVGGAEA RINTQWLLTS GTTEANAWKS TLVGHDTFTK VKPSAASIDA AKKAGVNNGN PLDAVQQ.

    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 His
  • View Data Sheet

    Name :

    VAMP3 Human

    Description:

    Synaptobrevin-3 Human Recombinant

    VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    Product # :

    PRO-652

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    • More Info

    Description

    VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

    • Synonyms

      VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    • 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

      MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.

    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.

    Vamp3 Human
  • View Data Sheet

    Name :

    FGF 8 Mouse, 194 a.a.

    Description:

    Fibroblast Growth Factor-8 Mouse Recombinant, 194 a.a.

    FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

    Product # :

    CYT-840

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    • More Info

    Description

    FGF 8 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 5mM Na3PO4 and 50 mM NaCl, pH 7.5.

    Purity

    Greater than 97.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

    More Info

    • Introduction

      FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

    • Synonyms

      FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF 8 although stable at room temperature for 3 weeks, should be stored desiccated below -18?C. Upon reconstitution FGF 8 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 FGF 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

    • Background

      What is the molecular weight/Mw of FGF8 Protein?
      FGF8 Protein has a total Mw of 22.5kDa.

      What is the source or expression system of FGF8 Protein?
      Escherichia Coli.

      What is the Purity of FGF8 Protein?
      FGF8 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF8 Protein?
      The activity is determined by its ability to induce proliferation of mouse 3T3 cells and is typically less than 20ng/ml corresponding to a specific activity of 50,000units/mg.

      What is the amino acid sequence of FGF8 Protein?
      MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR

      What applications can FGF8 Protein be used in?
      FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF8 Protein?
      The endotoxin level is minimal, FGF8 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.

    Fgf 8 Mouse 194 Aa
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